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Review
. 2003 Jan 15;22(2):175-82.
doi: 10.1093/emboj/cdg017.

Termination of translation: interplay of mRNA, rRNAs and release factors?

Lev Kisselev  1 , Måns Ehrenberg, Ludmila Frolova
Affiliations
Review

Termination of translation: interplay of mRNA, rRNAs and release factors?

Lev Kisselev et al. EMBO J. .

Abstract

Termination of translation in eukaryotes has focused recently on functional anatomy of polypeptide chain release factor, eRF1, by using a variety of different approaches. The tight correlation between the domain structure and different functions of eRF1 has been revealed. Independently, the role of prokaryotic RF1/2 in GTPase activity of RF3 has been deciphered, as well as RF3 function itself.

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Figures

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Fig. 1. Functional anatomy of eRF1. Proposed locations of the eRF1 functional sites.
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Fig. 2. Two minidomains of the N domain of class-1 eRF1 containing functionally essential amino acid residues in the NIKS and Y-x-C-x-x-x-F motifs. Numbering is as in human eRF1. Sequences are taken from the Swiss Prot database.
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Fig. 3. The mechanism of action of RF3 in bacteria. (A) The ribosome in the pre-termination state with peptidyl-tRNA in the P-site and a class-1 release factor (RF) in the A-site. (B) The ribosome in the post-termination state with deacylated tRNA in the P-site and a RF in the A-site. (C and D) The ribosome with tRNA as in (B) and an RF in complex with RF3 in its guanine nucleotide-free state. (E) The ribosome with tRNA as in (B) in complex with RF3 in its GTP conformation. (F) The ribosome with tRNA as in (B) now free from both RF2 and RF3.
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References

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