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
SN - 0021-9258
VL - 277
SP - 35880
EP - 35886
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
ER -