Termination of Protein-Synthesis

Tuite, Mick F. and Stansfield, Ian (1994) Termination of Protein-Synthesis. Molecular Biology Reports, 19 (3). pp. 171-181. ISSN 0301-4851. (The full text of this publication is not available from this repository)

The full text of this publication is not available from this repository. (Contact us about this Publication)

Abstract

One of three mRNA codons - UAA, UAG and UGA - is used to signal to the elongating ribosome that translation should be terminated at this point. Upon the arrival of the stop codon at the ribosomal acceptor(A)-site, a protein release factor (RF) binds to the ribosome resulting in the peptidyl transferase centre of the ribosome switching to a hydrolytic function to remove the completed polypeptide chain from the peptidyl-tRNA bound at the adjacent ribosomal peptidyl(P)-site. In this review recent advances in our understanding of the mechanism of termination in the bacterium Escherichia coil will be summarised, paying particular attention to the roles of 16S ribosomal RNA and the release factors RF-1, RF-2 and RF-3 in stop codon recognition. Our understanding of the translation termination process in eukaryotes is much more rudimentary with the identity of the single eukaryotic release factor (eRF) still remaining elusive. Finally, several examples of how the termination mechanism can be subverted either to expand the genetic code (e.g. selenocysteine insertion at UGA codons) or to regulate the expression of mammalian retroviral or plant viral genomes will be discussed.

Item Type: Article
Uncontrolled keywords: TRANSLATION; PROTEIN SYNTHESIS; TERMINATION; RELEASE FACTORS; STOP CODONS; NONSENSE SUPPRESSION
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: P. Ogbuji
Date Deposited: 10 Jun 2009 07:40
Last Modified: 10 Jun 2014 12:58
Resource URI: http://kar.kent.ac.uk/id/eprint/20079 (The current URI for this page, for reference purposes)
  • Depositors only (login required):