REVIEW: Structural and Functional Features of Viral Chaperonins

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Lidia P. Kurochkina^1,a*, Pavel I. Semenyuk¹, and Olga S. Sokolova²

¹Belozersky Research Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, Russia

²Department of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 119991 Moscow, Russia

^* To whom correspondence should be addressed.

Received November 16, 2021; Revised December 6, 2021; Accepted December 6, 2021

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Chaperonins provide proper folding of proteins in vivo and in vitro and, as was thought until recently, are characteristic of prokaryotes, eukaryotes, and archaea. However, it turned out that some bacteria viruses (bacteriophages) encode their own chaperonins. This review presents results of the investigations of the first representatives of this new chaperonin group: the double-ring EL chaperonin and the single-ring OBP and AR9 chaperonins. Biochemical properties and structure of the phage chaperonins were compared within the group and with other known group I and group II chaperonins.

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KEY WORDS: chaperonin, bacteriophage, spatial structure, cryo-electron microscopy, crystallography

DOI: 10.1134/S0006297922010011

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