Linked Life Data

15210351

Source:http://linkedlifedata.com/resource/pubmed/id/15210351

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-6-22
pubmed:abstractText
In bacteria, the Sec-protein transport complex facilitates the passage of most secretory and membrane proteins across and into the plasma membrane. The core complex SecYEG forms the protein channel and engages either ribosomes or the ATPase SecA, which drive translocation of unfolded polypeptide chains through the complex and into the periplasmic space. Escherichia coli SecYEG forms dimers in membranes, but in detergent solution the population of these dimers is low. However, we find that stable dimers can be assembled by the addition of a monoclonal antibody. Normally, a stable SecYEG-SecA complex can only form on isolated membranes or on reconstituted proteo-liposomes. The antibody-stabilised SecYEG dimer binds one SecA molecule in detergent solution. In the presence of AMPPNP, a non-hydrolysable analogue of ATP, a complex forms containing one antibody and two each of SecYEG and SecA. SecYEG monomers or tetramers do not associate to a significant degree with SecA. The observed variability in the stoichiometry of SecYEG and SecA association and its nucleotide modulation may be important and necessary for the protein translocation reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 2004 Elsevier Ltd.
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
340
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
513-24
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules.
pubmed:affiliation
Institute für Biophysik, JWG-Universität, 60590 Frankfurt am Main, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't