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

Author:
Osterman, Ilya A., Sergiev, Petr V., Tsvetkov, Philipp O., Makarov, Alexander A., Bogdanov, Alexey A., Dontsova, Olga A.
Source:
Biochimie 2011 v.93 no.4 pp. 725-729
ISSN:
0300-9084
Subject:
Escherichia coli, bacteria, calorimetry, guanosinetriphosphatase, light scattering, methylation, nucleotides, oxidative stress, ribosomal RNA, ribosomes, titration, translation (genetics)
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 m²G1835 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.
Agid:
901433