New molecular insights into an archaeal RNase J reveal a conserved processive exoribonucleolysis mechanism of the RNase J family

doi:10.1111/mmi.13769

	New molecular insights into an archaeal RNase J reveal a conserved processive exoribonucleolysis mechanism of the RNase J family
	Zheng X(郑欣); Zheng, X., N. Feng, D. Li, X. Dong and J. Li
刊名	MOLECULAR MICROBIOLOGY
	2017
卷号	106 期号:3 页码:351-366
ISSN号	0950-382X
DOI	10.1111/mmi.13769
文献子类	Article
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.
电子版国际标准刊号	1365-2958
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
语种	英语
WOS记录号	WOS:000413542800002
内容类型	期刊论文
源URL	[http://ir.ihep.ac.cn/handle/311005/285368]
专题	高能物理研究所_多学科研究中心
作者单位	中国科学院高能物理研究所
推荐引用方式 GB/T 7714	Zheng X,Zheng, X., N. Feng, D. Li, X. Dong and J. Li. 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	郑欣,&Zheng, X., N. Feng, D. Li, X. Dong and J. Li.(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	郑欣,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.