OMPwiki - User contributions [en]

OMP ST:926 ! Escherichia coli K-12 JW5248

2016-06-20T19:14:52Z

165.91.108.55: Page creation by SpecialNewPage

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==Strain Summary==
<newTableEdit>
Template:Strain_info_table
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==Notes==

==Phenotype Annotation==
<newTableEdit>
Template:OMP_annotation_table
</newTableEdit>

==Additional Information==

==Links==

==References==
{{RefHelp}}<references/>

OMP ST:926 ! Escherichia coli K-12 JW5248

2016-06-20T19:14:52Z

165.91.108.55: touch

__TOC__

==Strain Summary==
<protect>

{| id="H576840ac474ca" class=" tableEdit Strain_info_table"

|-
!align=left align='left' bgcolor='#CCCCFF' |Strain Name
|-
!align=left align='left' bgcolor='#CCCCFF' |Synonyms
|-
!align=left align='left' bgcolor='#CCCCFF' |Taxon Information
|-
!align=left align='left' bgcolor='#CCCCFF' |Genotype
|-
!align=left align='left' bgcolor='#CCCCFF' |Strain Reference
|-
!align=left align='left' bgcolor='#CCCCFF' |Strain availability
|-
!align=left align='left' bgcolor='#CCCCFF' |Ancestry
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!align=left align='left' bgcolor='#CCCCFF' |Annotated phenotypes

|- class="tableEdit_footer"
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|}
<noinclude>

</noinclude>
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==Notes==

==Phenotype Annotation==
<protect>

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!|Annotation ID!!not!!OMP ID!!OMP term name!!Relative phenotype information!!Experimental condition!!ECO ID!!ECO term name!!Reference!!Annotation Extension!!Notes

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==Additional Information==

==Links==

==References==
{{RefHelp}}<references/>

OMP ST:926 ! Escherichia coli K-12 JW5248

2016-06-20T19:14:52Z

165.91.108.55: touch

__TOC__

==Strain Summary==
<protect>

{| id="H576840ac474ca" class=" tableEdit Strain_info_table"

|-
!align=left align='left' bgcolor='#CCCCFF' |Strain Name
||
Escherichia_coli_K-12_JW5248
|-
!align=left align='left' bgcolor='#CCCCFF' |Synonyms
||
BW25113 marR751(del)::kan, ECK1523
|-
!align=left align='left' bgcolor='#CCCCFF' |Taxon Information
||
*Pangenome:
|-
!align=left align='left' bgcolor='#CCCCFF' |Genotype
||
DE(araD-araB)567 DE(rhaD-rhaB)568 F- Lambda- hsdR514 lacZ4787(del)(::rrnB-3) rph-1
|-
!align=left align='left' bgcolor='#CCCCFF' |Strain Reference
||
PMID:16738554
|-
!align=left align='left' bgcolor='#CCCCFF' |Strain availability
||
[http://cgsc.biology.yale.edu/Strain.php?ID=109549 CGSC]
|-
!align=left align='left' bgcolor='#CCCCFF' |Ancestry
||
parent:OMP ST:800 ! Strain:Escherichia coli K-12 BW25113
|-
!align=left align='left' bgcolor='#CCCCFF' |Annotated phenotypes
||

|- class="tableEdit_footer"
|<div class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.7904.H576840ac474ca&page=7904&pagename={{FULLPAGENAMEE}}&type=1&template=Strain_info_table edit table]</div> ||
|}
<noinclude>
[[Category:OMP ST:800 ! Strain:Escherichia coli K-12 BW25113 derivatives]]
[[Category:Strains with genotype identical to parent]]
</noinclude>
</protect>

==Notes==

==Phenotype Annotation==
<protect>

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|- align='left' bgcolor='#CCCCFF'
!|Annotation ID!!not!!OMP ID!!OMP term name!!Relative phenotype information!!Experimental condition!!ECO ID!!ECO term name!!Reference!!Annotation Extension!!Notes

|- class="tableEdit_footer"
|<div class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.7904.F576840ac4e3e7&page=7904&pagename={{FULLPAGENAMEE}}&type=0&template=OMP_annotation_table edit table]</div> || || || || || || || || || ||
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<noinclude>

</noinclude>
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==Additional Information==

