MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10

Summary: MOV10L1 and its paralog MOV10 are evolutionally conserved RNA helicases involved in distinct RNA regulatory pathways. The testis-specific MOV10L1 is essential for spermatogenesis and PIWI-interacting RNAs biogenesis, whereas MOV10 is ubiquitous and multifunctional. Although both proteins ha...

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Main Authors:	Xia Zhang, Lina Yu, Shasha Ye, Jie Xie, Xingxu Huang, Ke Zheng, Bo Sun
Format:	Article
Language:	English
Published:	Elsevier 2019-07-01
Series:	iScience
Online Access:	http://www.sciencedirect.com/science/article/pii/S2589004219301981

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spelling	doaj-e8f7c4d4d9d7477d9a6bf92651c5d69d2020-11-24T21:21:38ZengElsevieriScience2589-00422019-07-01173648MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10Xia Zhang0Lina Yu1Shasha Ye2Jie Xie3Xingxu Huang4Ke Zheng5Bo Sun6School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, ChinaState Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing, Jiangsu 211166, ChinaSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China; Shanghai Institute of Biochemistry and Cell Biology, Chinese Academy of Sciences, Shanghai 200031, China; University of Chinese Academy of Sciences, Beijing 100049, ChinaState Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing, Jiangsu 211166, ChinaSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, ChinaState Key Laboratory of Reproductive Medicine, Nanjing Medical University, Nanjing, Jiangsu 211166, China; Corresponding authorSchool of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China; Corresponding authorSummary: MOV10L1 and its paralog MOV10 are evolutionally conserved RNA helicases involved in distinct RNA regulatory pathways. The testis-specific MOV10L1 is essential for spermatogenesis and PIWI-interacting RNAs biogenesis, whereas MOV10 is ubiquitous and multifunctional. Although both proteins have been implied to correlate with RNA G-quadruplex (RG4) in vivo, their capabilities in binding and resolving RG4 and their respective biological significance remain unclear. Herein, we comprehensively characterize and compare the activities of these two helicases on various nucleic acid substrates in vitro, with a focus on RG4 structure. We find that both MOV10L1 and MOV10 are able to resolve RG4, with MOV10L1 being more efficient in that. In contrast to MOV10, MOV10L1 prefers to bind to a junction between single-stranded RNA and RG4, which is mediated by both its N and C termini. Furthermore, we show that RG4 unwinding by MOV10L1 facilitates the cleavage of this specific RNA structure by an endonuclease. : Biological Sciences; Biochemistry; Molecular Biology Subject Areas: Biological Sciences, Biochemistry, Molecular Biologyhttp://www.sciencedirect.com/science/article/pii/S2589004219301981
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Xia Zhang Lina Yu Shasha Ye Jie Xie Xingxu Huang Ke Zheng Bo Sun
spellingShingle	Xia Zhang Lina Yu Shasha Ye Jie Xie Xingxu Huang Ke Zheng Bo Sun MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10 iScience
author_facet	Xia Zhang Lina Yu Shasha Ye Jie Xie Xingxu Huang Ke Zheng Bo Sun
author_sort	Xia Zhang
title	MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10
title_short	MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10
title_full	MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10
title_fullStr	MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10
title_full_unstemmed	MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10
title_sort	mov10l1 binds rna g-quadruplex in a structure-specific manner and resolves it more efficiently than mov10
publisher	Elsevier
series	iScience
issn	2589-0042
publishDate	2019-07-01
description	Summary: MOV10L1 and its paralog MOV10 are evolutionally conserved RNA helicases involved in distinct RNA regulatory pathways. The testis-specific MOV10L1 is essential for spermatogenesis and PIWI-interacting RNAs biogenesis, whereas MOV10 is ubiquitous and multifunctional. Although both proteins have been implied to correlate with RNA G-quadruplex (RG4) in vivo, their capabilities in binding and resolving RG4 and their respective biological significance remain unclear. Herein, we comprehensively characterize and compare the activities of these two helicases on various nucleic acid substrates in vitro, with a focus on RG4 structure. We find that both MOV10L1 and MOV10 are able to resolve RG4, with MOV10L1 being more efficient in that. In contrast to MOV10, MOV10L1 prefers to bind to a junction between single-stranded RNA and RG4, which is mediated by both its N and C termini. Furthermore, we show that RG4 unwinding by MOV10L1 facilitates the cleavage of this specific RNA structure by an endonuclease. : Biological Sciences; Biochemistry; Molecular Biology Subject Areas: Biological Sciences, Biochemistry, Molecular Biology
url	http://www.sciencedirect.com/science/article/pii/S2589004219301981
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MOV10L1 Binds RNA G-Quadruplex in a Structure-Specific Manner and Resolves It More Efficiently Than MOV10

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