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PMID: 7969104 Published · ppublish English Journal Article Review

Peptide-chain elongation in eukaryotes.

Molecular biology reports ·Vol. 19 ·No. 3 ·1994-05-00 ·Pages 161-70

Proud CG

Abstract

The elongation phase of translation leads to the decoding of the mRNA and the synthesis of the corresponding polypeptide chain. In most eukaryotes, two distinct protein elongation factors (eEF-1 and eEF-2) are required for elongation. Each is active as a complex with GTP. eEF-1 is a multimer and mediates the binding of the cognate aminoacyl-tRNA to the ribosome, while eEF-2, a monomer, catalyses the movement of the ribosome relative to the mRNA. Recent work showing that bacterial ribosomes possess three sites for tRNA binding and that during elongation tRNAs may occupy 'hybrid' sites is incorporated into a model of eukaryotic elongation. In fungi, elongation also requires a third factor, eEF-3. A number of mechanisms exist to promote the accuracy or 'fidelity' of elongation: eEF-3 may play a role here. cDNAs for this and the other elongation factors have been cloned and sequenced, and the structural and functional properties of the elongation factors are discussed. eEF-1 and eEF-2 can be regulated by phosphorylation, and this may serve to control rates of elongation in vivo.

MeSH Terms
Animals Eukaryotic Cells/metabolism Fungal Proteins Humans Models, Biological Peptide Chain Elongation, Translational Peptide Elongation Factor 1 Peptide Elongation Factor 2 Peptide Elongation Factors/metabolism Protein Biosynthesis RNA, Transfer, Amino Acyl/metabolism Ribosomes/metabolism Saccharomyces cerevisiae Proteins
Chemicals
Fungal Proteins Peptide Elongation Factor 1 Peptide Elongation Factor 2 Peptide Elongation Factors RNA, Transfer, Amino Acyl Saccharomyces cerevisiae Proteins YEF3 protein, S cerevisiae
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Proud C G
Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.
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Article Info
Journal
Molecular biology reports
Abbr.
Mol Biol Rep
ISSN
0301-4851
DOI
10.1007/BF00986958
Published
1994-05-00
Pages
161-70
Language
English
Region
Netherlands
NLM ID
0403234
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00986958 View journal details
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