==Links==

==References==
{{RefHelp}}<references/>

PMID:790385

2015-07-17T18:39:48Z

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{| id="S55a94bf3964ce" class=" tableEdit PMID_info_table"

|-
!align=left align='left' bgcolor='#CCCCFF' |Citation
||
'''Silhavy, TJ, Casadaban, MJ, Shuman, HA and Beckwith, JR''' (1976) Conversion of beta-galactosidase to a membrane-bound state by gene fusion. ''Proc. Natl. Acad. Sci. U.S.A.'' '''73''':3423-7
|-
!align=left align='left' bgcolor='#CCCCFF' |Abstract
||
We have isolated a series of strains in which the lacZ gene has been fused to one of the maltose operons, such that the synthesis of beta-galactosidase (beta-D-galactoside galactohydrolase; EC 3.2.1.23) is inducible by maltose. The most frequent event that generates such fusions results in strains in which an intact lacZ gene has become a part of the malE,F operon. By using a special selection procedure, we have detected much rarer fusion events resulting in an altered beta-galactosidase molecule. In these strains, we presume that there is a hybrid protein molecule produced, comprised of an NH2-terminal amino acid sequence from a maltose transport protein (malF) and a COOH-terminal amino acid sequence from beta-galactosidase. The hybrid protein, which still retains some beta-galactosidase activity, is found in the cytoplasmic membrane. These results provide information on the component of the malF gene essential for incorporation of its product into the membrane.
|-
!align=left align='left' bgcolor='#CCCCFF' |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=790385 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC431127 PMC431127]

|-
!align=left align='left' bgcolor='#CCCCFF' |Keywords
||
Biological Transport; Cell Membrane/enzymology; Cytoplasm/enzymology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Galactosidases/metabolism; Genes; Genes, Regulator; Genetic Engineering; Maltose/metabolism; Operon

|- class="tableEdit_footer"
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|}
<noinclude>

</noinclude>


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="A55a94bf498f36" class=" tableEdit Phenotype_Table_2"
|- align='left' bgcolor='#CCCCFF'
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.6618.A55a94bf498f36&page=6618&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
<noinclude>

</noinclude>
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:790385

2015-07-17T18:39:47Z

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PMID on Demand placeholder

PMID:8913474

2012-11-30T23:29:04Z

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PMID:8913474

2012-11-30T23:29:04Z

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{| id="K50b9414023875" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Diarra, MS , Lavoie, MC , Jacques, M , Darwish, I , Dolence, EK , Dolence, JA , Ghosh, A , Ghosh, M , Miller, MJ and Malouin, F ''' (1996) Species selectivity of new siderophore-drug conjugates that use specific iron uptake for entry into bacteria. ''Antimicrob. Agents Chemother.'' '''40''':2610-7
|-
!align=left |Abstract
||
Siderophores selectively bind ferric iron and are involved in receptor-specific iron transport into bacteria. Several types of siderophores were synthesized, and growth-promoting or inhibitory activities when they were conjugated to carbacephalosporin, erythromycylamine, or nalidixic acid were investigated. Overall, 11 types of siderophores and 21 drug conjugates were tested against seven different bacterial species: Escherichia coli, Bordetella bronchiseptica, Pasteurella multocida, Pasteurella haemolytica, Streptococcus suis, Staphylococcus aureus, and Staphylococcus epidermidis. In some species, the inhibitory activities of the drug conjugates were associated with the ability of the bacteria to use the siderophore portion of the molecules for growth promotion in disc diffusion tests (0.04 mumol of conjugate or siderophore per disc). E. coli used catechol-based siderophore portions as well as hydroxamate-based tri-delta-OH-N-OH-delta-N-acetyl-L-ornithine ferric iron ligands for growth under iron-restricted conditions achieved by supplemental ethylenediamine di (O-hydroxyphenylacetic acid) (100 micrograms/ml) and was sensitive to carbacephalosporin conjugated to these siderophore types (up to a 34-mm-diameter inhibition zone). B. bronchiseptica used desferrioxamine B and an isocyanurate-based or trihydroxamate in addition to catechol-based siderophore portions for promotion but was not inhibited by beta-lactam conjugates partly because of the presence of beta-lactamase. P. multocida and P. haemolytica did not use any of the synthetic siderophores for growth promotion, and the inhibitory activities of some conjugates seemed partly linked to their ability to withhold iron from these bacteria, since individual siderophore portions showed some antibacterial effects. Individual siderophores did not promote S. suis growth in restrictive conditions, but the type of ferric iron ligands attached to beta-lactams affected inhibitory activities. The antibacterial activities of the intracellular-acting agents erythromycylamine and nalidixic acid were reduced or lost, even against S. aureus and S. epidermidis, when the agents were conjugated to siderophores. Conjugate-resistant E. coli mutants showed the absence of some iron-regulated outer membrane proteins in gel electrophoresis profiles and in specific phage or colicin sensitivity tests, implying that the drugs used outer membrane receptors of ferric complexes to get into cells.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8913474 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC163585 PMC163585]

