PMID:8021205: Difference between revisions

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<span style = 'font-size: large'> '''Chun, SY and Randall, LL'''  (1994) In vivo studies of the role of SecA during protein export in Escherichia coli.''J. Bacteriol.'' '''176''':4197-203</span>
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!align=left  |Citation
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'''Chun, SY and Randall, LL'''  (1994) In vivo studies of the role of SecA during protein export in Escherichia coli. ''J. Bacteriol.'' '''176''':4197-203
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!align=left  |Abstract
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SecA is found in Escherichia coli both tightly associated with the cytoplasmic membrane where it functions as a translocation ATPase during protein export and free in the cytosol (R. J. Cabelli, K. M. Dolan, L. Qian, and D. B. Oliver, J. Biol. Chem. 266:24420-24427, 1991; D. B. Oliver and J. Beckwith, Cell 30:311-319, 1982; W. Wickner, A. J. M. Driessen, and F.-U. Hartl, Annu. Rev. Biochem. 60:101-124, 1991). Here we show that SecA can be immunoprecipitated from the cytosol in complex with both fully elongated and nascent species of the precursor of maltose-binding protein, an exported, periplasmic protein. In addition, under conditions in which the distribution of SecA between the cytosolic and membrane-bound states changes from that normally observed, the distribution of precursor maltose-binding protein changes in parallel. These results support the idea that cytosolic SecA plays a role in export. With the aim of determining the roles of the multiple binding sites for ATP on SecA, we compared the export defect in a culture of E. coli expressing a temperature-sensitive allele of secA with the defect in a culture treated with sodium azide. The results indicate that the mutational change and treatment with sodium azide inhibit export by affecting different steps in the cycle of ATP binding and hydrolysis by SecA.
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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=8021205 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC205629 PMC205629]


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|{{TableHeadingColor}} |'''Abstract''' || SecA is found in Escherichia coli both tightly associated with the cytoplasmic membrane where it functions as a translocation ATPase during protein export and free in the cytosol (R. J. Cabelli, K. M. Dolan, L. Qian, and D. B. Oliver, J. Biol. Chem. 266:24420-24427, 1991; D. B. Oliver and J. Beckwith, Cell 30:311-319, 1982; W. Wickner, A. J. M. Driessen, and F.-U. Hartl, Annu. Rev. Biochem. 60:101-124, 1991). Here we show that SecA can be immunoprecipitated from the cytosol in complex with both fully elongated and nascent species of the precursor of maltose-binding protein, an exported, periplasmic protein. In addition, under conditions in which the distribution of SecA between the cytosolic and membrane-bound states changes from that normally observed, the distribution of precursor maltose-binding protein changes in parallel. These results support the idea that cytosolic SecA plays a role in export. With the aim of determining the roles of the multiple binding sites for ATP on SecA, we compared the export defect in a culture of E. coli expressing a temperature-sensitive allele of secA with the defect in a culture treated with sodium azide. The results indicate that the mutational change and treatment with sodium azide inhibit export by affecting different steps in the cycle of ATP binding and hydrolysis by SecA.
!align=left  |Keywords
</noinclude>
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ATP-Binding Cassette Transporters; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Azides/pharmacology; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Binding Sites; Biological Transport/drug effects; Carrier Proteins/metabolism; Cell Membrane/metabolism; Cytosol/metabolism; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins; Maltose-Binding Proteins; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutation; Periplasmic Binding Proteins; Protein Precursors/metabolism; Sodium Azide
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8021205 PubMed]
 
[http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&pubmedid=8021205 Full text]
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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==EcoliWiki Links {{HelpIcon|Help:Literature}} ==
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Latest revision as of 04:52, 15 September 2013

Citation

Chun, SY and Randall, LL (1994) In vivo studies of the role of SecA during protein export in Escherichia coli. J. Bacteriol. 176:4197-203

Abstract

SecA is found in Escherichia coli both tightly associated with the cytoplasmic membrane where it functions as a translocation ATPase during protein export and free in the cytosol (R. J. Cabelli, K. M. Dolan, L. Qian, and D. B. Oliver, J. Biol. Chem. 266:24420-24427, 1991; D. B. Oliver and J. Beckwith, Cell 30:311-319, 1982; W. Wickner, A. J. M. Driessen, and F.-U. Hartl, Annu. Rev. Biochem. 60:101-124, 1991). Here we show that SecA can be immunoprecipitated from the cytosol in complex with both fully elongated and nascent species of the precursor of maltose-binding protein, an exported, periplasmic protein. In addition, under conditions in which the distribution of SecA between the cytosolic and membrane-bound states changes from that normally observed, the distribution of precursor maltose-binding protein changes in parallel. These results support the idea that cytosolic SecA plays a role in export. With the aim of determining the roles of the multiple binding sites for ATP on SecA, we compared the export defect in a culture of E. coli expressing a temperature-sensitive allele of secA with the defect in a culture treated with sodium azide. The results indicate that the mutational change and treatment with sodium azide inhibit export by affecting different steps in the cycle of ATP binding and hydrolysis by SecA.

Links

PubMed PMC205629

Keywords

ATP-Binding Cassette Transporters; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Azides/pharmacology; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Binding Sites; Biological Transport/drug effects; Carrier Proteins/metabolism; Cell Membrane/metabolism; Cytosol/metabolism; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins; Maltose-Binding Proteins; Membrane Transport Proteins; Monosaccharide Transport Proteins; Mutation; Periplasmic Binding Proteins; Protein Precursors/metabolism; Sodium Azide

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