Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides Journal Article
| Authors: | Hotokezaka, Y.; Tobben, U.; Hotokezaka, H.; Van Leyen, K.; Beatrix, B.; Smith, D. H.; Nakamura, T.; Wiedmann, M. |
| Article Title: | Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides |
| 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. |
| Keywords: | nonhuman; animals; protein binding; bacteria (microorganisms); rna; protein purification; eukaryota; escherichia coli; peptides; plasmid; protein folding; biochemistry; enzyme assay; enzymes; synthesis (chemical); peptide synthesis; assays; electrophoresis, polyacrylamide gel; beetles; polypeptides; polypeptide; ribosome; cross linking; priority journal; article; bacterial elongation factor; elongation factor 1alpha; peptide elongation factor 1 |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 277 |
| Issue: | 21 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2002-05-24 |
| Start Page: | 18545 |
| End Page: | 18551 |
| Language: | English |
| DOI: | 10.1074/jbc.M201022200 |
| PUBMED: | 11893745 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 14 November 2014 -- Source: Scopus |
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