Binding of the 5′-Triphosphate End of mRNA to the γ-Subunit of Translation Initiation Factor 2 of the Crenarchaeon Sulfolobus solfataricus. Issue 19 (25th September 2015)

• Record Type: Journal Article
• Authors: Arkhipova, Valentina; Stolboushkina, Elena; Kravchenko, Olesya; Kljashtorny, Vladislav; Gabdulkhakov, Azat; Garber, Maria; Nikonov, Stanislav; Märtens, Birgit; Bläsi, Udo; Nikonov, Oleg
• Is Part Of: Journal of molecular biology. Volume 427:Issue 19(2015:Oct. 01)
• Page Start: 3086
• Page End: 3095
• Publication Date: 2015-09-25
• Subjects: SPR surface plasmon resonance -- MD molecular dynamics; crystal structure -- archaea -- a/eIF2γ -- mRNA -- GTP; Molecular biology -- Periodicals; Biology -- Periodicals; Biochemistry -- Periodicals; Bacteriology -- Periodicals; Molecular Biology -- Periodicals; Biochemistry -- Periodicals; Biologie moléculaire -- Périodiques; Biologie -- Périodiques; Biochimie -- Périodiques; Moleculaire biologie; Biochemistry; Biology; Molecular biology; Periodicals; 572.805
• DOI: 10.1016/j.jmb.2015.07.020
• Languages: English
• ISSNs: 0022-2836

Abstract

Abstract: The heterotrimeric archaeal IF2 orthologue of eukaryotic translation initiation factor 2 consists of the α-subunit, β-subunit and γ-subunit. Previous studies showed that the γ-subunit of aIF2, besides its central role in Met-tRNAi binding, has an additional function: it binds to the 5′-triphosphorylated end of mRNA and protects its 5′-part from degradation. Competition studies with nucleotides and mRNA, as well as structural and kinetic analyses of aIF2γ mutants, strongly implicate the canonical GTP/GDP-binding pocket in binding to the 5′-triphosphate end of mRNAs. The biological implication of these findings is being discussed. Graphical Abstract: Highlights: 5′-end GTP of mRNAs binds to the canonical nucleotide-binding pocket of SsoIF2γ.