title: Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides.
abstract: 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.
authors.affiliation: Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
authors.forename: Yuka
authors.initials: Y
authors.lastname: Hotokezaka
authors.forename: Udo
authors.initials: U
authors.lastname: Tobben
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Hotokezaka
authors.forename: Klaus
authors.initials: K
authors.lastname: Van Leyen
authors.forename: Birgitta
authors.initials: B
authors.lastname: Beatrix
authors.forename: Deborah H
authors.initials: DH
authors.lastname: Smith
authors.forename: Takashi
authors.initials: T
authors.lastname: Nakamura
authors.forename: Martin
authors.initials: M
authors.lastname: Wiedmann
mesh_terms: D000818:Animals; D001517:Coleoptera / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D020648:Peptide Elongation Factor 1 / Q000378:metabolism* / Q000502:physiology; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding
chemical_list: D020648:Peptide Elongation Factor 1; D010455:Peptides