|-
!align=left |Keywords
||
Animals; Anti-Bacterial Agents/chemistry; Anti-Bacterial Agents/metabolism; Bacteria/genetics; Bacteria/metabolism; Bacterial Outer Membrane Proteins/metabolism; Bordetella/genetics; Bordetella/growth & development; Bordetella/metabolism; Colicins/pharmacology; Drug Resistance, Microbial; Escherichia coli/drug effects; Escherichia coli/genetics; Hydroxamic Acids/pharmacology; Iron/metabolism; Microbial Sensitivity Tests; Mutation; Pasteurella/genetics; Pasteurella/growth & development; Pasteurella/metabolism; Siderophores/chemistry; Siderophores/metabolism; Streptococcus suis/genetics; Streptococcus suis/growth & development; Streptococcus suis/metabolism; Swine; Swine Diseases/microbiology

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3581.K50b9414023875&page=3581&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="D50b941403f1de" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3581.D50b941403f1de&page=3581&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:6997269

2012-10-22T18:16:03Z

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PMID:6997269

2012-10-22T18:16:03Z

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{| id="X50858d634b070" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Wandersman, C , Moreno, F and Schwartz, M ''' (1980) Pleiotropic mutations rendering Escherichia coli K-12 resistant to bacteriophage TP1. ''J. Bacteriol.'' '''143''':1374-83
|-
!align=left |Abstract
||
tpo mutations, located at 74 min on the genetic map, rendered Escherichia coli K-12 resistant to TP1, a phage which can use either the OmpF protein or the LamB protein as its receptor. tpo mutants synthesized decreased amounts of OmpF and LamB proteins but increased amounts of the OmpC product, another outer membrane protein. The effect of the tpo mutations in lam B gene expression was transcriptional. It is one facet of the following effect on the maltose regulon: strong decreases in the syntheses of the LamB protein and the periplasmic MalE protein occurred when the regulon was uninduced; a lesser decrease occurred in the syntheses of the LamB protein the MalE protein, and the cytoplasmic MalQ protein (amylomaltase) when the regulon was induced. The tpo mutants were found to be phenotypically identical to the perA mutant recently described by Wanner et al. (J. Bacteriol. 140:229--239, 1979) and to some of the ompB mutants described by Verhoef et al. (Mol. Gen. Genet. 169:137--146, 1979). Mapping and complementation analysis suggested that these three types of mutations belong to the same cistron. Our results bring to at least four the number of clearly distinct phenotypes which can result from mutations at, or close to, ompB, a locus which appears increasingly complex.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6997269 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC294516 PMC294516]

|-
!align=left |Keywords
||
Bacterial Proteins/genetics; Coliphages/growth & development; Escherichia coli/genetics; Escherichia coli/physiology; Genes; Maltose/metabolism; Mutation; Operon; Receptors, Virus/genetics; Transcription, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3550.X50858d634b070&page=3550&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="D50858d6375d3a" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3550.D50858d6375d3a&page=3550&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:3025879

2012-08-27T23:33:59Z

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PMID:3025879

2012-08-27T23:33:59Z

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{| id="R503c03e790078" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Rudd, KE and Menzel, R''' (1987) his operons of Escherichia coli and Salmonella typhimurium are regulated by DNA supercoiling.''Proc. Natl. Acad. Sci. U.S.A.'' '''84''':517-21
|-
!align=left |Abstract
||
The hisW mutations of Salmonella typhimurium are highly pleiotropic mutations that elevate his operon expression, reduce ilv gene expression, alter stable RNA metabolism, and confer defective growth properties. The hisW mutations are highly linked to a naladixic acid-resistant gyrA mutation of S. typhimurium. Multicopy recombinant plasmids containing the Escherichia coli gyrA gene are able to complement both the growth defects and the elevated his operon expression associated with the hisW mutations. We conclude that hisW mutations are alleles of the gyrA gene. The hisU1820 mutant of S. typhimurium exhibits many of the same phenotypes as hisW mutants. Several lines of evidence, including high transduction linkage to recF, suggest that hisU1820 is an allele of gyrB. Finally, well-characterized gyrA and gyrB alleles of E. coli are also his regulatory mutations. We propose that a wild-type degree of chromosomal superhelicity is required for maximal production of histidyl-tRNA and normal his operon regulation.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3025879 PubMed]

