YidC and SecY Mediate Membrane Insertion of a Type I Transmembrane Domain

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 r...

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Bibliographic Details
Published in:The Journal of biological chemistry 2002-09, Vol.277 (39), p.35880-35886
Main Authors: Houben, Edith N.G., Urbanus, Malene L., van der Laan, Martin, ten Hagen-Jongman, Corinne M., Driessen, Arnold J.M., Brunner, Josef, Oudega, Bauke, Luirink, Joen
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
Cell Membrane - metabolism
Cross-Linking Reagents - pharmacology
Electrophoresis, Polyacrylamide Gel
Escherichia coli - metabolism
Escherichia coli Proteins - metabolism
Light
Lipid Metabolism
Membrane Proteins
Membrane Transport Proteins
Models, Biological
Phospholipases A - metabolism
Plasmids - metabolism
Precipitin Tests
Protein Binding
Protein Biosynthesis
Protein Structure, Tertiary
Ribosomes - metabolism
SEC Translocation Channels
Serine Endopeptidases - metabolism
Transcription, Genetic
Ultraviolet Rays
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M205556200