cEF1A, 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 cEF1A 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, cEF1A also interacts with polypeptides after their release from the ribosome. We demonstrate that cEF1A 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.
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides. / Hotokezaka, Yuka; Bben, Udo Tö; Hotokezaka, Hitoshi; Van Leyen, Klaus; Beatrix, Birgitta; Smith, Deborah H.; Nakamura, Takashi; Wiedmann, Martin.In: Journal of Biological Chemistry, Vol. 277, No. 21, 24.05.2002, p. 18545-18551.
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