YidC is required for the assembly of the MscL homopentameric pore.

O.I. Pop, Z. Soprova, G.M. Koningstein, D.J. Scheffers, J.P. van Ulsen, D. Wickstrom, J.-W. de Gier, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

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. © 2009 FEBS.
Original languageEnglish
Pages (from-to)4891-4899
JournalThe FEBS Journal
Volume276
Issue number17
DOIs
Publication statusPublished - 2009

Fingerprint

Membranes
Escherichia coli
Signal Recognition Particle
Lipid bilayers
Lipid Bilayers
Machinery
Proteins

Cite this

Pop, O.I. ; Soprova, Z. ; Koningstein, G.M. ; Scheffers, D.J. ; van Ulsen, J.P. ; Wickstrom, D. ; de Gier, J.-W. ; Luirink, S. / YidC is required for the assembly of the MscL homopentameric pore. In: The FEBS Journal. 2009 ; Vol. 276, No. 17. pp. 4891-4899.
@article{85d3989f23fe4b61b74e494c2e59157e,
title = "YidC is required for the assembly of the MscL homopentameric pore.",
abstract = "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. {\circledC} 2009 FEBS.",
author = "O.I. Pop and Z. Soprova and G.M. Koningstein and D.J. Scheffers and {van Ulsen}, J.P. and D. Wickstrom and {de Gier}, J.-W. and S. Luirink",
year = "2009",
doi = "10.1111/j.1742-4658.2009.07188.x",
language = "English",
volume = "276",
pages = "4891--4899",
journal = "The FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "17",

}

YidC is required for the assembly of the MscL homopentameric pore. / Pop, O.I.; Soprova, Z.; Koningstein, G.M.; Scheffers, D.J.; van Ulsen, J.P.; Wickstrom, D.; de Gier, J.-W.; Luirink, S.

In: The FEBS Journal, Vol. 276, No. 17, 2009, p. 4891-4899.

Research output: Contribution to JournalArticleAcademicpeer-review

TY - JOUR

T1 - YidC is required for the assembly of the MscL homopentameric pore.

AU - Pop, O.I.

AU - Soprova, Z.

AU - Koningstein, G.M.

AU - Scheffers, D.J.

AU - van Ulsen, J.P.

AU - Wickstrom, D.

AU - de Gier, J.-W.

AU - Luirink, S.

PY - 2009

Y1 - 2009

N2 - 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. © 2009 FEBS.

AB - 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. © 2009 FEBS.

U2 - 10.1111/j.1742-4658.2009.07188.x

DO - 10.1111/j.1742-4658.2009.07188.x

M3 - Article

VL - 276

SP - 4891

EP - 4899

JO - The FEBS Journal

JF - The FEBS Journal

SN - 1742-464X

IS - 17

ER -