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Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation

Mathur, C and Jimsheena, VK and Banerjee, S and Makinen, K and Gowda, LR and Savithri, HS (2012) Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation. In: Virology, 422 (2). pp. 254-264.

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Official URL: http://dx.doi.org/10.1016/j.virol.2011.10.009

Abstract

Regulation of NIa-Pro is crucial for polyprotein processing and hence, for successful infection of potyviruses. We have examined two novel mechanisms that could regulate NIa-Pro activity. Firstly, the influence of VPg domain on the proteolytic activity of NIa-Pro was investigated. It was shown that the turnover number of the protease increases when these two domains interact (as: two-fold; trans: seven-fold) with each other. Secondly, the protease activity of NIa-Pro could also be modulated by phosphorylation at Ser129. A mutation of this residue either to aspartate (phosphorylation-mimic) or alanine (phosphorylation-deficient) drastically reduces the protease activity. Based on these observations and molecular modeling studies, we propose that interaction with VPg as well as phosphorylation of Ser129 could relay a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro. (C) 2011 Elsevier Inc. All rights reserved.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Potyviridae;Pepper Vein Banding Virus (PVBV);Nuclear Inclusion protein-a protease (NIa-Pro);Viral Protein genome-linked (VPg);VPg-Pro;HPLC-based protease assay;Molecular modeling
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 27 Feb 2012 11:40
Last Modified: 27 Feb 2012 11:40
URI: http://eprints.iisc.ernet.in/id/eprint/43672

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