PMID:9190818: Difference between revisions

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<span style = 'font-size: large'> '''Helde, R, Wiesler, B, Wachter, E, Neubüser, A, Hoffschulte, HK, Hengelage, T, Schimz, KL, Stuart, RA and Müller, M'''  (1997) Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity.''J. Bacteriol.'' '''179''':4003-12</span>
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'''Helde, R, Wiesler, B, Wachter, E, Neubüser, A, Hoffschulte, HK, Hengelage, T, Schimz, KL, Stuart, RA and Müller, M'''  (1997) Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity. ''J. Bacteriol.'' '''179''':4003-12
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!align=left  |Abstract
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We have cloned the secA gene of the alpha-subclass purple bacterium Rhodobacter capsulatus, a close relative to the mitochondrial ancestor, and purified the protein after expression in Escherichia coli. R. capsulatus SecA contains 904 amino acids with 53% identity to E. coli and 54% identity to Caulobacter crescentus SecA. In contrast to the nearly equal partitioning of E. coli SecA between the cytosol and plasma membrane, R. capsulatus SecA is recovered predominantly from the membrane fraction. A SecA-deficient, cell-free synthesis-translocation system prepared from R. capsulatus is used to demonstrate translocation activity of the purified R. capsulatus SecA. This translocation activity is then compared to that of the E. coli counterpart by using various precursor proteins and inside-out membrane vesicles prepared from both bacteria. We find a preference of the R. capsulatus SecA for the homologous membrane vesicles whereas E. coli SecA is active with either type of membrane. Furthermore, the two SecA proteins clearly select between distinct precursor proteins. In addition, we show here for the first time that a bacterial c-type cytochrome utilizes the canonical, Sec-dependent export pathway.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9190818 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC179211 PMC179211]


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|{{TableHeadingColor}} |'''Abstract''' || We have cloned the secA gene of the alpha-subclass purple bacterium Rhodobacter capsulatus, a close relative to the mitochondrial ancestor, and purified the protein after expression in Escherichia coli. R. capsulatus SecA contains 904 amino acids with 53% identity to E. coli and 54% identity to Caulobacter crescentus SecA. In contrast to the nearly equal partitioning of E. coli SecA between the cytosol and plasma membrane, R. capsulatus SecA is recovered predominantly from the membrane fraction. A SecA-deficient, cell-free synthesis-translocation system prepared from R. capsulatus is used to demonstrate translocation activity of the purified R. capsulatus SecA. This translocation activity is then compared to that of the E. coli counterpart by using various precursor proteins and inside-out membrane vesicles prepared from both bacteria. We find a preference of the R. capsulatus SecA for the homologous membrane vesicles whereas E. coli SecA is active with either type of membrane. Furthermore, the two SecA proteins clearly select between distinct precursor proteins. In addition, we show here for the first time that a bacterial c-type cytochrome utilizes the canonical, Sec-dependent export pathway.
!align=left  |Keywords
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Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/physiology; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/physiology; Biological Transport; Cell Membrane/metabolism; Cytochrome c Group/biosynthesis; Cytochromes c2; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Transport Proteins; Molecular Sequence Data; Protein Precursors/metabolism; Rhodobacter capsulatus/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9190818 PubMed]
 
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Latest revision as of 04:57, 15 September 2013

Citation

Helde, R, Wiesler, B, Wachter, E, Neubüser, A, Hoffschulte, HK, Hengelage, T, Schimz, KL, Stuart, RA and Müller, M (1997) Comparative characterization of SecA from the alpha-subclass purple bacterium Rhodobacter capsulatus and Escherichia coli reveals differences in membrane and precursor specificity. J. Bacteriol. 179:4003-12

Abstract

We have cloned the secA gene of the alpha-subclass purple bacterium Rhodobacter capsulatus, a close relative to the mitochondrial ancestor, and purified the protein after expression in Escherichia coli. R. capsulatus SecA contains 904 amino acids with 53% identity to E. coli and 54% identity to Caulobacter crescentus SecA. In contrast to the nearly equal partitioning of E. coli SecA between the cytosol and plasma membrane, R. capsulatus SecA is recovered predominantly from the membrane fraction. A SecA-deficient, cell-free synthesis-translocation system prepared from R. capsulatus is used to demonstrate translocation activity of the purified R. capsulatus SecA. This translocation activity is then compared to that of the E. coli counterpart by using various precursor proteins and inside-out membrane vesicles prepared from both bacteria. We find a preference of the R. capsulatus SecA for the homologous membrane vesicles whereas E. coli SecA is active with either type of membrane. Furthermore, the two SecA proteins clearly select between distinct precursor proteins. In addition, we show here for the first time that a bacterial c-type cytochrome utilizes the canonical, Sec-dependent export pathway.

Links

PubMed PMC179211

Keywords

Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/physiology; Amino Acid Sequence; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/physiology; Biological Transport; Cell Membrane/metabolism; Cytochrome c Group/biosynthesis; Cytochromes c2; Escherichia coli/metabolism; Escherichia coli Proteins; Membrane Transport Proteins; Molecular Sequence Data; Protein Precursors/metabolism; Rhodobacter capsulatus/metabolism

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