Identification of the enzyme responsible for N1-methylation of pseudouridine 54 in archaeal tRNAs |
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Authors: | Wurm Jan Philip Griese Marco Bahr Ute Held Martin Heckel Alexander Karas Michael Soppa Jörg Wöhnert Jens |
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Affiliation: | Institut für Molekulare Biowissenschaften, Johann-Wolfgang-Goethe-Universit?t, 60438 Frankfurt/M., Germany. |
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Abstract: | tRNAs from all three kingdoms of life contain a variety of modified nucleotides required for their stability, proper folding, and accurate decoding. One prominent example is the eponymous ribothymidine (rT) modification at position 54 in the T-arm of eukaryotic and bacterial tRNAs. In contrast, in most archaea this position is occupied by another hypermodified nucleotide: the isosteric N1-methylated pseudouridine. While the enzyme catalyzing pseudouridine formation at this position is known, the pseudouridine N1-specific methyltransferase responsible for this modification has not yet been experimentally identified. Here, we present biochemical and genetic evidence that the two homologous proteins, Mja_1640 (COG 1901, Pfam DUF358) and Hvo_1989 (Pfam DUF358) from Methanocaldococcus jannaschii and Haloferax volcanii, respectively, are representatives of the methyltransferase responsible for this modification. However, the in-frame deletion of the pseudouridine N1-methyltransferase gene in H. volcanii did not result in a discernable phenotype in line with similar observations for knockouts of other T-arm methylating enzymes. |
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Keywords: | tRNA modification N1-methyl pseudouridine SAM SPOUT-class methyltransferase archaea |
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