Open AccessInteraction of Sesbania mosaic virus (SeMV) RNA‐dependent RNA polymerase (RdRp) with the p10 domain of polyprotein 2a and its implications in SeMV replication
Author(s) -
Govind Kunduri,
Bakshi Arindam,
Savithri Handanahal S.
Publication year - 2014
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2014.03.009
Subject(s) - rna polymerase , biology , rna dependent rna polymerase , polymerase , rna , virology , genetics , gene
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, CΔ43 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.