Interaction of Sesbania mosaic virus (SeMV) RNA-dependent RNA polymerase (RdRp) with the p10 domain of polyprotein 2a and its implications in SeMV replication

Govind, Kunduri and Bakshi, Arindam and Savithri, Handanahal S (2014) Interaction of Sesbania mosaic virus (SeMV) RNA-dependent RNA polymerase (RdRp) with the p10 domain of polyprotein 2a and its implications in SeMV replication. In: FEBS OPEN BIO, 4 . pp. 362-369.

PDF feb_opn_bio_4-362_2014.pdf - Published Version Restricted to Registered users only Download (1MB) | Request a copy

Abstract

Identification of viral encoded proteins that interact with RNA-dependent RNA polymerase (RdRp) is an important step towards unraveling the mechanism of replication. Sesbania mosaic virus (SeMV) RdRp was shown to interact strongly with p10 domain of polyprotein 2a and moderately with the protease domain. Mutational analysis suggested that the C-terminal disordered domain of RdRp is involved in the interaction with p10. Coexpression of full length RdRp and p10 resulted in formation of RdRp-p10 complex which showed significantly higher polymerase activity than RdRp alone. Interestingly, C Delta 43 RdRp also showed a similar increase in activity. Thus, p10 acts as a positive regulator of RdRp by interacting with the C-terminal disordered domain of RdRp. (C) 2014 The Authors. Published by Elsevier B.V.

Item Type:	Journal Article
Publication:	FEBS OPEN BIO
Publisher:	ELSEVIER SCIENCE LONDON
Additional Information:	Copyright for this article belongs to the ELSEVIER SCIENCE LONDON, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND
Keywords:	Sobemovirus; Sesbania mosaic virus; Replication; RNA-dependent RNA polymerase (RdRp); Protein-protein interactions
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	21 Jan 2015 06:46
Last Modified:	21 Jan 2015 06:46
URI:	http://eprints.iisc.ac.in/id/eprint/50737

Actions (login required)

View Item