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...

Celý popis

Uloženo v:

Podrobná bibliografie
Vydáno v:	Biomolecules (Basel, Switzerland) Ročník 12; číslo 9; s. 1247
Hlavní autor:	Mushegian, Arcady
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Switzerland MDPI AG 06.09.2022 MDPI
Témata:	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
On-line přístup:	Získat plný text
Tagy:	Přidat tag Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!

Popis
Shrnutí:	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.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23
ISSN:	2218-273X 2218-273X
DOI:	10.3390/biom12091247