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- W2028268511 abstract "We have recently identified RrmJ, the first encoded protein of the rrmJ-ftsH heat shock operon, as being the Um(2552) 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." @default.
- W2028268511 created "2016-06-24" @default.
- W2028268511 creator A5031041918 @default.
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- W2028268511 date "2005-02-01" @default.
- W2028268511 modified "2023-10-17" @default.
- W2028268511 title "U2552 methylation at the ribosomal A-site is a negative modulator of translational accuracy" @default.
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- W2028268511 doi "https://doi.org/10.1016/j.gene.2004.12.025" @default.
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