Journal
FEBS LETTERS
Volume 584, Issue 3, Pages 571-576Publisher
WILEY
DOI: 10.1016/j.febslet.2009.12.003
Keywords
P10; P8; Natively unfolded; Nucleic acid binding; ATPase; Sesbania mosaic virus
Funding
- Council of Scientific and Industrial Research (CSIR) of the Government of India
- Indian Institute of Science, Bangalore
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Open reading frame (ORF) 2a of Sesbania mosaic virus (SeMV) codes for polyprotein 2a (Membrane anchor-protease-VPg-P10-P8). The C-terminal domain of SeMV polyprotein 2a was cloned, expressed and purified in order to functionally characterize it. The protein of size 8 kDa (P8) domain, like viral protein genome linked (VPg), was found to be natively unfolded and could bind to nucleic acids. Interestingly, P10-P8 but not P8 showed a novel Mg2+ dependent ATPase activity that was inhibited in the presence of poly A. In the absence of P8, the ATPase activity of the protein of size 10 kDa (P10) domain was reduced suggesting that the natively unfolded P8 domain influenced the P10 ATPase. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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