The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins.

Z. Yu, G.M. Koningstein, O.I. Pop, S. Luirink

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Escherichia coli YidC is a polytopic inner membrane protein that plays an essential and versatile role in the biogenesis of inner membrane proteins. YidC functions in Sec-dependent membrane insertion but acts also independently as a separate insertase for certain small membrane proteins. We have used a site-specific cross-linking approach to show that the conserved third transmembrane segment of YidC contacts the transmembrane domains of both nascent Sec-dependent and -independent substrates, indicating a generic recognition of insertion intermediates by YidC. Our data suggest that specific residues of the third YidC transmembrane segment α-helix is oriented toward the transmembrane domains of nascent inner membrane proteins that, in contrast, appear quite flexibly positioned at this stage in biogenesis. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.
LanguageEnglish
JournalJournal of Biological Chemistry
DOIs
Publication statusPublished - 2009

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Escherichia coli
Membrane Proteins
Membranes
Substrates

Bibliographical note

onderhanden werk

Cite this

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title = "The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins.",
abstract = "Escherichia coli YidC is a polytopic inner membrane protein that plays an essential and versatile role in the biogenesis of inner membrane proteins. YidC functions in Sec-dependent membrane insertion but acts also independently as a separate insertase for certain small membrane proteins. We have used a site-specific cross-linking approach to show that the conserved third transmembrane segment of YidC contacts the transmembrane domains of both nascent Sec-dependent and -independent substrates, indicating a generic recognition of insertion intermediates by YidC. Our data suggest that specific residues of the third YidC transmembrane segment α-helix is oriented toward the transmembrane domains of nascent inner membrane proteins that, in contrast, appear quite flexibly positioned at this stage in biogenesis. {\circledC} 2008 by The American Society for Biochemistry and Molecular Biology, Inc.",
author = "Z. Yu and G.M. Koningstein and O.I. Pop and S. Luirink",
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T1 - The conserved third transmembrane segment of YidC contacts nascent Escherichia coli inner membrane proteins.

AU - Yu, Z.

AU - Koningstein, G.M.

AU - Pop, O.I.

AU - Luirink, S.

N1 - onderhanden werk

PY - 2009

Y1 - 2009

N2 - Escherichia coli YidC is a polytopic inner membrane protein that plays an essential and versatile role in the biogenesis of inner membrane proteins. YidC functions in Sec-dependent membrane insertion but acts also independently as a separate insertase for certain small membrane proteins. We have used a site-specific cross-linking approach to show that the conserved third transmembrane segment of YidC contacts the transmembrane domains of both nascent Sec-dependent and -independent substrates, indicating a generic recognition of insertion intermediates by YidC. Our data suggest that specific residues of the third YidC transmembrane segment α-helix is oriented toward the transmembrane domains of nascent inner membrane proteins that, in contrast, appear quite flexibly positioned at this stage in biogenesis. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

AB - Escherichia coli YidC is a polytopic inner membrane protein that plays an essential and versatile role in the biogenesis of inner membrane proteins. YidC functions in Sec-dependent membrane insertion but acts also independently as a separate insertase for certain small membrane proteins. We have used a site-specific cross-linking approach to show that the conserved third transmembrane segment of YidC contacts the transmembrane domains of both nascent Sec-dependent and -independent substrates, indicating a generic recognition of insertion intermediates by YidC. Our data suggest that specific residues of the third YidC transmembrane segment α-helix is oriented toward the transmembrane domains of nascent inner membrane proteins that, in contrast, appear quite flexibly positioned at this stage in biogenesis. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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DO - 10.1074/jbc.M804344200

M3 - Article

JO - Journal of Biological Chemistry

T2 - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -