Methylation of Ribosomal Protein L42 Regulates Ribosomal Function and Stress-adapted Cell Growth |
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Authors: | Atsuko Shirai Mahito Sadaie Kaori Shinmyozu Jun-ichi Nakayama |
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Affiliation: | From the ‡Laboratory for Chromatin Dynamics and ;¶Proteomics Support Unit, RIKEN Center for Developmental Biology, Kobe 650-0047, Japan and ;the §Cambridge Research Institute, Cancer Research UK, Robinson Way, Cambridge CB2 0RE, United Kingdom |
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Abstract: | Lysine methylation is one of the most common protein modifications. Although lysine methylation of histones has been extensively studied and linked to gene regulation, that of non-histone proteins remains incompletely understood. Here, we show a novel regulatory role of ribosomal protein methylation. Using an in vitro methyltransferase assay, we found that Schizosaccharomyces pombe Set13, a SET domain protein encoded by SPAC688.14, specifically methylates lysine 55 of ribosomal protein L42 (Rpl42). Mass spectrometric analysis revealed that endogenous Rpl42 is monomethylated at lysine 55 in wild-type S. pombe cells and that the methylation is lost in Δset13 mutant cells. Δset13 and Rpl42 methylation-deficient mutant S. pombe cells showed higher cycloheximide sensitivity and defects in stress-responsive growth control compared with wild type. Genetic analyses suggested that the abnormal growth phenotype was distinct from the conserved stress-responsive pathway that modulates translation initiation. Furthermore, the Rpl42 methylation-deficient mutant cells showed a reduced ability to survive after entering stationary phase. These results suggest that Rpl42 methylation plays direct roles in ribosomal function and cell proliferation control independently of the general stress-response pathway. |
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Keywords: | Protein Methylation Ribosome Function Ribosome Structure Translation Regulation Yeast Genetics Chronological Aging SET Domain Protein |
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