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Biomolecules 2017, 7(1), 32; doi:10.3390/biom7010032

Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m1G37

1
Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan
2
Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama 230-0045, Japan
3
RIKEN Structural Biology Laboratory, Yokohama 230-0045, Japan
*
Authors to whom correspondence should be addressed.
Academic Editor: Valérie de Crécy-Lagard
Received: 13 February 2017 / Revised: 7 March 2017 / Accepted: 16 March 2017 / Published: 21 March 2017
(This article belongs to the Special Issue tRNA Modifications: Synthesis, Function and Beyond)
View Full-Text   |   Download PDF [3515 KB, uploaded 22 March 2017]   |  

Abstract

The N1-atom of guanosine at position 37 in transfer RNA (tRNA) is methylated by tRNA methyltransferase 5 (Trm5) in eukaryotes and archaea, and by tRNA methyltransferase D (TrmD) in bacteria. The resultant modified nucleotide m1G37 positively regulates the aminoacylation of the tRNA, and simultaneously functions to prevent the +1 frameshift on the ribosome. Interestingly, Trm5 and TrmD have completely distinct origins, and therefore bear different tertiary folds. In this review, we describe the different strategies utilized by Trm5 and TrmD to recognize their substrate tRNAs, mainly based on their crystal structures complexed with substrate tRNAs. View Full-Text
Keywords: m1G37; Trm5; TrmD; tRNA m1G37; Trm5; TrmD; tRNA
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Goto-Ito, S.; Ito, T.; Yokoyama, S. Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m1G37. Biomolecules 2017, 7, 32.

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