Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m¹G37.
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.
Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo 113-0032, Japan. sakurako@iam.u-tokyo.ac.jp.
Sakurako
S
Goto-Ito
Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Yokohama 230-0045, Japan. takuhiro.ito@riken.jp.
Takuhiro
T
Ito
RIKEN Structural Biology Laboratory, Yokohama 230-0045, Japan. yokoyama@riken.jp.
Shigeyuki
S
Yokoyama
D049148:Aminoacylation; D002384:Catalysis; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D012343:RNA, Transfer / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D012359:tRNA Methyltransferases / Q000737:chemistry / Q000378:metabolism*
D012343:RNA, Transfer; D012359:tRNA Methyltransferases
Trm5; TrmD; m1G37; tRNA