Nucleolar methyltransferase fibrillarin: Evolution of structure and functions
- Authors: Shubina M.Y.1, Musinova Y.R.1, Sheval E.V.1
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Affiliations:
- Lomonosov Moscow State University
- Issue: Vol 81, No 9 (2016)
- Pages: 941-950
- Section: Review
- URL: https://journals.rcsi.science/0006-2979/article/view/150997
- DOI: https://doi.org/10.1134/S0006297916090030
- ID: 150997
Cite item
Abstract
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.
Keywords
About the authors
M. Y. Shubina
Lomonosov Moscow State University
Email: evsheval@gmail.com
Russian Federation, Moscow, 119991
Y. R. Musinova
Lomonosov Moscow State University
Email: evsheval@gmail.com
Russian Federation, Moscow, 119991
E. V. Sheval
Lomonosov Moscow State University
Author for correspondence.
Email: evsheval@gmail.com
Russian Federation, Moscow, 119991
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