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J. Biol. Chem., Vol. 282, Issue 44, 32176-32184, November 2, 2007

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Escherichia coli Signal Recognition Particle Receptor FtsY Contains an Essential and Autonomous Membrane-binding Amphipathic Helix^*

Richard Parlitz¹, Asa Eitan¹, Goran Stjepanovic, Liat Bahari, Gert Bange, Eitan Bibi², and Irmgard Sinning³

From the Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg 69120, Germany and the Department of Biological Chemistry, The Weizmann Institute of Science, P. O. Box 26, Rehovot 76100, Israel

Escherichia coli membrane protein biogenesis is mediated by a signal recognition particle 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 enabled us to identify an essential membrane-interacting determinant. Comparison of the three-dimensional structures of the mutants, combined with site-directed mutagenesis, modeling, and liposome-binding assays, revealed that FtsY contains a conserved autonomous lipid-binding amphipathic -helix at the N-terminal end 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.

Received for publication, July 2, 2007 , and in revised form, August 27, 2007.

The atomic coordinates and structure factors (code 2QY9) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the German-Israeli Foundation for Scientific Research and Development (to I. S. and E. B.), by the Israel Science Foundation and the Dr. Josef Cohn MINERVA Center for Biomembrane Research (to E. B.), and by the Deutsche Forschungsgemeinschaft (Grant SFB 638 and Graduate Program Grant 1188 to I. S.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S2.

¹ These authors contributed equally to this work.

² To whom correspondence may be addressed: Tel.: 972-8-934-3464; Fax: 972-8-934-4118; E-mail: e.bibi{at}weizmann.ac.il. ³ To whom correspondence may be addressed: Tel.: 49-6221-54-4781; Fax: 49-6221-54-4790; E-mail: Irmi.Sinning{at}bzh.uni-heidelberg.de.

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