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Reconstitution of Sec‐dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG‐dependent manner
Author(s) -
van der Laan Martin,
Houben Edith N G,
Nouwen Nico,
Luirink Joen,
Driessen Arnold J M
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve106
Subject(s) - translocase , transmembrane protein , membrane protein , microbiology and biotechnology , membrane transport protein , transport protein , transmembrane domain , biology , inner membrane , escherichia coli , biophysics , membrane , chemistry , biochemistry , chromosomal translocation , mitochondrion , gene , receptor
The inner membrane protein YidC is associated with the preprotein translocase of Escherichia coli and contacts transmembrane segments of nascent inner membrane proteins during membrane insertion. YidC was purified to homogeneity and co‐reconstituted with the SecYEG complex. YidC had no effect on the SecA/SecYEG‐mediated translocation of the secretory protein proOmpA; however, using a crosslinking approach, the transmembrane segment of nascent FtsQ was found to gain access to YidC via SecY. These data indicate the functional reconstitution of the initial stages of YidC‐dependent membrane protein insertion via the SecYEG complex.