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Structure and Function of Archaeal Translation Initiation Factor 2 Fragments Containing Cys2-Cys2 Motifs

Oleg S. Nikonov1,a*, Natalia A. Nevskaya1, Maria B. Garber1, and Stanislav V. Nikonov1

1Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

* To whom correspondence should be addressed.

Received April 23, 2021; Revised May 21, 2021; Accepted May 25, 2021
The heterotrimeric (αβγ) translation initiation factor 2 of archaea and eukaryotes (a/eIF2) supplies the P-site of the ribosome with the initiation tRNA. Its two subunits (β and γ) contain the Cys2-Cys2 motif, which is capable of forming a stable zinc finger structure in the presence of zinc ions. In this work, comparative analysis of the fragments containing Cys2-Cys2 motifs in the aIF2β and aIF2γ structures from different organisms was carried out and their environments in crystals was analyzed. Based on the obtained data, a conclusion was made that the conformation and role of these fragments in the β- and γ-subunits of the aIF2 are different.
KEY WORDS: translation initiation factor 2, Sulfolobus solfataricus, crystal structure, zinc finger, Cys2-Cys2 motif

DOI: 10.1134/S0006297921080101