期刊
NUCLEIC ACIDS RESEARCH
卷 38, 期 19, 页码 6533-6543出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkq451
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资金
- 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
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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