New molecular insights into an archaeal rnase j reveal a conserved processive exoribonucleolysis mechanism of the rnase j family
文献类型：期刊论文
| 作者 | Zheng, Xin1,2,3; Feng, Na2,4; Li, Defeng4; Dong, Xiuzhu1; Li, Jie1 |
| 刊名 | Molecular microbiology
 |
| 出版日期 | 2017-11-01 |
| 卷号 | 106期号:3页码:351-366 |
| ISSN号 | 0950-382X |
| DOI | 10.1111/mmi.13769 |
| 通讯作者 | Li, defeng(lidefeng@moon.ibp.ac.cn) ; Dong, xiuzhu(dongxz@im.ac.cn) ; Li, jie(lijie824@im.ac.cn) |
| 英文摘要 | Rnase j, a prokaryotic 5-3 exo/endoribonuclease, contributes to mrna decay, rrna maturation and post-transcriptional regulation. yet the processive-exoribonucleolysis mechanism remains obscure. here, we solved the first rna-free and rna-bound structures of an archaeal rnase j, and through intensive biochemical studies provided detailed mechanistic insights into the catalysis and processivity. distinct dimerization/tetramerization patterns were observed for archaeal and bacterial rnase js, and unique archaeal loops i and ii were found involved in rna interaction. a hydrogen-bond-network was identified for the first time that assists catalysis by facilitating efficient proton transfer in the catalytic center. a conserved 5-monophosphate-binding pocket that coordinates the rna 5-end ensures the 5-monophosphate preferential exoribonucleolysis. to achieve exoribonucleolytic processivity, the 5-monophosphate-binding pocket and nucleotide +4 binding site anchor rna within the catalytic track; the 5-capping residue leu37 of the sandwich pocket coupled with the 5-monophosphate-binding pocket are dedicated to translocating and controlling the rna orientation for each exoribonucleolytic cycle. the processive-exoribonucleolysis mechanism was verified as conserved in bacterial rnase j and also exposes striking parallels with the non-homologous eukaryotic 5-3 exoribonuclease, xrn1. the findings in this work shed light on not only the molecular mechanism of the rnase j family, but also the evolutionary convergence of divergent exoribonucleases. |
| WOS关键词 | BETA-CASP RIBONUCLEASES ; MESSENGER-RNA ; BACILLUS-SUBTILIS ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; GENE-EXPRESSION ; RIBOSOMAL-RNA ; POLYNUCLEOTIDE PHOSPHORYLASE ; EXONUCLEASE ACTIVITY ; DECAY |
| WOS研究方向 | Biochemistry & Molecular Biology ; Microbiology |
| WOS类目 | Biochemistry & Molecular Biology ; Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:000413542800002 |
| 出版者 | WILEY |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2176886 |
| 专题 | 高能物理研究所 |
| 通讯作者 | Li, Defeng; Dong, Xiuzhu; Li, Jie |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, 1 Beichen West Rd, Beijing 100101, Peoples R China 2.Univ Chinese Acad Sci, 19A Yuquan Rd, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, 19B YuquanLu, Beijing 100049, Peoples R China 4.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, 15 Datun Rd, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zheng, Xin,Feng, Na,Li, Defeng,et al. New molecular insights into an archaeal rnase j reveal a conserved processive exoribonucleolysis mechanism of the rnase j family[J]. Molecular microbiology,2017,106(3):351-366. |
| APA | Zheng, Xin,Feng, Na,Li, Defeng,Dong, Xiuzhu,&Li, Jie.(2017).New molecular insights into an archaeal rnase j reveal a conserved processive exoribonucleolysis mechanism of the rnase j family.Molecular microbiology,106(3),351-366. |
| MLA | Zheng, Xin,et al."New molecular insights into an archaeal rnase j reveal a conserved processive exoribonucleolysis mechanism of the rnase j family".Molecular microbiology 106.3(2017):351-366. |
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来源：高能物理研究所
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