Journal
NUCLEIC ACIDS RESEARCH
Volume 38, Issue 19, Pages 6533-6543Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq451
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Funding
- Fonds pour le Recherche Fondamentale Collective [2.4.520.05F]
- Fonds D. et A. Van Buuren
- Fonds pour la Formation a la Recherche dans l'Industrie et dans l'Agriculture
- European Commission
- Polish Ministry of Science and Higher Education [301 2396 33, 301 105 32/3599]
- Foundation for Polish Science
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Two archaeal tRNA methyltransferases belonging to the SPOUT superfamily and displaying unexpected activities are identified. These enzymes are orthologous to the yeast Trm10p methyltransferase, which catalyses the formation of 1-methylguanosine at position 9 of tRNA. In contrast, the Trm10p orthologue from the crenarchaeon Sulfolobus acidocaldarius forms 1-methyladenosine at the same position. Even more surprisingly, the Trm10p orthologue from the euryarchaeon Thermococcus kodakaraensis methylates the N-1-atom of either adenosine or guanosine at position 9 in different tRNAs. This is to our knowledge the first example of a tRNA methyltransferase with a broadened nucleoside recognition capability. The evolution of tRNA methyltransferases methylating the N-1 atom of a purine residue is discussed.
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