Mapping the domain of interaction of PVBV VPg with NIa-Pro: Role of N-terminal disordered region of VPg in the modulation of structure and function

Sabharwal, Pallavi and Srinivas, Sistla and Savithri, Handanahal S (2018) Mapping the domain of interaction of PVBV VPg with NIa-Pro: Role of N-terminal disordered region of VPg in the modulation of structure and function. In: VIROLOGY, 524 . pp. 18-31.

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Abstract

VPg-Pro is involved in polyprotein processing, therefore its regulation is important for a successful potyviral infection. We report here that the N-terminal disordered region of VPg forms the domain of interaction with NIa-Pro. This region is also demonstrated to be responsible for modulating the protease activity of VPg-Pro, both in cis and trans. The disordered nature of VPg is elicited by the N-terminal 22 residues as removal of these residues (Delta N22 VPg) brought about gross structural and conformational changes in the protein. Interestingly, Delta N22 VPg gained ATPase activity which suggested the presence of autoinhibitory motif within the N-terminal region of VPg. The autoinhibition gets relieved upon interaction of VPg with NIa-Pro or removal of the inhibitory motif. Thus, the N-terminal 22 residues of VPg qualify as molecular recognition feature (MoRF), regulating both protease and ATPase activity of VPg-Pro as well as forming the domain of interaction with other viral/host proteins.

Item Type:	Journal Article
Publication:	VIROLOGY
Publisher:	ACADEMIC PRESS INC ELSEVIER SCIENCE
Additional Information:	Copy right for this article belong to ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords:	Potyviridae; Pepper vein banding virus (PVBV); Viral protein genome linked (VPg); Molecular recognition feature (MoRF); Intrinsically disordered proteins (IDPs); Nuclear inclusion a-protease (NIa-Pro); Analytical ultracentrifugation (AUC)
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	22 Oct 2018 15:03
Last Modified:	22 Oct 2018 15:03
URI:	http://eprints.iisc.ac.in/id/eprint/60929

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