Author: Shu, Ting; Gan, Tianyu; Bai, Peng; Wang, Xiaotong; Qian, Qi; Zhou, Hui; Cheng, Qi; Qiu, Yang; Yin, Lei; Zhong, Jin; Zhou, Xi
Title: Ebola virus VP35 has novel NTPase and helicase-like activities Document date: 2019_6_20
ID: u3pxycqh_48
Snippet: Because the RNA helix-unwinding activity of EBOV VP35 is NTP-dependent, we sought to determine the region responsible for the NTPase activity within VP35. Our data showed that VP35 mutant with the deletion of a.a. 137-173 ( 137-173) failed to hydrolyze ATP ( Figure 6A ), indicating that this region, which is highly conserved within multiple filoviruses (Supplementary Figure S7) , is crucial for the ATPase of VP35. Furthermore, we examined the hel.....
Document: Because the RNA helix-unwinding activity of EBOV VP35 is NTP-dependent, we sought to determine the region responsible for the NTPase activity within VP35. Our data showed that VP35 mutant with the deletion of a.a. 137-173 ( 137-173) failed to hydrolyze ATP ( Figure 6A ), indicating that this region, which is highly conserved within multiple filoviruses (Supplementary Figure S7) , is crucial for the ATPase of VP35. Furthermore, we examined the helix-unwinding and dsRNA-binding activities of the VP35 deletion mutant, and found that while MBP-VP35 137-173 retained its dsRNA binding activity ( Figure 6B) , it failed to unwind RNA helix even in the presence of ATP ( Figure 6C ), ruling out the possibility that the observed NTPase and helicase-like activities are caused by unknown contaminant via dsRNA.
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