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Originally published In Press as doi:10.1074/jbc.M201022200 on March 13, 2002

J. Biol. Chem., Vol. 277, Issue 21, 18545-18551, May 24, 2002
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Interaction of the Eukaryotic Elongation Factor 1A with Newly Synthesized Polypeptides*

Yuka HotokezakaDagger §, Udo TöbbenDagger , Hitoshi HotokezakaDagger , Klaus van LeyenDagger , Birgitta BeatrixDagger ||, Deborah H. SmithDagger , Takashi Nakamura§, and Martin WiedmannDagger **

From the Dagger  Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, the § Department of Radiology and Cancer Biology and the  Department of Orthodontics, Nagasaki University School of Dentistry, 1-7-1 Sakamoto, Nagasaki 852-8588, Japan, and || Institut für Kristallographie, Freie Universität Berlin, 14195 Berlin, Germany

eEF1A, the eukaryotic homologue of bacterial elongation factor Tu, is a well characterized translation elongation factor responsible for delivering aminoacyl-tRNAs to the A-site at the ribosome. Here we show for the first time that eEF1A also associates with the nascent chain distal to the peptidyltransferase center. This is demonstrated for a variety of nascent chains of different lengths and sequences. Interestingly, unlike other ribosome-associated factors, eEF1A also interacts with polypeptides after their release from the ribosome. We demonstrate that eEF1A does not bind to correctly folded full-length proteins but interacts specifically with proteins that are unable to fold correctly in a cytosolic environment. This association was demonstrated both by photo-cross-linking and by a functional refolding assay.

* This work was supported in part by fellowships from the Deutsche Forschungsgemeinschaft (to B. B. and K. v. L.), the Sloan-Kettering Institute (to M. W.), National Institutes of Health Grant GM50920-01 (to M. W.), and a grant-in-aid from the Ministry of Education, Science, Sports and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed: Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Ave., New York, NY 10021. Tel.: 212-639-8549; Fax: 212-717-3604; E-mail: m-wiedmann@ski.mskcc.org.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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