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Trm7p catalyses the formation of two 2′‐ O ‐methylriboses in yeast tRNA anticodon loop
Author(s) -
Pintard Lionel,
Lecointe François,
Bujnicki Janusz M.,
Bonnerot Claire,
Grosjean Henri,
Lapeyre Bruno
Publication year - 2002
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/21.7.1811
Subject(s) - art history , transfer rna , art , humanities , biology , genetics , gene , rna
The genome of Saccharomyces cerevisiae encodes three close homologues of the Escherichia coli 2′‐ O ‐rRNA methyltransferase FtsJ/RrmJ, designated Trm7p, Spb1p and Mrm2p. We present evidence that Trm7p methylates the 2′‐ O ‐ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop, both in vivo and in vitro . In a trm7 Δ strain, which is viable but grows slowly, translation is impaired, thus indicating that these tRNA modifications could be important for translation efficiency. We discuss the emergence of a family of three 2′‐ O ‐RNA methyltransferases in Eukaryota and one in Prokaryota from a common ancestor. We propose that each eukaryotic enzyme is located in a different cell compartment, in which it would methylate a different RNA that can adopt a very similar secondary structure.