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M705430200v1
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Papers In Press, published online ahead of print August 28, 2007
J. Biol. Chem, 10.1074/jbc.M705430200
Submitted on July 2, 2007
Revised on August 27, 2007
Accepted on August 28, 2007

E. coli SRP-receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix

Richard Parlitz, Asa Eitan, Goran Stjepanovic, Liat Bahari, Gert Bange, Eitan Bibi, and Irmgard Sinning

Biological Chemistry, Weizmann Institute of Science, Rehovot 76100

Corresponding Author: e.bibi{at}weizmann.ac.il

Escherichia coli membrane protein biogenesis is mediated by the signal recognition particle (SRP) and its membrane-associated receptor (FtsY). Although crucial for its function, it is still not clear how FtsY interacts with the membrane. Analysis of the structure/function differences between severely truncated active (NG+1) and inactive (NG) mutants of FtsY now enabled us to identify an essential membrane-interacting determinant. Comparison of the 3D structures of the mutants, combined with site-directed mutagenesis, modeling, and liposome-binding assays, revealed that FtsY contains a conserved autonomous lipid-binding amphipathic a-helix at the N-terminal edge of the N domain. Deletion experiments showed that this helix is essential for FtsY function in vivo, thus offering, for the first time, clear evidence for the functionally important, physiologically relevant interaction of FtsY with lipids.


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S. Ravaud, G. Stjepanovic, K. Wild, and I. Sinning
The Crystal Structure of the Periplasmic Domain of the Escherichia coli Membrane Protein Insertase YidC Contains a Substrate Binding Cleft
J. Biol. Chem., April 4, 2008; 283(14): 9350 - 9358.
[Abstract] [Full Text] [PDF]


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