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Peptide-chain elongation in eukaryotes

C G Proud1

  • 1Department of Biochemistry, School of Medical Sciences, University of Bristol, UK.

Molecular Biology Reports
|May 1, 1994
PubMed
Summary
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Protein translation elongation involves eukaryotic elongation factors (eEF-1, eEF-2) and GTP. New models incorporate bacterial ribosome findings and fungal eEF-3, discussing factor roles in polypeptide synthesis and fidelity.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Translation elongation synthesizes polypeptide chains from mRNA.
  • Eukaryotic elongation requires at least two protein factors: eEF-1 and eEF-2, both GTP-dependent.
  • Fungal translation elongation additionally involves eEF-3.

Purpose of the Study:

  • To model eukaryotic translation elongation incorporating recent findings on bacterial ribosome tRNA binding sites.
  • To discuss the roles of eukaryotic elongation factors (eEF-1, eEF-2, eEF-3) in polypeptide synthesis and translational fidelity.
  • To review the structural and functional properties of these elongation factors, including their regulation.

Main Methods:

  • Incorporation of data on bacterial ribosome tRNA binding sites into a eukaryotic elongation model.

Related Experiment Videos

  • Cloning and sequencing of cDNAs for elongation factors.
  • Discussion of structural and functional properties, and regulatory mechanisms like phosphorylation.

    • Main Results:

    • A refined model of eukaryotic elongation considering hybrid tRNA binding sites.
    • Identification of potential roles for eEF-3 in translational accuracy.
    • Characterization of eEF-1 and eEF-2 regulation by phosphorylation.

    Conclusions:

    • Eukaryotic translation elongation is a complex process involving multiple GTP-dependent factors.
    • Structural and functional studies of elongation factors provide insights into polypeptide synthesis and fidelity.
    • Phosphorylation serves as a regulatory mechanism controlling elongation rates in vivo.