Methyltransferases of Riboviria

Many viruses from the realm Riboviria infecting eukaryotic hosts encode protein domains with sequence similarity to S-adenosylmethionine-dependent methyltransferases. These protein domains are thought to be involved in methylation of the 5′-terminal cap structures in virus mRNAs. Some methyltransfer...

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Bibliographic Details
Published in:Biomolecules (Basel, Switzerland) Vol. 12; no. 9; p. 1247
Main Author: Mushegian, Arcady
Format: Journal Article
Language:English
Published: Switzerland MDPI AG 06.09.2022
MDPI
Subjects:
Adenosylmethionine
Amino Acid Sequence
Aspartic Acid
Conserved sequence
Coronaviruses
DNA methylation
Enzymes
FtsJ
Genomes
Horizontal transfer
Lysine
Lysine - genetics
Methylation
Methyltransferase
Methyltransferases - metabolism
Nucleotide sequence
Phylogeny
Proteins
Riboviria
RNA viruses
Rossmann fold
RrmJ
S-Adenosylmethionine
S-Adenosylmethionine - metabolism
Viruses
Water
Riboviria
Rossmann fold
methyltransferase
tobacco mosaic virus
FtsJ
SN2 nucleophilic substitution
coronavirus
RrmJ
S-adenosylmethionine
ISSN:2218-273X, 2218-273X
Online Access:Get full text
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Summary:Many viruses from the realm Riboviria infecting eukaryotic hosts encode protein domains with sequence similarity to S-adenosylmethionine-dependent methyltransferases. These protein domains are thought to be involved in methylation of the 5′-terminal cap structures in virus mRNAs. Some methyltransferase-like domains of Riboviria are homologous to the widespread cellular FtsJ/RrmJ-like methyltransferases involved in modification of cellular RNAs; other methyltransferases, found in a subset of positive-strand RNA viruses, have been assigned to a separate “Sindbis-like” family; and coronavirus-specific Nsp13/14-like methyltransferases appeared to be different from both those classes. The representative structures of proteins from all three groups belong to a specific variety of the Rossmann fold with a seven-stranded β-sheet, but it was unclear whether this structural similarity extends to the level of conserved sequence signatures. Here I survey methyltransferases in Riboviria and derive a joint sequence alignment model that covers all groups of virus methyltransferases and subsumes the previously defined conserved sequence motifs. Analysis of the spatial structures indicates that two highly conserved residues, a lysine and an aspartate, frequently contact a water molecule, which is located in the enzyme active center next to the methyl group of S-adenosylmethionine cofactor and could play a key role in the catalytic mechanism of the enzyme. Phylogenetic evidence indicates a likely origin of all methyltransferases of Riboviria from cellular RrmJ-like enzymes and their rapid divergence with infrequent horizontal transfer between distantly related viruses.
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ISSN:2218-273X
2218-273X
DOI:10.3390/biom12091247