Selected article for: "bind activity and RNA helix"
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_37
    Snippet: To further confirm the dsRNA-binding activity of MBP-VP35, we incubated the protein with an artificial dsRNA that was constructed by annealing two complementary digoxin (DIG)-labeled RNA strands that are derived from 5 200-nt egfp ORF, followed by the gel mobility shift assay. Our data show that while MBP alone showed no dsRNA binding activity, MBP-VP35 did bind to the RNA helix substrate in a dose-dependent manner (Supplementary Figure S4A and B.....
    Document: To further confirm the dsRNA-binding activity of MBP-VP35, we incubated the protein with an artificial dsRNA that was constructed by annealing two complementary digoxin (DIG)-labeled RNA strands that are derived from 5 200-nt egfp ORF, followed by the gel mobility shift assay. Our data show that while MBP alone showed no dsRNA binding activity, MBP-VP35 did bind to the RNA helix substrate in a dose-dependent manner (Supplementary Figure S4A and B). Moreover, we generated three EBOVspecific RNA helix substrates that contain 1-200 nts of EBOV 5 -UTR, 1-200 nts of 3 -UTR, and 1-200 nts of NP ORF of EBOV genomic RNA. Our data show that VP35 can bind to these EBOV-specific RNA helices (Supplementary Figure S4C -E).

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