Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9127310 | Gene | 2005 | 6 Pages |
Abstract
We have recently identified RrmJ, the first encoded protein of the rrmJ-ftsH heat shock operon, as being the Um2552 methyltransferase of 23S rRNA, and reported that rrmJ-deficient strains exhibit growth defects, reduced translation rates and reduced stability of 70S ribosomes. U2552 is an ubiquitously methylated residue. It belongs to the A loop of 23S RNA which is an essential component of the ribosome peptidyltransferase centre and interacts directly with aminoacyl(A)-site tRNA. In the present study, we show that a lack of U2552 methylation, obtained in rrmJ-deficient mutants, results in a decrease in programmed +1 and â1 translational frameshifing and a decrease in readthrough of UAA and UGA stop codons. The increased translational accuracy of rrmJ-deficient strains suggests that the interaction between aminoacyl-tRNA and U2552 is important for selection of the correct tRNA at the ribosomal A site, and supports the idea that translational accuracy in vivo is optimal rather than maximal, thus pointing to the participation of recoding events in the normal cell physiology.
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Authors
Magdalena Widerak, Renée Kern, Abderrahim Malki, Gilbert Richarme,