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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
49
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pubmed:dateCreated |
2010-8-17
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pubmed:abstractText |
Many bacterial proteins, including most secretory proteins, are translocated across the plasma membrane by the interplay of the cytoplasmic SecA ATPase and a protein-conducting channel formed by the SecY complex. SecA catalyzes the sequential movement of polypeptide segments through the SecY channel. How SecA interacts with a broad range of polypeptide segments is unclear, but structural data raise the possibility that translocation substrates bind into a "clamp" of SecA. Here, we have used disulfide bridge cross-linking to test this hypothesis. To analyze polypeptide interactions of SecA during translocation, two cysteines were introduced into a translocation intermediate: one that cross-links to the SecY channel and the other one for cross-linking to a cysteine placed at various positions in SecA. Our results show that a translocating polypeptide is indeed captured inside SecA's clamp and moves in an extended conformation through the clamp into the SecY channel. These results define the polypeptide path during SecA-mediated protein translocation and suggest a mechanism by which ATP hydrolysis by SecA is used to move a polypeptide chain through the SecY channel.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-10085146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-10348856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-11101515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-12242434,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-12606717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-14661030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-15256599,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-15450979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-16148946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-16243836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-16828554,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-16989859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-17028145,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-17229438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-17418789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-18022369,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-18046402,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-1825804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-18602400,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-18923516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-18923526,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-18923527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-8087850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-8428582,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-8658133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933328-9450995
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/SecY protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Tetrahydrofolate Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/outer membrane protein A precursor...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
8
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pubmed:volume |
106
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20800-5
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pubmed:dateRevised |
2010-9-28
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pubmed:meshHeading |
pubmed-meshheading:19933328-Adenosine Triphosphatases,
pubmed-meshheading:19933328-Bacterial Outer Membrane Proteins,
pubmed-meshheading:19933328-Bacterial Proteins,
pubmed-meshheading:19933328-Cross-Linking Reagents,
pubmed-meshheading:19933328-Disulfides,
pubmed-meshheading:19933328-Escherichia coli,
pubmed-meshheading:19933328-Escherichia coli Proteins,
pubmed-meshheading:19933328-Membrane Transport Proteins,
pubmed-meshheading:19933328-Peptides,
pubmed-meshheading:19933328-Protein Binding,
pubmed-meshheading:19933328-Protein Interaction Mapping,
pubmed-meshheading:19933328-Protein Precursors,
pubmed-meshheading:19933328-Protein Structure, Secondary,
pubmed-meshheading:19933328-Protein Transport,
pubmed-meshheading:19933328-Tetrahydrofolate Dehydrogenase
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pubmed:year |
2009
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pubmed:articleTitle |
Mapping polypeptide interactions of the SecA ATPase during translocation.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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