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YidC is required for the assembly of the MscL homopentameric pore
Author(s) -
Pop Ovidiu I.,
Soprova Zora,
Koningstein Gregory,
Scheffers DirkJan,
van Ulsen Peter,
Wickström David,
de Gier JanWillem,
Luirink Joen
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07188.x
Subject(s) - mechanosensitive channels , signal recognition particle , biogenesis , biophysics , inner membrane , chaperone (clinical) , membrane protein , biology , escherichia coli , membrane , ion channel , microbiology and biotechnology , chemistry , biochemistry , signal peptide , peptide sequence , receptor , medicine , pathology , gene
The mechanosensitive channel with large conductance (MscL) of Escherichia coli is formed by a homopentameric assembly of MscL proteins. Here, we describe MscL biogenesis as determined using in vivo approaches. Evidence is presented that MscL is targeted to the inner membrane via the signal recognition particle (SRP) pathway, and is inserted into the lipid bilayer independently of the Sec machinery. This is consistent with published data. Surprisingly, and in conflict with earlier data, YidC is not critical for membrane insertion of MscL. In the absence of YidC, assembly of the homopentameric MscL complex was strongly reduced, suggesting a late role for YidC in the biogenesis of MscL. The data are consistent with the view that YidC functions as a membrane‐based chaperone ‘module’ to facilitate assembly of a subset of protein complexes in the inner membrane of E. coli .