Natively unfolded nucleic acid binding P8 domain of SeMV polyprotein 2a affects the novel ATPase activity of the preceding P10 domain

Nair, Smita and Savithri, HS (2010) Natively unfolded nucleic acid binding P8 domain of SeMV polyprotein 2a affects the novel ATPase activity of the preceding P10 domain. In: FEBS letters, 584 (3). pp. 571-576.

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Abstract

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.

Item Type:	Journal Article
Publication:	FEBS letters
Publisher:	Elsevier science
Additional Information:	Copyright for this article belongs to Elsevier science.
Keywords:	P10; P8; Natively unfolded; Nucleic acid binding; ATPase; Sesbania mosaic virus
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	09 Feb 2010 11:28
Last Modified:	19 Sep 2010 05:54
URI:	http://eprints.iisc.ac.in/id/eprint/25523

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