|-
!align=left |Keywords
||
Alcohol Oxidoreductases; DNA Restriction Enzymes; DNA, Superhelical; Escherichia coli; Genes; Genes, Bacterial; Genes, Regulator; Genotype; Mutation; Operon; Salmonella typhimurium; Transduction, Genetic; beta-Galactosidase

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3273.R503c03e790078&page=3273&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="U503c03e7be482" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3273.U503c03e7be482&page=3273&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:363690

2012-07-11T23:02:28Z

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PMID:363690

2012-07-11T23:02:28Z

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{| id="I4ffe060448f88" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Iwaya, M, Goldman, R, Tipper, DJ, Feingold, B and Strominger, JL''' (1978) Morphology of an Escherichia coli mutant with a temperature-dependent round cell shape.''J. Bacteriol.'' '''136''':1143-58
|-
!align=left |Abstract
||
Mutants of Escherichia coli capable of growing in the presence of 10 microgram of mecillinam per ml were selected after intensive mutagenesis. Of these mutants, 1.4% formed normal, rod-shaped cells at 30 degrees C but grew as spherical cells at 42 degrees C. The phenotype of one of these rod(Ts) mutants was 88% cotransducible with lip (14.3 min), and all lip+ rod(Ts) transductants of a lip recipient had the following characteristics: (i) growth was relatively sensitive to mecillinam at 30 degrees C but relatively resistant to mecillinam at 42 degrees C; (ii) penicillin-binding protein 2 was present in membranes of cells grown at 30 degrees C in reduced amounts and was undetectable in the membranes of cells grown at 42 degrees C. The mecillinam resistance, penicillin-binding protein 2 defect, and rod phenotypes all cotransduced with lip with high frequency. Thus the mutation [rodA(Ts)] is most likely in the gene for penicillin-binding protein 2 and causes the organism to grow as a sphere at 42 degrees C, although it grows with normal rodlike morphology at 30 degrees C. At 42 degrees C, cells of this strain were round with many wrinkles on their surfaces, as revealed by scanning electron microscopy. In these round cells, chromosomes were dispersed or distributed peripherally, in contrast to normal rod-shaped cells which had centrally located, more condensed chromosomes. The round cells divided asymmetrically on solid agar, and it seemed that the plane of each successive division was perpendicular to the preceding one. On temperature shift-down in liquid medium many cells with abnormal morphology appeared before normal rod-shaped cells developed. Few abnormal cells were seen when cells were placed on solid medium during temperature shift-down. These pleiotropic effects are presumably caused by one or more mutations in the rodA gene.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=363690 PubMed]

|-
!align=left |Keywords
||
Amdinocillin; Carrier Proteins; Cell Division; Chromosome Mapping; Chromosomes, Bacterial; Escherichia coli; Genes; Mutation; Penicillins; Temperature

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3239.I4ffe060448f88&page=3239&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="G4ffe06044df0a" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3239.G4ffe06044df0a&page=3239&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:2185221

