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Archaeal NSUN6 catalyzes m(5)C72 modification on a wide-range of specific tRNAs | |
2019-02-28 | |
Source Publication | NUCLEIC ACIDS RESEARCH
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ISSN | 0305-1048 |
Volume | 47Issue:4Pages:2041-2055 |
Status | 已发表 |
DOI | 10.1093/nar/gky1236 |
Abstract | Human NOL1/NOP2/Sun RNA methyltransferase family member 6 (hNSun6) generates 5-methylcytosine (m(5)C) at C72 of four specific tRNAs, and its homologs are present only in higher eukaryotes and hyperthermophilic archaea. Archaeal NSun6 homologs possess conserved catalytic residues, but have distinct differences in their RNA recognition motifs from eukaryotic NSun6s. Until now, the biochemical properties and functions of archaeal NSun6 homologs were unknown. In archaeon Pyrococcus horikoshii OT3, the gene encoding the NSun6 homolog is PH1991. We demonstrated that the PH1991 protein could catalyze m(5)C72 formation on some specific PhtRNAs in vitro and was thus named as PhNSun6. Remarkably, PhNSun6 has a much wider range of tRNA substrates than hNSun6, which was attributed to its tRNA substrate specificity. The mechanism was further elucidated using biochemical and crystallographic experiments. Structurally, the binding pocket for nucleotide 73 in PhNSun6 is specific to accommodate U73 or G73-containing PhtRNAs. Furthermore, PhNSun6 lacks the eukaryotic NSun6-specific Lys-rich loop, resulting in the non-recognition of D-stem region by PhNSun6. Functionally, the m(5)C72 modification could slightly promote the thermal stability of PhtRNAs, but did not affect the amino acid accepting activity of PhtRNAs. |
Indexed By | SCI ; SCIE |
Funding Project | Youth Innovation Promotion Association (Chinese Academy of Sciences)[Y319S21291] |
WOS Research Area | Biochemistry & Molecular Biology |
WOS Subject | Biochemistry & Molecular Biology |
WOS ID | WOS:000467961200039 |
Publisher | OXFORD UNIV PRESS |
WOS Keyword | POSTTRANSCRIPTIONAL MODIFICATION ; METHYLTRANSFERASE ; 5-METHYLCYTOSINE ; ANTICODON ; SEQUENCE ; BINDING ; IDENTIFICATION ; STABILIZATION ; BIOSYNTHESIS ; DATABASE |
Original Document Type | Article |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/40896 |
Collection | 生命科学与技术学院_特聘教授组_王恩多组 生命科学与技术学院_PI研究组_刘如娟组 |
Corresponding Author | Wang, En-Duo; Liu, Ru-Juan |
Affiliation | 1.Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, CAS Ctr Excellence Mol Cell Sci, State Key Lab Mol Biol, 320 Yueyang Rd, Shanghai 200031, Peoples R China 2.Univ Chinese Acad Sci, 320 Yueyang Rd, Shanghai 200031, Peoples R China 3.ShanghaiTech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China |
Corresponding Author Affilication | School of Life Science and Technology |
Recommended Citation GB/T 7714 | Li, Jing,Li, Hao,Long, Tao,et al. Archaeal NSUN6 catalyzes m(5)C72 modification on a wide-range of specific tRNAs[J]. NUCLEIC ACIDS RESEARCH,2019,47(4):2041-2055. |
APA | Li, Jing,Li, Hao,Long, Tao,Dong, Han,Wang, En-Duo,&Liu, Ru-Juan.(2019).Archaeal NSUN6 catalyzes m(5)C72 modification on a wide-range of specific tRNAs.NUCLEIC ACIDS RESEARCH,47(4),2041-2055. |
MLA | Li, Jing,et al."Archaeal NSUN6 catalyzes m(5)C72 modification on a wide-range of specific tRNAs".NUCLEIC ACIDS RESEARCH 47.4(2019):2041-2055. |
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