REVIEW: Nucleolar Methyltransferase Fibrillarin: Evolution of Structure and Functions

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M. Y. Shubina¹, Y. R. Musinova², and E. V. Sheval^2*

¹Lomonosov Moscow State University, Faculty of Bioengineering and Bioinformatics, 119991 Moscow, Russia; fax: +7 (495) 939-3181; E-mail: mariashubina23@gmail.com

²Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, 119991 Moscow, Russia; fax: +7 (495) 939-3181; E-mail: evsheval@gmail.com

^* To whom correspondence should be addressed.

Received May 24, 2016; Revision received June 6, 2016

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Fibrillarin is one of the most studied nucleolar proteins. Its main functions are methylation and processing of pre-rRNA. Fibrillarin is a highly conserved protein; however, in the course of evolution from archaea to eukaryotes, it acquired an additional N-terminal glycine and arginine-rich (GAR) domain. In this review, we discuss the evolution of fibrillarin structure and its relation to the functions of the protein in prokaryotes and eukaryotes.

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KEY WORDS: fibrillarin, nucleolus, methyltransferase, GAR domain

DOI: 10.1134/S0006297916090030

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