Nucleolar methyltransferase fibrillarin: Evolution of structure and functions
- Authors: Shubina M.Y.1, Musinova Y.R.1, Sheval E.V.1
- 
							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
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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.
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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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