Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides

Yuka Hotokezaka, Udo Tö Bben, Hitoshi Hotokezaka, Klaus Van Leyen, Birgitta Beatrix, Deborah H. Smith, Takashi Nakamura, Martin Wiedmann

Research output: Contribution to journalArticle

60 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)18545-18551
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number21
DOIs
StatePublished - May 24 2002

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Hotokezaka, Y., Bben, U. T., Hotokezaka, H., Van Leyen, K., Beatrix, B., Smith, D. H., Nakamura, T., & Wiedmann, M. (2002). Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides. Journal of Biological Chemistry, 277(21), 18545-18551. https://doi.org/10.1074/jbc.M201022200