PMID:9853401: Difference between revisions

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<span style = 'font-size: large'> '''Ohba, A, Inoue, R, Akimitsu, N, Mizushima, T and Sekimizu, K'''  (1998) Identification of proteins whose amounts are altered by mutation in the pgsA gene of Escherichia coli.''Biol. Pharm. Bull.'' '''21''':1139-41</span>
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!align=left  |Citation
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'''No author listed'''  (1998) Identification of proteins whose amounts are altered by mutation in the pgsA gene of Escherichia coli. ''Biol. Pharm. Bull.'' '''21''':1139-41
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!align=left  |Abstract
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We identified proteins whose amounts were altered in an Escherichia coli pgsA3 mutant lacking the potential to synthesize phosphatidylglycerolphosphate, a precursor of phosphatidylglycerol. Proteins whose amounts were increased in the mutant were protease Do, periplasmic oligopeptide-binding protein, tryptophanase, and an unidentified protein, while the decreased one was flagellin. Transformation of the mutant with a plasmid containing the wild type pgsA gene complemented the phenotype, indicating that the pgsA3 mutation is responsible for the phenotype.
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!align=left  |Links
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9853401 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || We identified proteins whose amounts were altered in an Escherichia coli pgsA3 mutant lacking the potential to synthesize phosphatidylglycerolphosphate, a precursor of phosphatidylglycerol. Proteins whose amounts were increased in the mutant were protease Do, periplasmic oligopeptide-binding protein, tryptophanase, and an unidentified protein, while the decreased one was flagellin. Transformation of the mutant with a plasmid containing the wild type pgsA gene complemented the phenotype, indicating that the pgsA3 mutation is responsible for the phenotype.
!align=left  |Keywords
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Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Flagellin/metabolism; Heat-Shock Proteins; Molecular Sequence Data; Mutation; Periplasmic Proteins; Sequence Analysis; Serine Endopeptidases/metabolism; Transferases (Other Substituted Phosphate Groups)/genetics; Transferases (Other Substituted Phosphate Groups)/metabolism; Tryptophanase/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9853401 PubMed]
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
{{LitSignificance}}
{{LitSignificance}}

Revision as of 20:10, 1 September 2013

Citation

No author listed (1998) Identification of proteins whose amounts are altered by mutation in the pgsA gene of Escherichia coli. Biol. Pharm. Bull. 21:1139-41

Abstract

We identified proteins whose amounts were altered in an Escherichia coli pgsA3 mutant lacking the potential to synthesize phosphatidylglycerolphosphate, a precursor of phosphatidylglycerol. Proteins whose amounts were increased in the mutant were protease Do, periplasmic oligopeptide-binding protein, tryptophanase, and an unidentified protein, while the decreased one was flagellin. Transformation of the mutant with a plasmid containing the wild type pgsA gene complemented the phenotype, indicating that the pgsA3 mutation is responsible for the phenotype.

Links

PubMed

Keywords

Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/metabolism; Flagellin/metabolism; Heat-Shock Proteins; Molecular Sequence Data; Mutation; Periplasmic Proteins; Sequence Analysis; Serine Endopeptidases/metabolism; Transferases (Other Substituted Phosphate Groups)/genetics; Transferases (Other Substituted Phosphate Groups)/metabolism; Tryptophanase/metabolism

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Gene product Qualifier GO ID GO term name Evidence Code with/from Aspect Notes Status
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