Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides.
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.
Hotokezaka
Yuka
Y
Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
Tobben
Udo
U
Hotokezaka
Hitoshi
H
Van Leyen
Klaus
K
Beatrix
Birgitta
B
Smith
Deborah H
DH
Nakamura
Takashi
T
Wiedmann
Martin
M
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
D020648:Peptide Elongation Factor 1; D010455:Peptides