PMID:2883171: Difference between revisions

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{|  id="L4d81058a141c3"  class=" tableEdit PMID_info_table" 
|-
!align=left  |Citation
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'''Jenkins, LS and Nunn, WD'''  (1987) Regulation of the ato operon by the atoC gene in Escherichia coli.''J. Bacteriol.'' '''169''':2096-102
|-
!align=left  |Abstract
||
The expression of the Ato enzymes, acetyl coenzyme A:acetoacetyl coenzyme A transferase and thiolase II, is required for growth of Escherichia coli on short-chain fatty acids. The structural genes for these enzymes, atoD, atoA, and atoB, respectively, make up the ato operon. A 48-kilodalton protein encoded by atoC was required for the synthesis or activation of the Ato enzymes. The expression of Ato enzyme activities was inducible in atoC+ strains, constitutive in atoCc strains, and noninducible in atoC mutants. Merodiploid studies demonstrated that the atoCc allele is trans-dominant to the atoC+ allele. To study the action of the trans-acting atoC-encoded activator, the promoter of the ato operon was fused to the promoterless galK gene and introduced into a low-copy-number vector. The resulting low-copy-number fusion plasmid was introduced into atoC+, atoC, and atoCc hosts. The expression of the fused galK gene was inducible in the atoC+ host, noninducible in atoC host strains, and constitutive when harbored in the atoCc host. This indicated that the atoC+ and atoCc gene products act at the level of transcription, stimulating the expression of the ato operon. A working model consistent with these results is presented.
|-
!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2883171 PubMed]
|-
!align=left  |Keywords
||
Acetoacetates; Acetyl-CoA C-Acetyltransferase; Butyrates; Cloning, Molecular; Coenzyme A-Transferases; DNA-Binding Proteins; Enzyme Induction; Escherichia coli; Gene Expression Regulation; Genes, Bacterial; Operon; Promoter Regions, Genetic; Sulfurtransferases
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==Main Points of the Paper ==
{{LitSignificance}}
== Materials and Methods Used ==
{{LitMaterials}}
==Phenotype Annotations==
{{AnnotationTableHelp}}
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{|  id="J4d81058a2a2c1"  class=" tableEdit PMID_Phenotype_table" 
|-
!|Species!!Taxon ID!!Strain!!Gene (if known)!!OMP!!Phenotype!!Details!!Evidence!!Notes
|-
|
''Escherichia coli''
|
|
LS5218
|
''atoC<sup>c2</sup>
|
Growth on butyrate as a sole carbon source
|
Growth
|
spontaneous butyrate+ colonies
|
Plating Assay
|
|-
|
''Escherichia coli''
|
|
LS5218
|
''atoC<sup>c2</sup>
|
constitutive acetoacetate (AA)-CoA transferase level
|
Expression
|
|
Biochemical Assay
|
Table 3
|-
|
''Escherichia coli''
|
|
LS5218
|
''atoC<sup>c2</sup>
|
constitutive thiolase level
|
Expression
|
|
Biochemical Assay
|
Table 3
|-
|
''Escherichia coli''
|
|
LS5218
|
''atoC<sup>c2</sup>
|
increased levels of acetoacetate (AA)-CoA transferase
|
Metabolic Activity
|
two-fold higher than the inducible levels measured for the ''atoC''<sup>+</sup>
|
Biochemical Assay
|
Table 3
|-
|
''Escherichia coli''
|
|
LS5218
|
''atoC<sup>c2</sup>
|
Growth on butyrate as a sole carbon source
|
Growth
|
spontaneous butyrate+ colonies
|
Plating Assay
|
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
constitutive thiolase level
|
Expression
|
merodiploid- fully dominant to the ''atoC<sup>+</sup>'' genotype
|
Biochemical Assay
|
Table 3
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
constitutive acetoacetate (AA)-CoA transferase level
|
Expression
|
merodiploid- fully dominant to the ''atoC<sup>+</sup>'' genotype
|
Biochemical Assay
|
Table 3
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
constitutive acetoacetate (AA)-CoA transferase level
|
Expression
|
''trans''-dominant to the ''atoC<sup>+</sup>'' genotype
|
Biochemical Assay
|
Table 3
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
Growth on butyrate as a sole carbon source
|
Growth
|
''trans''-dominant to the ''atoC<sup>+</sup> genotype
|
Plating Assay
|
|-
|
''Escherichia coli''
|
|
|
''atoC31''
|
absent galactokinase activity
|
Metabolic Activity
|
with induction
|
Biochemical Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC61''
|
white colonies on MacConkey-galactose plates
|
|
with induction
|
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
Growth on butyrate as a sole carbon source
|
Growth
|
''trans''-dominant to the ''atoC<sup>+</sup> genotype
|
Plating Assay
|
|-
|
''Escherichia coli''
|
|
|
''atoC31''
|
white colonies on MacConkey-galactose plates
|
|
with induction
|
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC61''
|
absent galactokinase activity
|
Metabolic Activity
|
with induction
|
Biochemical Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
red colonies on MacConkey-galactose plates
|
Metabolic Activity
|
when induced or uninduced
|
Plating Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>
|
increased galactokinase activity
|
Metabolic Activity
|
2-3 fold higher galactokinase activity than ''atoC<sup>+</sup>''
|
Biochemical Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>+</sup>''
|
able to utilize galactose as carbon source
|
Metabolic Activity
|
|
Plating Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC<sup>c2</sup>''
|
able to utilize galactose as carbon source
|
Metabolic Activity
|
|
Plating Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC31''
|
unable to utilize galactose as carbon source
|
Metabolic Activity
|
|
Plating Assay
|
Table 5
|-
|
''Escherichia coli''
|
|
|
''atoC61''
|
unable to utilize galactose as carbon source
|
Metabolic Activity
|
|
Plating Assay
|
Table 5
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==Notes==
==References==
{{RefHelp}}
<references/>
[[Category:Publication]]
[[Category:To Be Converted]]

