Pmt1, a Dnmt2 homolog in Schizosaccharomyces pombe, mediates tRNA methylation in response to nutrient signaling

The fission yeast Schizosaccharomyces pombe carries a cytosine 5-methyltransferase homolog of the Dnmt2 family (termed pombe methyltransferase 1, Pmt1), but contains no detectable DNA methylation. Here, we found that Pmt1, like other Dnmt2 homologs, has in vitro methylation activity on cytosine 38 o...

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Bibliographic Details
Published in:Nucleic acids research 2012-12, Vol.40 (22), p.11648-11658
Main Authors: Becker, Maria, Müller, Sara, Nellen, Wolfgang, Jurkowski, Tomasz P, Jeltsch, Albert, Ehrenhofer-Murray, Ann E
Format: Article
Language:English
Subjects:
Cytosine
Cytosine - metabolism
DNA (Cytosine-5-)-Methyltransferases - metabolism
DNA methylation
Glucose
Glutamic acid
Methylation
Methyltransferase
Nitrogen - metabolism
Nitrogen sources
Nucleic Acid Enzymes
Nutrients
Nutritional status
peptone
Protein-Serine-Threonine Kinases - physiology
Protein-serine/threonine kinase
Ribosomes
RNA, Transfer - metabolism
RNA, Transfer, Asp - chemistry
RNA, Transfer, Asp - metabolism
RNA, Transfer, Glu - metabolism
Schizosaccharomyces - enzymology
Schizosaccharomyces pombe
Schizosaccharomyces pombe Proteins - metabolism
Schizosaccharomyces pombe Proteins - physiology
Signal Transduction
Translation initiation
tRNA
tRNA Methyltransferases - metabolism
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Summary:The fission yeast Schizosaccharomyces pombe carries a cytosine 5-methyltransferase homolog of the Dnmt2 family (termed pombe methyltransferase 1, Pmt1), but contains no detectable DNA methylation. Here, we found that Pmt1, like other Dnmt2 homologs, has in vitro methylation activity on cytosine 38 of tRNA(Asp) and, to a lesser extent, of tRNA(Glu), despite the fact that it contains a non-consensus residue in catalytic motif IV as compared with its homologs. In vivo tRNA methylation also required Pmt1. Unexpectedly, however, its in vivo activity showed a strong dependence on the nutritional status of the cell because Pmt1-dependent tRNA methylation was induced in cells grown in the presence of peptone or with glutamate as a nitrogen source. Furthermore, this induction required the serine/threonine kinase Sck2, but not the kinases Sck1, Pka1 or Tor1 and was independent of glucose signaling. Taken together, this work reveals a novel connection between nutrient signaling and tRNA methylation that thus may link tRNA methylation to processes downstream of nutrient signaling like ribosome biogenesis and translation initiation.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gks956