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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, V. K. and Banerjee, S. and Makinen, K. and Gowda, L. R. (2012) Functional regulation of PVBV Nuclear Inclusion protein-a protease activity upon interaction with Viral Protein genome-linked and phosphorylation. Virology , 422. 254–264.

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Virology, Volume 422, Issue 2, 20 January 2012, Pages 254-264.pdf - Published Version
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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 (cis: 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.

Item Type: Article
Uncontrolled 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
Subjects: 600 Technology > 01 Medical sciences > 19 Viruses
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 20 Jan 2012 07:03
Last Modified: 18 Nov 2016 10:41
URI: http://ir.cftri.com/id/eprint/10547

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