Jump to Main Content
Binding of the 5′-Triphosphate End of mRNA to the γ-Subunit of Translation Initiation Factor 2 of the Crenarchaeon Sulfolobus solfataricus
- Arkhipova, Valentina, Stolboushkina, Elena, Kravchenko, Olesya, Kljashtorny, Vladislav, Gabdulkhakov, Azat, Garber, Maria, Nikonov, Stanislav, Märtens, Birgit, Bläsi, Udo, Nikonov, Oleg
- Journal of Molecular Biology 2015 v.427 pp. 3086-3095
- Sulfolobus solfataricus, messenger RNA, mutants, nucleotides, translation (genetics)
- 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.