Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-9-5
pubmed:abstractText
Recent evidence suggests that in Escherichia coli, SecA/SecB and signal recognition particle (SRP) are constituents of two different pathways targeting secretory and inner membrane proteins to the SecYEG translocon of the plasma membrane. We now show that a secY mutation, which compromises a functional SecY-SecA interaction, does not impair the SRP-mediated integration of polytopic inner membrane proteins. Furthermore, under conditions in which the translocation of secretory proteins is strictly dependent on SecG for assisting SecA, the absence of SecG still allows polytopic membrane proteins to integrate at the wild-type level. These results indicate that SRP-dependent integration and SecA/SecB-mediated translocation do not only represent two independent protein delivery systems, but also remain mechanistically distinct processes even at the level of the membrane where they engage different domains of SecY and different components of the translocon. In addition, the experimental setup used here enabled us to demonstrate that SRP-dependent integration of a multispanning protein into membrane vesicles leads to a biologically active enzyme.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-10085146, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-10397756, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-1447197, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-1633829, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-2254269, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-2654138, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-2848248, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-3881443, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-6390437, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-7929016, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8058823, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8175697, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8183945, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8521840, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8620539, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8647843, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8940120, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-8999901, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9008159, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9190818, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9393850, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9451453, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9575202, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9593737, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9701825, http://linkedlifedata.com/resource/pubmed/commentcorrection/10931878-9843943
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
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/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/OMPA outer membrane proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoenolpyruvate Sugar..., http://linkedlifedata.com/resource/pubmed/chemical/SecA protein, Bacteria, http://linkedlifedata.com/resource/pubmed/chemical/SecE protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/SecG protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/SecY protein, E coli, http://linkedlifedata.com/resource/pubmed/chemical/Signal Recognition Particle, http://linkedlifedata.com/resource/pubmed/chemical/mannitol PTS permease, E coli
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
150
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
689-94
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Dissecting the translocase and integrase functions of the Escherichia coli SecYEG translocon.
pubmed:affiliation
Institut für Biochemie und Molekularbiologie, Universität Freiburg, 79104 Freiburg, Germany. kochhans@ruf.uni-freiburg.de
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't