Nucleolar Methyltransferase Fibrillarin: Evolution of Structure and Functions

M Y Shubina; Y R Musinova; E V Sheval

doi:10.1134/S0006297916090030

Nucleolar Methyltransferase Fibrillarin: Evolution of Structure and Functions

Biochemistry (Mosc). 2016 Sep;81(9):941-50. doi: 10.1134/S0006297916090030.

Authors

M Y Shubina¹, Y R Musinova, E V Sheval

Affiliation

¹ Lomonosov Moscow State University, Faculty of Bioengineering and Bioinformatics, Moscow, 119991, Russia. mariashubina23@gmail.com.

PMID: 27682166
DOI: 10.1134/S0006297916090030

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.

Publication types

Review

MeSH terms

Animals
Chromosomal Proteins, Non-Histone* / chemistry
Chromosomal Proteins, Non-Histone* / genetics
Chromosomal Proteins, Non-Histone* / metabolism
Evolution, Molecular*
Humans
Protein Domains
RNA Precursors / biosynthesis
RNA Precursors / chemistry
RNA Precursors / genetics
Structure-Activity Relationship
tRNA Methyltransferases* / chemistry
tRNA Methyltransferases* / genetics
tRNA Methyltransferases* / metabolism

Substances

Chromosomal Proteins, Non-Histone
RNA Precursors
fibrillarin
tRNA Methyltransferases