2012-06-22T22:43:34Z

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PMID:2185221

2012-06-22T22:43:34Z

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{| id="E4fe4f5162f8cc" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Rainwater, S and Silverman, PM''' (1990) The Cpx proteins of Escherichia coli K-12: evidence that cpxA, ecfB, ssd, and eup mutations all identify the same gene.''J. Bacteriol.'' '''172''':2456-61
|-
!align=left |Abstract
||
An existing cpxA(Ts) mutant was resistant to amikacin at levels that inhibited completely the growth of a cpxA+ and a cpxA deletion strain and failed to grow as efficiently on exogenous proline. These properties are similar to those of mutants altered in a gene mapped to the cpxA locus and variously designated as ecfB, ssd, and eup. The amikacin resistance phenotype of the cpxA mutant was inseparable by recombination from the cpxA mutant phenotype (inability to grow at 41 degrees C without exogenous isoleucine and valine) and was recessive to the cpxA+ allele of a recombinant plasmid. Using methods that ensured independent mutations in the cpxA region of the chromosome, we isolated six new amikacin-resistant mutants following nitrosoguanidine mutagenesis. Three-factor crosses mapped the mutations to the cpxA locus. When transferred by P1 transduction to a cpxB11 Hfr strain, each of the mutations conferred the Tra- and Ilv- phenotypes characteristic of earlier cpxA mutants. Two of the new mutations led to a significantly impaired ability to utilize exogenous proline, and four led to partial resistance to colicin A. Two of the new cpxA alleles were recessive to the cpxA+ allele, and four were dominant, albeit to different degrees. On the basis of these data, we argue that cpxA, ecfB, eup, and ssd are all the same gene. We discuss the cellular function of the cpxA gene product in that light.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2185221 PubMed]

|-
!align=left |Keywords
||
Alleles; Amikacin; Bacterial Proteins; Colicins; Drug Resistance, Microbial; Escherichia coli; Genes, Bacterial; Genetic Linkage; Genotype; Mutation; Plasmids

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3219.E4fe4f5162f8cc&page=3219&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="E4fe4f51632c79" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3219.E4fe4f51632c79&page=3219&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:783151

2012-06-21T18:47:44Z

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PMID:783151

2012-06-21T18:47:44Z

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{{RightTOC}}



{| id="Q4fe36c5054152" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Ramabhadran, TV''' (1976) Method for the isolation of Escherichia coli relaxed mutants, utilizing near-ultraviolet irradiation.''J. Bacteriol.'' '''127''':1587-9
|-
!align=left |Abstract
||
Near-ultraviolet radiation (300 to 380 nm) induces a transient growth inhibition in "stringent" (rel+) strains of Escherichia coli, whereas "relaxed" (rel-) strains are only mildly affected. This difference permits rapid isolation of large numbers of relaxed mutants of E. coli.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=783151 PubMed]

|-
!align=left |Keywords
||
Bacteriological Techniques; Escherichia coli; Mutation; Ultraviolet Rays

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3216.Q4fe36c5054152&page=3216&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="Y4fe36c505967c" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3216.Y4fe36c505967c&page=3216&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:358966

2012-06-08T18:35:33Z

165.91.108.55: Fill PMID: Page!

{{RightTOC}}



{| id="K4fd245f500003" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Delcuve, G, Cabezón, T, Herzog, A, Cannon, M and Bollen, A''' (1978) Resistance to the aminoglycoside antibiotic neamine in Escherichia coli. A new mutant whose NeaR phenotype results from the cumulative effects of two distinct mutations.''Biochem. J.'' '''174''':1-7
|-
!align=left |Abstract
||
A spontaneous mutant of Escherichia coli (strain AB2847), selected for resistance to the aminoglycoside antibiotic neamine, shows severe restriction of amber suppressors in vivo. Ribosomes isolated from the mutant exhibit only low misreading in vitro in the presence of the antibiotic. Genetic and biochemical analyses indicate that the neamine-resistant phenotype is the result of two distinct mutations. The first, res3128, appears to affect the gene (strA) coding for the ribosomal protein S12. Although it leads to a restrictive phenotype it does not, however, confer resistance to streptomycin. The second mutation, X3128, is located between the sirA and AROB loci and is lethal when segregated from the res3128 mutation. It may affect the ribosome at the level of a post-translational modification.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=358966 PubMed]

|-
!align=left |Keywords
||
Drug Resistance, Microbial; Escherichia coli; Mutation; Neomycin; Phenotype; Ribosomes; Suppression, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3205.K4fd245f500003&page=3205&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="C4fd245f520b94" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3205.C4fd245f520b94&page=3205&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:358966

2012-06-08T18:35:32Z

165.91.108.55: New PMID: Page!

