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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
24
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pubmed:dateCreated |
2003-6-17
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pubmed:abstractText |
Integral membrane components SecY, SecE, and SecG of protein translocase form a complex in the Escherichia coli plasma membrane. To characterize subunit interactions of the SecYEG complex, a series of SecY variants having a single cysteine in its cytoplasmic (C1-C6) or periplasmic (P1-P5) domain were subjected to site-specific cross-linking experiments using bifunctional agents with thiol-amine reactivity. Experiments using inverted membrane vesicles revealed specific cross-linkings between a cysteine residue placed in the C2 or C3 domain of SecY and the cytosolic lysine (Lys26) near the first transmembrane segment of SecG. These SecY Cys residues also formed a disulfide bond with an engineered cytosolic cysteine at position 28 of SecG. Thus, the C2-C3 region of SecY is in the proximity of the N-terminal half of the SecG cytoplasmic loop. Experiments using spheroplasts revealed the physical proximity of P2 (SecY) and the C-terminal periplasmic region of SecG. In addition, mutations in secG were isolated as suppressors against a cold-sensitive mutation (secY104) affecting the TM4-C3 boundary of SecY. These results collectively suggest that a C2-TM3-P2-TM4-C3 region of SecY serves as an interface with SecG.
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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/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Maleimides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SecG protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/SecY protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7434-41
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12809499-Amino Acid Sequence,
pubmed-meshheading:12809499-Amino Acid Substitution,
pubmed-meshheading:12809499-Cross-Linking Reagents,
pubmed-meshheading:12809499-Cysteine,
pubmed-meshheading:12809499-Cytoplasm,
pubmed-meshheading:12809499-Disulfides,
pubmed-meshheading:12809499-Escherichia coli,
pubmed-meshheading:12809499-Escherichia coli Proteins,
pubmed-meshheading:12809499-Immunoblotting,
pubmed-meshheading:12809499-Maleimides,
pubmed-meshheading:12809499-Membrane Proteins,
pubmed-meshheading:12809499-Molecular Sequence Data,
pubmed-meshheading:12809499-Mutagenesis, Site-Directed,
pubmed-meshheading:12809499-Mutation,
pubmed-meshheading:12809499-Plasmids,
pubmed-meshheading:12809499-Protein Conformation,
pubmed-meshheading:12809499-Protein Subunits,
pubmed-meshheading:12809499-Recombinant Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
Nearest neighbor analysis of the SecYEG complex. 1. Identification of a SecY-SecG interface.
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pubmed:affiliation |
Institute for Virus Research, Kyoto University, Kyoto 606-8507, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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