Latest revision as of 17:09, 22 June 2011

Citation

Jenkins, LS and Nunn, WD (1987) Regulation of the ato operon by the atoC gene in Escherichia coli.J. Bacteriol. 169:2096-102

Abstract

The expression of the Ato enzymes, acetyl coenzyme A:acetoacetyl coenzyme A transferase and thiolase II, is required for growth of Escherichia coli on short-chain fatty acids. The structural genes for these enzymes, atoD, atoA, and atoB, respectively, make up the ato operon. A 48-kilodalton protein encoded by atoC was required for the synthesis or activation of the Ato enzymes. The expression of Ato enzyme activities was inducible in atoC+ strains, constitutive in atoCc strains, and noninducible in atoC mutants. Merodiploid studies demonstrated that the atoCc allele is trans-dominant to the atoC+ allele. To study the action of the trans-acting atoC-encoded activator, the promoter of the ato operon was fused to the promoterless galK gene and introduced into a low-copy-number vector. The resulting low-copy-number fusion plasmid was introduced into atoC+, atoC, and atoCc hosts. The expression of the fused galK gene was inducible in the atoC+ host, noninducible in atoC host strains, and constitutive when harbored in the atoCc host. This indicated that the atoC+ and atoCc gene products act at the level of transcription, stimulating the expression of the ato operon. A working model consistent with these results is presented.

Links

PubMed

Keywords

Acetoacetates; Acetyl-CoA C-Acetyltransferase; Butyrates; Cloning, Molecular; Coenzyme A-Transferases; DNA-Binding Proteins; Enzyme Induction; Escherichia coli; Gene Expression Regulation; Genes, Bacterial; Operon; Promoter Regions, Genetic; Sulfurtransferases

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Main Points of the Paper

Please summarize the main points of the paper.

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

See Help:AnnotationTable for details on how to edit this table.

Species Taxon ID Strain Gene (if known) OMP Phenotype Details Evidence Notes

Escherichia coli

LS5218

atoCc2

Growth on butyrate as a sole carbon source

Growth

spontaneous butyrate+ colonies

Plating Assay

Escherichia coli

LS5218

atoCc2

constitutive acetoacetate (AA)-CoA transferase level

Expression

Biochemical Assay

Table 3

Escherichia coli

LS5218

atoCc2

constitutive thiolase level

Expression

Biochemical Assay

Table 3

Escherichia coli

LS5218

atoCc2

increased levels of acetoacetate (AA)-CoA transferase

Metabolic Activity

two-fold higher than the inducible levels measured for the atoC+

Biochemical Assay

Table 3

Escherichia coli

LS5218

atoCc2

Growth on butyrate as a sole carbon source

Growth

spontaneous butyrate+ colonies

Plating Assay

Escherichia coli

atoCc2

constitutive thiolase level

Expression

merodiploid- fully dominant to the atoC+ genotype

Biochemical Assay

Table 3

Escherichia coli

atoCc2

constitutive acetoacetate (AA)-CoA transferase level

Expression

merodiploid- fully dominant to the atoC+ genotype

Biochemical Assay

Table 3

Escherichia coli

atoCc2

constitutive acetoacetate (AA)-CoA transferase level

Expression

trans-dominant to the atoC+ genotype

Biochemical Assay

Table 3

Escherichia coli

atoCc2

Growth on butyrate as a sole carbon source

Growth

trans-dominant to the atoC+ genotype

Plating Assay

Escherichia coli

atoC31

absent galactokinase activity

Metabolic Activity

with induction

Biochemical Assay

Table 5

Escherichia coli

atoC61

white colonies on MacConkey-galactose plates

with induction

Table 5

Escherichia coli

atoCc2

Growth on butyrate as a sole carbon source

Growth

trans-dominant to the atoC+ genotype

Plating Assay

Escherichia coli

atoC31

white colonies on MacConkey-galactose plates

with induction

Table 5

Escherichia coli

atoC61

absent galactokinase activity

Metabolic Activity

with induction

Biochemical Assay

Table 5

Escherichia coli

atoCc2

red colonies on MacConkey-galactose plates

Metabolic Activity

when induced or uninduced

Plating Assay

Table 5

Escherichia coli

atoCc2

increased galactokinase activity

Metabolic Activity

2-3 fold higher galactokinase activity than atoC+

Biochemical Assay

Table 5

Escherichia coli

atoC+

able to utilize galactose as carbon source

Metabolic Activity

Plating Assay

Table 5

Escherichia coli

atoCc2

able to utilize galactose as carbon source

Metabolic Activity

Plating Assay

Table 5

Escherichia coli

atoC31

unable to utilize galactose as carbon source

Metabolic Activity

Plating Assay

Table 5

Escherichia coli

atoC61

unable to utilize galactose as carbon source

Metabolic Activity

Plating Assay

Table 5

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Notes

References

See Help:References for how to manage references in OMPwiki.

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