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, 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.
journal_name
FEBS Open Biojournal_title
FEBS open bioauthors
Govind K,Bakshi A,Savithri HSdoi
10.1016/j.fob.2014.03.009subject
Has Abstractpub_date
2014-03-29 00:00:00pages
362-9issn
2211-5463pii
S2211-5463(14)00032-1journal_volume
4pub_type
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