PMID:4904136

2012-06-05T21:55:32Z

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PMID:4904136

2012-06-05T21:55:32Z

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{{RightTOC}}



{| id="I4fce805484038" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Guest, JR''' (1969) Biochemical and genetic studies with nitrate reductase C-gene mutants of Escherichia coli.''Mol. Gen. Genet.'' '''105''':285-97
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=4904136 PubMed]

|-
!align=left |Keywords
||
Chromosome Mapping; Crosses, Genetic; Escherichia coli; Genes; Mutation; Oxidoreductases; Transduction, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3201.I4fce805484038&page=3201&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="J4fce805487737" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.3201.J4fce805487737&page=3201&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:342908

2012-04-12T17:19:06Z

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PMID:342908

2012-04-12T17:19:06Z

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{{RightTOC}}



{| id="F4f870e8a51abf" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Buckel, P, Buchberger, A, Böck, A and Wittmann, HG''' (1977) Alteration of ribosomal protein L6 in mutants of Escherichia coli resistant to gentamicin.''Mol. Gen. Genet.'' '''158''':47-54
|-
!align=left |Abstract
||
No abstract in PubMed
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=342908 PubMed]

|-
!align=left |Keywords
||
Drug Resistance, Microbial; Escherichia coli; Gentamicins; Ribosomal Proteins

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2927.F4f870e8a51abf&page=2927&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="C4f870e8a55364" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2927.C4f870e8a55364&page=2927&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:230407

2012-04-05T17:06:22Z

165.91.108.55: Fill PMID: Page!

{{RightTOC}}



{| id="O4f7dd10e3cd56" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Daniel, J and Danchin, A''' (1979) Involvement of cyclic AMP and its receptor protein in the sensitivity of Escherichia coli K 12 toward serine: excretion of 2-ketobutyrate, a precursor of isoleucine.''Mol. Gen. Genet.'' '''176''':343-50
|-
!align=left |Abstract
||
A relationship between serine-induced growth sensitivity and the cAMP-CAP complex is established. Mutants of Escherichia coli K 12 deficient either in the cya or crp gene function exhibit a resistant phenotype on serine media although they harbor a relA allele normally leading to sensitivity toward serine. The presence of a crp allele in a cya delta relA background restores the sensitivity phenotype, while the analysis of serine resistant mutants selected from a crp cya delta relA strain shows that the mutation leading to resistance is located at, or very near, the crp gene, giving a more or less Crp- phenotype. In addition crp cya delta relA strains excrete large quantities of 2-ketobutyrate when grown on glucose M63 medium. This excretion is unambiguously linked to the presence of the crp allele and is correlated with an enhanced threonine deaminase activity. Besides, the complex regulation exerted on the acetolactate synthase activities is discussed.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=230407 PubMed]

|-
!align=left |Keywords
||
Butyrates; Cyclic AMP; Escherichia coli; Isoleucine; Mutation; Phenotype; Receptors, Cyclic AMP; Serine; Transduction, Genetic

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2905.O4f7dd10e3cd56&page=2905&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="Z4f7dd10e5c2ad" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2905.Z4f7dd10e5c2ad&page=2905&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:230407

2012-04-05T17:06:21Z

165.91.108.55: New PMID: Page!

PMID:6178725

2012-03-02T16:43:48Z

165.91.108.55: Fill PMID: Page!

{{RightTOC}}



{| id="I4f50f8c40841d" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Ryals, J, Hsu, RY, Lipsett, MN and Bremer, H''' (1982) Isolation of single-site Escherichia coli mutants deficient in thiamine and 4-thiouridine syntheses: identification of a nuvC mutant.''J. Bacteriol.'' '''151''':899-904
|-
!align=left |Abstract
||
A method is described to rapidly select and classify many independent near-UV irradiation-resistant Escherichia coli mutants, which include tRNA modification and RNA synthesis control mutants. One class of these mutants was found to be simultaneously deficient in thiamine biosynthesis and in the ability to modify uridine in tRNA to 4-thiouridine, known to be the target for near-UV irradiation. These mutants were found to be unable to make thiazole, a thiamine precursor. The addition of thiazole restores the thiamine deficiency but does not render the cells near-UV irradiation sensitive. In vitro studies on one of these mutants indicated a deficiency in protein factor C (nuvC), required for the 4-thiouridine modification of tRNA. In P1 transduction, the thiazole marker cotransduced with the histidine marker, which places the thiazole marker between 42 and 46 min on the E. coli chromosome map. Both thiamine production and 4-thiouridine production were resumed by 87% of the spontaneous reversions, suggesting a single-point mutation. Our results indicate that we have isolated nuvC mutants and that the nuvC polypeptide is involved in two functions, tRNA modification and thiazole biosynthesis.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=6178725 PubMed]

|-
!align=left |Keywords
||
Chromosome Mapping; Chromosomes, Bacterial; Escherichia coli; Genes, Bacterial; Mutation; RNA, Bacterial; RNA, Transfer; Thiamine; Thiazoles; Thiouridine; Ultraviolet Rays

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2868.I4f50f8c40841d&page=2868&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="Q4f50f8c43f12b" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2868.Q4f50f8c43f12b&page=2868&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:6178725

2012-03-02T16:43:47Z

165.91.108.55: New PMID: Page!

