ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Phosphorylation status of the phosphoprotein P of rinderpest virus modulates transcription and replication of the genome

Saikia, Paramananda and Gopinath, M and Shaila, MS (2008) Phosphorylation status of the phosphoprotein P of rinderpest virus modulates transcription and replication of the genome. In: Archives of Virology, 153 (4). pp. 615-626.

[img] PDF
fulltext2.pdf - Published Version
Restricted to Registered users only

Download (491Kb) | Request a copy
Official URL: http://www.springerlink.com/content/cnrh17821r4g27...

Abstract

The phosphoprotein P of paramyxoviruses is known to play more than one role in genome transcription and replication. Phosphorylation of P at the NH2 terminus by cellular casein kinase II has been shown to be necessary for transcription of the genome in some of the viruses, while it is dispensable for replication. The phosphorylation null mutant of rinderpest virus P protein, in which three serine residues have been mutated, has been shown earlier to be non-functional in an in vivo minigenome replication/transcription system. In this work, we have shown that the phosphorylation of P protein is essential for transcription, whereas the null mutant is active in replication of the genome in vivo. The null mutant P acts as a transdominant repressor of transcriptional activity of wild-type P and as an activator of replication carried out by wild-type P protein. These results suggest the phosphorylation status of P may act as a replication switch during virus replication. We also show that the phosphorylation null mutant P is capable of interacting with L and N proteins and is able to form a tripartite complex of L-(N-P) when expressed in insect cells, similar to wild-type P protein.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Springer.
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 29 Mar 2010 11:20
Last Modified: 19 Sep 2010 05:58
URI: http://eprints.iisc.ernet.in/id/eprint/26672

Actions (login required)

View Item View Item