PMID:10698927: Difference between revisions

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<span style = 'font-size: large'> '''Manting, EH, van Der Does, C, Remigy, H, Engel, A and Driessen, AJ'''  (2000) SecYEG assembles into a tetramer to form the active protein translocation channel.''EMBO J.'' '''19''':852-61</span>
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|{{TableHeadingColor}} |'''Abstract''' || Translocase mediates preprotein translocation across the Escherichia coli inner membrane. It consists of the SecYEG integral membrane protein complex and the peripheral ATPase SecA. Here we show by functional assays, negative-stain electron microscopy and mass measurements with the scanning transmission microscope that SecA recruits SecYEG complexes to form the active translocation channel. The active assembly of SecYEG has a side length of 10.5 nm and exhibits an approximately 5 nm central cavity. The mass and structure of this SecYEG as well as the subunit stoichiometry of SecA and SecY in a soluble translocase-precursor complex reveal that translocase consists of the SecA homodimer and four SecYEG complexes.
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'''Manting, EH, van Der Does, C, Remigy, H, Engel, A and Driessen, AJ'''  (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. ''EMBO J.'' '''19''':852-61
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!align=left  |Abstract
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Translocase mediates preprotein translocation across the Escherichia coli inner membrane. It consists of the SecYEG integral membrane protein complex and the peripheral ATPase SecA. Here we show by functional assays, negative-stain electron microscopy and mass measurements with the scanning transmission microscope that SecA recruits SecYEG complexes to form the active translocation channel. The active assembly of SecYEG has a side length of 10.5 nm and exhibits an approximately 5 nm central cavity. The mass and structure of this SecYEG as well as the subunit stoichiometry of SecA and SecY in a soluble translocase-precursor complex reveal that translocase consists of the SecA homodimer and four SecYEG complexes.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10698927 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC305625 PMC305625]
Online version:[http://dx.doi.org/10.1093/emboj/19.5.852 10.1093/emboj/19.5.852]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10698927 PubMed]
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Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Dimerization; Escherichia coli; Escherichia coli Proteins; Mass Spectrometry; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Protein Binding
 
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Latest revision as of 04:11, 15 September 2013

Citation

Manting, EH, van Der Does, C, Remigy, H, Engel, A and Driessen, AJ (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19:852-61

Abstract

Translocase mediates preprotein translocation across the Escherichia coli inner membrane. It consists of the SecYEG integral membrane protein complex and the peripheral ATPase SecA. Here we show by functional assays, negative-stain electron microscopy and mass measurements with the scanning transmission microscope that SecA recruits SecYEG complexes to form the active translocation channel. The active assembly of SecYEG has a side length of 10.5 nm and exhibits an approximately 5 nm central cavity. The mass and structure of this SecYEG as well as the subunit stoichiometry of SecA and SecY in a soluble translocase-precursor complex reveal that translocase consists of the SecA homodimer and four SecYEG complexes.

Links

PubMed PMC305625 Online version:10.1093/emboj/19.5.852

Keywords

Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Dimerization; Escherichia coli; Escherichia coli Proteins; Mass Spectrometry; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Protein Binding

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