PMID:17709419

2012-02-01T19:37:58Z

165.91.108.55: Fill PMID: Page!

{{RightTOC}}



{| id="A4f2994959756c" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Autieri, SM, Lins, JJ, Leatham, MP, Laux, DC, Conway, T and Cohen, PS''' (2007) L-fucose stimulates utilization of D-ribose by Escherichia coli MG1655 DeltafucAO and E. coli Nissle 1917 DeltafucAO mutants in the mouse intestine and in M9 minimal medium.''Infect. Immun.'' '''75''':5465-75
|-
!align=left |Abstract
||
Escherichia coli MG1655 uses several sugars for growth in the mouse intestine. To determine the roles of L-fucose and D-ribose, an E. coli MG1655 DeltafucAO mutant and an E. coli MG1655 DeltarbsK mutant were fed separately to mice along with wild-type E. coli MG1655. The E. coli MG1655 DeltafucAO mutant colonized the intestine at a level 2 orders of magnitude lower than that of the wild type, but the E. coli MG1655 DeltarbsK mutant and the wild type colonized at nearly identical levels. Surprisingly, an E. coli MG1655 DeltafucAO DeltarbsK mutant was eliminated from the intestine by either wild-type E. coli MG1655 or E. coli MG1655 DeltafucAO, suggesting that the DeltafucAO mutant switches to ribose in vivo. Indeed, in vitro growth experiments showed that L-fucose stimulated utilization of D-ribose by the E. coli MG1655 DeltafucAO mutant but not by an E. coli MG1655 DeltafucK mutant. Since the DeltafucK mutant cannot convert L-fuculose to L-fuculose-1-phosphate, whereas the DeltafucAO mutant accumulates L-fuculose-1-phosphate, the data suggest that L-fuculose-1-phosphate stimulates growth on ribose both in the intestine and in vitro. An E. coli Nissle 1917 DeltafucAO mutant, derived from a human probiotic commensal strain, acted in a manner identical to that of E. coli MG1655 DeltafucAO in vivo and in vitro. Furthermore, L-fucose at a concentration too low to support growth stimulated the utilization of ribose by the wild-type E. coli strains in vitro. Collectively, the data suggest that L-fuculose-1-phosphate plays a role in the regulation of ribose usage as a carbon source by E. coli MG1655 and E. coli Nissle 1917 in the mouse intestine.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17709419 PubMed]
Online version:[http://dx.doi.org/10.1128/IAI.00822-07 10.1128/IAI.00822-07]
|-
!align=left |Keywords
||
Animals; Biomass; Colony Count, Microbial; Escherichia coli; Escherichia coli Proteins; Fructose-Bisphosphate Aldolase; Fucose; Gene Deletion; Hexosephosphates; Intestines; Male; Mice; Phosphotransferases (Alcohol Group Acceptor); Ribose; Spectrophotometry

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2842.A4f2994959756c&page=2842&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="W4f299495c7677" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2842.W4f299495c7677&page=2842&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:17709419

2012-02-01T19:37:57Z

165.91.108.55: New PMID: Page!

PMID:1938875

2012-01-25T22:32:53Z

165.91.108.55: Fill PMID: Page!

{{RightTOC}}



{| id="V4f208314b9aa2" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Nurse, P, Zavitz, KH and Marians, KJ''' (1991) Inactivation of the Escherichia coli priA DNA replication protein induces the SOS response.''J. Bacteriol.'' '''173''':6686-93
|-
!align=left |Abstract
||
Many of the proteins that operate at the replication fork in Escherichia coli have been defined genetically. These include some of the subunits of the DNA polymerase III holoenzyme, the DnaB replication fork helicase, and the DnaG primase. The multiprotein primosome (which includes the DnaB and DnaG proteins), defined biochemically on the basis of its requirement during bacteriophage phi X174 complementary-strand synthesis, could serve as the helicase-primase replication machine on the lagging-strand template. In order to determine if this is the case, we have begun an investigation of the phenotypes of mutants with mutations priA, priB, and priC, which encode the primosomal proteins factor Y (protein n'), n, and n", respectively. Inactivation of priA by insertional mutagenesis resulted in the induction of the SOS response, as evinced by induction of a resident lambda prophage, extreme filamentation, and derepression of an indicator operon in which beta-galactosidase production was controlled by the dinD1 promoter. In addition, the copy numbers of resident pBR322 plasmids were reduced four- to fivefold in these strains, and production of phi X174 phage was delayed considerably. These results are discussed in the context of existing models for SOS induction and possible roles for the PriA protein at the replication fork in vivo.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1938875 PubMed]

