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J Mol Biol. 2015 Sep 25;427(19):3086-95. doi: 10.1016/j.jmb.2015.07.020. Epub 2015 Aug 2.

Binding of the 5'-Triphosphate End of mRNA to the γ-Subunit of Translation Initiation Factor 2 of the Crenarchaeon Sulfolobus solfataricus.

Author information

1
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation.
2
Max F. Perutz Laboratories, Department of Microbiology, Immunobiology and Genetics, University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9/4, A-1030 Vienna, Austria.
3
Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russian Federation. Electronic address: alik@vega.protres.ru.

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.

KEYWORDS:

GTP; a/eIF2γ; archaea; crystal structure; mRNA

PMID:
26244522
DOI:
10.1016/j.jmb.2015.07.020
[Indexed for MEDLINE]

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