The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface.

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Abstract

We have addressed the mechanism of insertion of both transmembrane segments (TMs) of leader peptidase, a double-spanning protein, into the Escherichia coli inner membrane. Using photo-crosslinking, the first TM (H1) was shown to insert at a Sec-translocon/YidC interface in a fixed orientation. H1 lost its contacts with the Sec-translocon and gained access to lipids near YidC soon after complete exposure outside the ribosome. Following lipid integration, it moved away from the Sec/YidC insertion site. The second TM (H2) inserted and interacted with SecY and YidC in a similar transient fashion. The data are consistent with a linear integration model in which the TMs of polytopic inner membrane proteins move one by one from a Sec/YidC insertion site into the lipid bilayer. We propose that YidC assists the lipid partitioning of single TMs. © 2004 European Molecular Biology Organization.
Original languageEnglish
Pages (from-to)970-975
Number of pages6
JournalEMBO Reports
Volume5
DOIs
Publication statusPublished - 2004

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Lipid bilayers
Lipid Bilayers
Membranes
Lipids
Molecular biology
Escherichia coli Proteins
Ribosomes
Crosslinking
Escherichia coli
Molecular Biology
Linear Models
Membrane Proteins
type I signal peptidase
Proteins

Cite this

@article{32a989e37a604ab490fa1314c95c85f2,
title = "The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface.",
abstract = "We have addressed the mechanism of insertion of both transmembrane segments (TMs) of leader peptidase, a double-spanning protein, into the Escherichia coli inner membrane. Using photo-crosslinking, the first TM (H1) was shown to insert at a Sec-translocon/YidC interface in a fixed orientation. H1 lost its contacts with the Sec-translocon and gained access to lipids near YidC soon after complete exposure outside the ribosome. Following lipid integration, it moved away from the Sec/YidC insertion site. The second TM (H2) inserted and interacted with SecY and YidC in a similar transient fashion. The data are consistent with a linear integration model in which the TMs of polytopic inner membrane proteins move one by one from a Sec/YidC insertion site into the lipid bilayer. We propose that YidC assists the lipid partitioning of single TMs. {\circledC} 2004 European Molecular Biology Organization.",
author = "E.N.G. Houben and {ten Hagen-Jongman ten}, C.M. and J Brunner and B. Oudega and S. Luirink",
year = "2004",
doi = "10.1038/sj.embor.7400261",
language = "English",
volume = "5",
pages = "970--975",
journal = "EMBO Reports",
issn = "1469-221X",
publisher = "Nature Publishing Group",

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T1 - The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface.

AU - Houben, E.N.G.

AU - ten Hagen-Jongman ten, C.M.

AU - Brunner, J

AU - Oudega, B.

AU - Luirink, S.

PY - 2004

Y1 - 2004

N2 - We have addressed the mechanism of insertion of both transmembrane segments (TMs) of leader peptidase, a double-spanning protein, into the Escherichia coli inner membrane. Using photo-crosslinking, the first TM (H1) was shown to insert at a Sec-translocon/YidC interface in a fixed orientation. H1 lost its contacts with the Sec-translocon and gained access to lipids near YidC soon after complete exposure outside the ribosome. Following lipid integration, it moved away from the Sec/YidC insertion site. The second TM (H2) inserted and interacted with SecY and YidC in a similar transient fashion. The data are consistent with a linear integration model in which the TMs of polytopic inner membrane proteins move one by one from a Sec/YidC insertion site into the lipid bilayer. We propose that YidC assists the lipid partitioning of single TMs. © 2004 European Molecular Biology Organization.

AB - We have addressed the mechanism of insertion of both transmembrane segments (TMs) of leader peptidase, a double-spanning protein, into the Escherichia coli inner membrane. Using photo-crosslinking, the first TM (H1) was shown to insert at a Sec-translocon/YidC interface in a fixed orientation. H1 lost its contacts with the Sec-translocon and gained access to lipids near YidC soon after complete exposure outside the ribosome. Following lipid integration, it moved away from the Sec/YidC insertion site. The second TM (H2) inserted and interacted with SecY and YidC in a similar transient fashion. The data are consistent with a linear integration model in which the TMs of polytopic inner membrane proteins move one by one from a Sec/YidC insertion site into the lipid bilayer. We propose that YidC assists the lipid partitioning of single TMs. © 2004 European Molecular Biology Organization.

U2 - 10.1038/sj.embor.7400261

DO - 10.1038/sj.embor.7400261

M3 - Article

VL - 5

SP - 970

EP - 975

JO - EMBO Reports

JF - EMBO Reports

SN - 1469-221X

ER -