C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction - PubMed (original) (raw)

C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction

T I Merkulova et al. FEBS Lett. 1999.

Free article

Abstract

At the termination step of protein synthesis, hydrolysis of the peptidyl-tRNA is jointly catalysed at the ribosome by the termination codon and the polypeptide release factor (eRF1 in eukaryotes). eRF1 forms in vivo and in vitro a stable complex with release factor eRF3, an eRF1-dependent and ribosome-dependent GTPase. The role of the eRF1-eRF3 complex in translation remains unclear. We have undertaken a systematic analysis of the interactions between the human eRF1 and eRF3 employing a yeast two-hybrid assay. We show that the N-terminal parts of eRF1 (positions 1-280) and of eRF3 (positions 1477) are either not involved or non-essential for binding. Two regions in each factor are critical for mutual binding: positions 478-530 and 628-637 of eRF3 and positions 281-305 and 411-415 of eRF1. The GTP binding domain of eRF3 is not involved in complex formation with eRF1. The GILRY pentamer (positions 411-415) conserved in eukaryotes and archaebacteria is critical for eRF1's ability to stimulate eRF3 GTPase. The human eRF1 lacking 22 C-terminal amino acids remains active as a release factor and promotes an eRF3 GTPase activity whereas C-terminally truncated eRF3 is inactive as a GTPase.

PubMed Disclaimer

Cited by

Termination of translation: interplay of mRNA, rRNAs and release factors?
Kisselev L, Ehrenberg M, Frolova L. Kisselev L, et al. EMBO J. 2003 Jan 15;22(2):175-82. doi: 10.1093/emboj/cdg017. EMBO J. 2003. PMID: 12514123 Free PMC article. Review.
Two-step model of stop codon recognition by eukaryotic release factor eRF1.
Kryuchkova P, Grishin A, Eliseev B, Karyagina A, Frolova L, Alkalaeva E. Kryuchkova P, et al. Nucleic Acids Res. 2013 Apr;41(8):4573-86. doi: 10.1093/nar/gkt113. Epub 2013 Feb 23. Nucleic Acids Res. 2013. PMID: 23435318 Free PMC article.
Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3.
Beißel C, Neumann B, Uhse S, Hampe I, Karki P, Krebber H. Beißel C, et al. Nucleic Acids Res. 2019 May 21;47(9):4798-4813. doi: 10.1093/nar/gkz177. Nucleic Acids Res. 2019. PMID: 30873535 Free PMC article.
Connection between stop codon reassignment and frequent use of shifty stop frameshifting.
Vallabhaneni H, Fan-Minogue H, Bedwell DM, Farabaugh PJ. Vallabhaneni H, et al. RNA. 2009 May;15(5):889-97. doi: 10.1261/rna.1508109. Epub 2009 Mar 27. RNA. 2009. PMID: 19329535 Free PMC article.
NMR solution structure and function of the C-terminal domain of eukaryotic class 1 polypeptide chain release factor.
Mantsyzov AB, Ivanova EV, Birdsall B, Alkalaeva EZ, Kryuchkova PN, Kelly G, Frolova LY, Polshakov VI. Mantsyzov AB, et al. FEBS J. 2010 Jun;277(12):2611-27. doi: 10.1111/j.1742-464X.2010.07672.x. FEBS J. 2010. PMID: 20553496 Free PMC article.

C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction - PubMed (original) (raw)