Translational termination comes of age.
Translational termination has been a largely ignored aspect of protein synthesis for many years. However, the recent identification of new release-factor genes, the mapping of release-factor functional sites and in vitro reconstitution experiments have provided a deeper understanding of the termination mechanism. In addition, protein-protein interactions among release factors and with other proteins have been revealed. The three-dimensional structures of a prokaryotic ribosome recycling factor and eukaryotic release factor 1 (eRF1) mimic the shape of transfer RNA, indicating that they bind to the same ribosomal site. Post-termination events in bacteria have been clarified, linking termination, ribosomal recycling and translation initiation.
Kisselev
L L
LL
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilova, 117984, Moscow, Russia. kissel@imb.ac.ru
Buckingham
R H
RH
D020816:Amino Acid Motifs; D020558:GTP Phosphohydrolases / Q000378:metabolism; D010443:Peptide Chain Termination, Translational / Q000502:physiology*; D010454:Peptide Termination Factors / Q000737:chemistry* / Q000378:metabolism*; D012270:Ribosomes / Q000235:genetics / Q000378:metabolism*
D010454:Peptide Termination Factors; C087971:peptide-chain-release factor 3; D020558:GTP Phosphohydrolases