Difference between revisions of "PMID:790385"
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+ | {| id="S55a94bf3964ce" class=" tableEdit PMID_info_table" | ||
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+ | !align=left align='left' bgcolor='#CCCCFF' |Citation | ||
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+ | '''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 | ||
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+ | !align=left align='left' bgcolor='#CCCCFF' |Abstract | ||
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+ | 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. | ||
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+ | !align=left align='left' bgcolor='#CCCCFF' |Links | ||
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+ | [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] | ||
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+ | !align=left align='left' bgcolor='#CCCCFF' |Keywords | ||
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+ | Biological Transport; Cell Membrane/enzymology; Cytoplasm/enzymology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Galactosidases/metabolism; Genes; Genes, Regulator; Genetic Engineering; Maltose/metabolism; Operon | ||
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+ | ==Main Points of the Paper == | ||
+ | {{LitSignificance}} | ||
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+ | == Materials and Methods Used == | ||
+ | {{LitMaterials}} | ||
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+ | ==Phenotype Annotations== | ||
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+ | !|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status | ||
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+ | ==Notes== | ||
+ | |||
+ | ==References== | ||
+ | {{RefHelp}} | ||
+ | <references/> | ||
+ | |||
+ | |||
+ | [[Category:Publication]] |
Latest revision as of 12:39, 17 July 2015
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 |
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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. |
Links | |
Keywords |
Biological Transport; Cell Membrane/enzymology; Cytoplasm/enzymology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Galactosidases/metabolism; Genes; Genes, Regulator; Genetic Engineering; Maltose/metabolism; Operon |
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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
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Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
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Notes
References
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