YidC and SecY mediate membrane insertion of a Type I transmembrane domain.

E.N.G. Houben, M.L. Urbanus, M. Van der laan, C.M. ten Hagen-Jongman ten, A.J.M. Driessen, J Brunner, B. Oudega, S. Luirink

Research output: Contribution to JournalArticleAcademic

Abstract

YidC has been identified recently as an evolutionary conserved factor that is involved in the integration of inner membrane proteins (IMPs) in Escherichia coli. The discovery of YidC has inspired the reevaluation of membrane protein assembly pathways in E. coli. In this study, we have analyzed the role of YidC in membrane integration of a widely used model IMP, leader peptidase (Lep). Site-directed photocross-linking experiments demonstrate that both YidC and SecY contact nascent Lep very early during biogenesis, at only 50-amino acid nascent chain length. At this length the first transmembrane domain (TM), which acquires a type I topology, is not even fully exposed outside the ribosome. The pattern of interactions appears dependent on the position of the cross-linking probe in the nascent chain. Upon elongation, nascent Lep remains close to YidC and comes into contact with lipids as well. Our results suggest a role for YidC in both the reception and lipid partitioning of type I TMs.
Original languageEnglish
Pages (from-to)35880-35886
Number of pages6
JournalJournal of Biological Chemistry
Volume277
DOIs
Publication statusPublished - 2002

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Membrane Proteins
Membranes
Escherichia coli
Lipids
Ribosomes
Chain length
Elongation
Topology
Amino Acids
type I signal peptidase
Experiments
lipid I

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title = "YidC and SecY mediate membrane insertion of a Type I transmembrane domain.",
abstract = "YidC has been identified recently as an evolutionary conserved factor that is involved in the integration of inner membrane proteins (IMPs) in Escherichia coli. The discovery of YidC has inspired the reevaluation of membrane protein assembly pathways in E. coli. In this study, we have analyzed the role of YidC in membrane integration of a widely used model IMP, leader peptidase (Lep). Site-directed photocross-linking experiments demonstrate that both YidC and SecY contact nascent Lep very early during biogenesis, at only 50-amino acid nascent chain length. At this length the first transmembrane domain (TM), which acquires a type I topology, is not even fully exposed outside the ribosome. The pattern of interactions appears dependent on the position of the cross-linking probe in the nascent chain. Upon elongation, nascent Lep remains close to YidC and comes into contact with lipids as well. Our results suggest a role for YidC in both the reception and lipid partitioning of type I TMs.",
author = "E.N.G. Houben and M.L. Urbanus and {Van der laan}, M. and {ten Hagen-Jongman ten}, C.M. and A.J.M. Driessen and J Brunner and B. Oudega and S. Luirink",
year = "2002",
doi = "10.1074/jbc.M205556200",
language = "English",
volume = "277",
pages = "35880--35886",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",

}

YidC and SecY mediate membrane insertion of a Type I transmembrane domain. / Houben, E.N.G.; Urbanus, M.L.; Van der laan, M.; ten Hagen-Jongman ten, C.M.; Driessen, A.J.M.; Brunner, J; Oudega, B.; Luirink, S.

In: Journal of Biological Chemistry, Vol. 277, 2002, p. 35880-35886.

Research output: Contribution to JournalArticleAcademic

TY - JOUR

T1 - YidC and SecY mediate membrane insertion of a Type I transmembrane domain.

AU - Houben, E.N.G.

AU - Urbanus, M.L.

AU - Van der laan, M.

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

AU - Driessen, A.J.M.

AU - Brunner, J

AU - Oudega, B.

AU - Luirink, S.

PY - 2002

Y1 - 2002

N2 - YidC has been identified recently as an evolutionary conserved factor that is involved in the integration of inner membrane proteins (IMPs) in Escherichia coli. The discovery of YidC has inspired the reevaluation of membrane protein assembly pathways in E. coli. In this study, we have analyzed the role of YidC in membrane integration of a widely used model IMP, leader peptidase (Lep). Site-directed photocross-linking experiments demonstrate that both YidC and SecY contact nascent Lep very early during biogenesis, at only 50-amino acid nascent chain length. At this length the first transmembrane domain (TM), which acquires a type I topology, is not even fully exposed outside the ribosome. The pattern of interactions appears dependent on the position of the cross-linking probe in the nascent chain. Upon elongation, nascent Lep remains close to YidC and comes into contact with lipids as well. Our results suggest a role for YidC in both the reception and lipid partitioning of type I TMs.

AB - YidC has been identified recently as an evolutionary conserved factor that is involved in the integration of inner membrane proteins (IMPs) in Escherichia coli. The discovery of YidC has inspired the reevaluation of membrane protein assembly pathways in E. coli. In this study, we have analyzed the role of YidC in membrane integration of a widely used model IMP, leader peptidase (Lep). Site-directed photocross-linking experiments demonstrate that both YidC and SecY contact nascent Lep very early during biogenesis, at only 50-amino acid nascent chain length. At this length the first transmembrane domain (TM), which acquires a type I topology, is not even fully exposed outside the ribosome. The pattern of interactions appears dependent on the position of the cross-linking probe in the nascent chain. Upon elongation, nascent Lep remains close to YidC and comes into contact with lipids as well. Our results suggest a role for YidC in both the reception and lipid partitioning of type I TMs.

U2 - 10.1074/jbc.M205556200

DO - 10.1074/jbc.M205556200

M3 - Article

VL - 277

SP - 35880

EP - 35886

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -