Methylated 23S rRNA nucleotide m2G1835 of Escherichia coli ribosome facilitates subunit association

Ilya A. Osterman, Petr V. Sergiev, Philipp O. Tsvetkov, Alexander A. Makarov, Alexey A. Bogdanov, Olga A. Dontsova

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

Among 4.5 thousand nucleotides of Escherichia coli ribosome 36 are modified. These nucleotides are clustered in the functional centers of ribosome, particularly on the interface of large and small subunits. Nucleotide m 2G1835 located on the 50S side of intersubunit bridge cluster B2 is modified by N2-methyltransferase RlmG. By means of isothermal titration calorimetry and Rayleigh light scattering, we have found that methylation of m2G1835 specifically enhances association of ribosomal subunits. No defects in fidelity of translation or interaction with translation GTPases could be ascribed to the ribosomes unmethylated at G1835 of the 23S rRNA. Methylation of G1835 was found to provide a significant advantage for bacteria at osmotic and oxidative stress.

Original languageEnglish
Pages (from-to)725-729
Number of pages5
JournalBiochimie
Volume93
Issue number4
DOIs
Publication statusPublished - Apr 2011
Externally publishedYes

Keywords

  • Methylation
  • Modification
  • N2-methylated guanosine
  • Ribosome
  • rlmG

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