Journal
GENE
Volume 347, Issue 1, Pages 109-114Publisher
ELSEVIER
DOI: 10.1016/j.gene.2004.12.025
Keywords
Escherichia coli; rrmJ/ftsJ; 23S RNA; methyltransferase; frameshift; readthrough
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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 -1 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. (c) 2004 Elsevier B.V. All rights reserved.
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