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

• Published in: iScience Vol. 17; pp. 36 - 48
• Main Authors: Zhang, Xia, Yu, Lina, Ye, Shasha, Xie, Jie, Huang, Xingxu, Zheng, Ke, Sun, Bo
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 26.07.2019; Elsevier
• Subjects: Biochemistry; Biological Sciences; Molecular Biology; Molecular Biology; Biological Sciences; Biochemistry
• ISSN: 2589-0042; 2589-0042
• DOI: 10.1016/j.isci.2019.06.016

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. [Display omitted] •Both MOV10L1 and MOV10 can resolve RG4 structure in an ATP-dependent manner•MOV10L1 unwinds RG4 more efficiently than MOV10•MOV10L1 preferentially binds to an ssRNA-RG4 junction•RG4 unwinding by MOV10L1 facilitates its endonucleolytic cleavage Biological Sciences; Biochemistry; Molecular Biology