title: Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-TRM61 from Saccharomyces cerevisiae.
abstract: The N(1) methylation of adenine at position 58 (m(1)A58) of tRNA is an important post-transcriptional modification, which is vital for maintaining the stability of the initiator methionine tRNAi(Met). In eukaryotes, this modification is performed by the TRM6-TRM61 holoenzyme. To understand the molecular mechanism that underlies the cooperation of TRM6 and TRM61 in the methyl transfer reaction, we determined the crystal structure of TRM6-TRM61 holoenzyme from Saccharomyces cerevisiae in the presence and absence of its methyl donor S-Adenosyl-L-methionine (SAM). In the structures, two TRM6-TRM61 heterodimers assemble as a heterotetramer. Both TRM6 and TRM61 subunits comprise an N-terminal β-barrel domain linked to a C-terminal Rossmann-fold domain. TRM61 functions as the catalytic subunit, containing a methyl donor (SAM) binding pocket. TRM6 diverges from TRM61, lacking the conserved motifs used for binding SAM. However, TRM6 cooperates with TRM61 forming an L-shaped tRNA binding regions. Collectively, our results provide a structural basis for better understanding the m(1)A58 modification of tRNA occurred in Saccharomyces cerevisiae.
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Mingxing
authors: M
authors: Wang
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Yuwei
authors: Y
authors: Zhu
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Chongyuan
authors: C
authors: Wang
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Xiaojiao
authors: X
authors: Fan
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Xuguang
authors: X
authors: Jiang
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Mohammad
authors: M
authors: Ebrahimi
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Zhi
authors: Z
authors: Qiao
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Liwen
authors: L
authors: Niu
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Maikun
authors: M
authors: Teng
authors: Hefei National Laboratory for Physical Sciences at Microscale, Innovation Center for Cell Signalling Network, School of Life Science, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.|Key Laboratory of Structural Biology, Hefei Science Center of CAS, Chinese Academy of Science, Hefei, Anhui, 230026, People's Republic of China.
authors: Xu
authors: X
authors: Li
mesh_terms: D020816:Amino Acid Motifs; D001665:Binding Sites; D020134:Catalytic Domain / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D015870:Gene Expression; D020035:Holoenzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008745:Methylation; D008958:Models, Molecular; D011485:Protein Binding; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D012323:RNA Processing, Post-Transcriptional; D012358:RNA, Transfer, Met / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012436:S-Adenosylmethionine / Q000737:chemistry* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013379:Substrate Specificity; D012359:tRNA Methyltransferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D020035:Holoenzymes; D012358:RNA, Transfer, Met; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D012436:S-Adenosylmethionine; C409023:Gcd10 protein, S cerevisiae; D012359:tRNA Methyltransferases; C119384:GCD14 protein, S cerevisiae