PMID: 16637272Apr 28, 2006Paper

Influence of individual domains of the translation termination factor eRF1 on induction of the GTPase activity of the translation termination factor eRF3

Molekuliarnaia biologiia
V I DubovaiaL L Kiselev

Abstract

Translation termination in eukaryotes is governed by two proteins, belonging to the class-1 (eRF1) and class-2 (eRF3) polypeptide release factors. eRF3 catalyzes hydrolysis of GTP to GDP and inorganic phosphate in the ribosome in the absence of mRNA, tRNA, aminoacyl-tRNA and peptidyl-tRNA but needs the presence of eRF1. It's known that eRF1 and eRF3 interact with each other in vitro and in vivo via their C-terminal regions. eRF1 consists of three domains - N, M, and C. In this study we examined the influence of individual domains of the human eRF1 on induction of the human eRF3 GTPase activity in the ribosome in vitro. It was shown that none of the N-, M-, C- and NM-domains induces eRF3 GTPase activity in presence of the ribosomes. MC-domain does induce GTPase activity of eRF3 but four times less efficient than full-length eRF1, therefore, MC-domain (and very likely M-domain) binds to the ribosome in the presence of eRF3. Based on these data and taking into account the data available in literature, a conclusion was drawn that the N domain of eRF1 is not essential for eRF1-dependent induction of the eRF3 GTPase activity. A working hypothesis is formulated, postulating that GTPase activity eRF3 during the translation termination ...Continue Reading

References

May 1, 1997·Molecular Microbiology·R H BuckinghamL Kisselev
Apr 3, 2001·Science·M M YusupovH F Noller
Mar 23, 2002·Cell·V Ramakrishnan
Jan 7, 2003·The EMBO Journal·Lev KisselevLudmila Frolova
Feb 11, 2003·Trends in Biochemical Sciences·Yoshikazu Nakamura, Koichi Ito

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Citations

Jun 19, 2007·Proceedings of the National Academy of Sciences of the United States of America·Sergey LekomtsevLev Kisselev
Mar 6, 2008·Molekuliarnaia biologiia·S A LekomtsevL L Kiselev
Feb 28, 2013·The Journal of Physical Chemistry. B·Carles Acosta-SilvaAntoni Oliva
Apr 18, 2019·The Journal of Biological Chemistry·Alexandr IvanovElena Alkalaeva

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