Methylation of yeast ribosomal protein Rpl3 promotes translational elongation fidelity

RNA
Qais Al-HadidSteven G Clarke

Abstract

Rpl3, a highly conserved ribosomal protein, is methylated at histidine 243 by the Hpm1 methyltransferase in Saccharomyces cerevisiae. Histidine 243 lies close to the peptidyl transferase center in a functionally important region of Rpl3 designated as the basic thumb that coordinates the decoding, peptidyl transfer, and translocation steps of translation elongation. Hpm1 was recently implicated in ribosome biogenesis and translation. However, the biological role of methylation of its Rpl3 substrate has not been identified. Here we interrogate the role of Rpl3 methylation at H243 by investigating the functional impact of mutating this histidine residue to alanine (rpl3-H243A). Akin to Hpm1-deficient cells, rpl3-H243A cells accumulate 35S and 23S pre-rRNA precursors to a similar extent, confirming an important role for histidine methylation in pre-rRNA processing. In contrast, Hpm1-deficient cells but not rpl3-H243A mutants show perturbed levels of ribosomal subunits. We show that Hpm1 has multiple substrates in different subcellular fractions, suggesting that methylation of proteins other than Rpl3 may be important for controlling ribosomal subunit levels. Finally, translational fidelity assays demonstrate that like Hpm1-deficien...Continue Reading

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Citations

Jan 24, 2016·Biochemical and Biophysical Research Communications·Qais Al-HadidSteven Clarke
Aug 11, 2016·Nucleic Acids Research·Rosario Francisco-VelillaEncarnación Martinez-Salas
Feb 9, 2019·RNA·Max B Ferretti, Katrin Karbstein
May 23, 2019·Nucleic Acids Research·Anne-Sophie Gribling-BurrerSabine Rospert
Oct 9, 2019·Cells·Sergey O Sulima, Jonathan D Dinman
May 11, 2018·The Journal of Biological Chemistry·Steven G Clarke
Feb 11, 2021·Wiley Interdisciplinary Reviews. RNA·Karl NorrisJulie Louise Aspden
Mar 20, 2020·Current Protein & Peptide Science·Sebastian Kwiatkowski, Jakub Drozak
Jul 28, 2021·Trends in Biochemical Sciences·David M GayMartin D Jansson

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