|-
!align=left |Keywords
||
Bacterial Proteins; Blotting, Southern; DNA Replication; DNA, Bacterial; Escherichia coli; Genes, Bacterial; Mutagenesis, Insertional; Phenotype; SOS Response (Genetics)

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2835.V4f208314b9aa2&page=2835&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="F4f208314df2b0" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.2835.F4f208314df2b0&page=2835&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
{{RefHelp}}
<references/>

[[Category:Publication]]

PMID:1938875

2012-01-25T22:32:52Z

165.91.108.55: New PMID: Page!

PMID:21889623

2011-09-29T22:51:50Z

165.91.108.55: Fill PMID: Page!

{{RightTOC}}



{| id="M4e84f68680120" class=" tableEdit PMID_info_table"

|-
!align=left |Citation
||
'''Updegrove, TB and Wartell, RM''' (2011) The influence of Escherichia coli Hfq mutations on RNA binding and sRNA•mRNA duplex formation in rpoS riboregulation.''Biochim Biophys Acta''
|-
!align=left |Abstract
||
The Escherichia coli RNA binding protein Hfq plays an important role in regulating mRNA translation through its interactions with small non-coding RNAs (sRNAs) and specific mRNAs sites. The rpoS mRNA, which codes for a transcription factor, is regulated by several sRNAs. DsrA and RprA enhance translation by pairing to a site on this mRNA, while OxyS represses rpoS mRNA translation. To better understand how Hfq interacts with these sRNAs and rpoS mRNA, the binding of wt Hfq and eleven mutant Hfqs to DsrA, RprA, OxyS and rpoS mRNA was examined. Nine of the mutant Hfq had single-residue mutations located on the proximal, distal, and outer-edge surfaces of the Hfq hexamer, while two Hfq had truncated C-terminal ends. Hfq with outer-edge mutations and truncated C-terminal ends behaved similar to wt Hfq with regard to binding the sRNAs, rpoS mRNA segments, and stimulating DsrA•rpoS mRNA formation. Proximal surface mutations decreased Hfq binding to the three sRNAs and the rpoS mRNA segment containing the translation initiation region. Distal surface mutations lowered Hfq's affinity for the rpoS mRNA segment containing the (ARN)(4) sequence. Strong Hfq binding to both rpoS mRNA segments appears to be needed for maximum enhancement of DsrA•rpoS mRNA annealing. OxyS bound tightly to Hfq but exhibited weak affinity for rpoS mRNA containing the leader region and 75 nt of coding sequence in the absence or presence of Hfq. This together with other results suggest OxyS represses rpoS mRNA translation by sequestering Hfq rather than binding to rpoS mRNA.
|-
!align=left |Links
||
[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=21889623 PubMed]
Online version:[http://dx.doi.org/10.1016/j.bbagrm.2011.08.006 10.1016/j.bbagrm.2011.08.006]
|-
!align=left |Keywords
||

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=2ccfb3c7bf1208312f02a69e64bfd9e0.2766.M4e84f68680120&page=2766&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table] ||
|}


==Main Points of the Paper ==
{{LitSignificance}}

== Materials and Methods Used ==
{{LitMaterials}}

==Phenotype Annotations==
{{AnnotationTableHelp}}
<protect>

{| id="Q4e84f686a4674" class=" tableEdit Phenotype_Table_2"
|-
!|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status

|- class="tableEdit_footer"
|[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=2ccfb3c7bf1208312f02a69e64bfd9e0.2766.Q4e84f686a4674&page=2766&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table] || || || || || || || || ||
|}
</protect>

==Notes==

==References==
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[[Category:Publication]]

PMID:21889623

2011-09-29T22:51:49Z

165.91.108.55: New PMID: Page!