Structural basis for ArfA–RF2-mediated translation termination on mRNAs lacking stop codons

Nature ◽  
2016 ◽  
Vol 541 (7638) ◽  
pp. 546-549 ◽  
Author(s):  
Paul Huter ◽  
Claudia Müller ◽  
Bertrand Beckert ◽  
Stefan Arenz ◽  
Otto Berninghausen ◽  
...  
Keyword(s):  
Translation Termination ◽  
Structural Basis ◽  
Stop Codons

scholarly journals Structural basis for translation termination by archaeal RF1 and GTP-bound EF1α complex

2012 ◽  
Vol 40 (18) ◽  
pp. 9319-9328 ◽  
Author(s):  
Kan Kobayashi ◽  
Kazuki Saito ◽  
Ryuichiro Ishitani ◽  
Koichi Ito ◽  
Osamu Nureki
Keyword(s):  
Translation Termination ◽  
Structural Basis

Termination of translation in eukaryotes

1995 ◽  
Vol 73 (11-12) ◽  
pp. 1079-1086 ◽  
Author(s):  
Lev L. Kisselev ◽  
Lyudmila Yu. Frolova
Keyword(s):  
Polypeptide Chain ◽  
Translation Termination ◽  
Protein Biosynthesis ◽  
High Rate ◽  
Vitro Assay ◽  
Binding Motifs ◽  
Stop Codons ◽  
Release Factors ◽  
Terminal Domain ◽  
Gtp Binding

Termination of translation is governed in ribosomes by polypeptide chain release factors (pRF and eRF in prokaryotes and eukaryotes, respectively). In prokaryotes, three pRF have been identified and sequenced, while in eukaryotes, only a single eRF has been identified to date. Recently, we have characterized a highly conserved protein family called eRF1. At least, human and Xenopus laevis proteins from this family are active as eRFs in the in vitro assay with any of the three stop codons. No structural similarity has been revealed between any of the three pRFs and eRF1 family. Furthermore, GTP-binding motifs have not been revealed, although translation termination in eukaryotes is a GTP-dependent process. We have demonstrated that in eukaryotes a second eRF exists in addition to eRF1, called eRF3. The eRF3 family has two features in common: presence of GTP-binding motifs and high conservation of the C-terminal domain structure. The C-terminal domain of the X. laevis eRF3 has no RF activity although it stimulates the eRF1 activity considerably at low concentration of the stop codons, conferring GTP dependence to the termination reaction. Without eRF3, the eRF1 activity is entirely GTP independent. Some features of X. laevis eRF3 (C-terminal domain) resemble those of pRF3. The newly identified eRF1 and eRF3 are structurally conserved and distinct from the respective pRF1/2 and pRF3 proteins, pointing to the possibility of different evolution of translation termination machinery in prokaryotes and eukaryotes. Bipartition of the translation termination apparatus probably provides high rate and accuracy of translation termination.Key words: higher eukaryotic polypeptide chain release factors, translation termination, protein biosynthesis.

Reassigning stop codons via translation termination: How a few eukaryotes broke the dogma

BioEssays ◽  
2016 ◽  
Vol 39 (3) ◽  
pp. 1600213 ◽  
Author(s):  
Elena Alkalaeva ◽  
Tatiana Mikhailova
Keyword(s):  
Translation Termination ◽  
Stop Codons

scholarly journals Distinct Paths To Stop Codon Reassignment by the Variant-Code Organisms Tetrahymena and Euplotes

2006 ◽  
Vol 26 (2) ◽  
pp. 438-447 ◽  
Author(s):  
Joe Salas-Marco ◽  
Hua Fan-Minogue ◽  
Adam K. Kallmeyer ◽  
Lawrence A. Klobutcher ◽  
Philip J. Farabaugh ◽  
...  
Keyword(s):  
Stop Codon ◽  
Translation Termination ◽  
Yeast Cells ◽  
Universal Genetic Code ◽  
Stop Codons ◽  
Codon Recognition ◽  
Ciliate Species ◽  
Stop Codon Recognition ◽  
Euplotes Octocarinatus

ABSTRACT The reassignment of stop codons is common among many ciliate species. For example, Tetrahymena species recognize only UGA as a stop codon, while Euplotes species recognize only UAA and UAG as stop codons. Recent studies have shown that domain 1 of the translation termination factor eRF1 mediates stop codon recognition. While it is commonly assumed that changes in domain 1 of ciliate eRF1s are responsible for altered stop codon recognition, this has never been demonstrated in vivo. To carry out such an analysis, we made hybrid proteins that contained eRF1 domain 1 from either Tetrahymena thermophila or Euplotes octocarinatus fused to eRF1 domains 2 and 3 from Saccharomyces cerevisiae. We found that the Tetrahymena hybrid eRF1 efficiently terminated at all three stop codons when expressed in yeast cells, indicating that domain 1 is not the sole determinant of stop codon recognition in Tetrahymena species. In contrast, the Euplotes hybrid facilitated efficient translation termination at UAA and UAG codons but not at the UGA codon. Together, these results indicate that while domain 1 facilitates stop codon recognition, other factors can influence this process. Our findings also indicate that these two ciliate species used distinct approaches to diverge from the universal genetic code.

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