Ribosomal RNA guanine-(N2)-methyltransferases and their targets

Petr V. Sergiev, Alexey A. Bogdanov, Olga A. Dontsova

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)

Abstract

Five nearly universal methylated guanine-(N2) residues are present in bacterial rRNA in the ribosome. To date four out of five ribosomal RNA guanine-(N2)-methyltransferases are described. RsmC(YjjT) methylates G1207 of the 16S rRNA. RlmG(YgjO) and RlmL(YcbY) are responsible for the 23S rRNA m2G1835 and m2G2445 formation, correspondingly. RsmD(YhhF) is necessary for methylation of G966 residue of 16S rRNA. Structure of Escherichia coli RsmD(YhhF) methyltransferase and the structure of the Methanococcus jannaschii RsmC ortholog were determined. All ribosomal guanine-(N2)-methyltransferases have similar AdoMet-binding sites. In relation to the ribosomal substrate recognition, two enzymes that recognize assembled subunits are relatively small single domain proteins and two enzymes that recognize naked rRNA are larger proteins containing separate methyltransferase- and RNA-binding domains. The model for recognition of specific target nucleotide is proposed. The hypothetical role of the m2G residues in rRNA is discussed.

Original languageEnglish
Pages (from-to)2295-2301
Number of pages7
JournalNucleic Acids Research
Volume35
Issue number7
DOIs
Publication statusPublished - Apr 2007
Externally publishedYes

Fingerprint

Dive into the research topics of 'Ribosomal RNA guanine-(N2)-methyltransferases and their targets'. Together they form a unique fingerprint.

Cite this