Phosphoprotein P of Rinderpest virus binds to plus sense leader RNA: regulation by phosphorylation

Raha, Tamal ; Kaushik, Rajnish ; Shaila, M. S. (2004) Phosphoprotein P of Rinderpest virus binds to plus sense leader RNA: regulation by phosphorylation Virus Research, 104 (2). pp. 191-200. ISSN 0168-1702

Full text not available from this repository.

Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.virusres.2004.04.004

Abstract

The negative sense genome RNA of Rinderpest virus, a Paramyxoviridae, is encapsidated with the nucleocapsid protein N and serves as a template for the viral RNA dependent RNA polymerase for transcription and replication. The viral RNA polymerase consists of the large protein L and the phosphoprotein P functioning as the P-L complex. We provide in this report, evidences for specific binding of P protein of Rinderpest virus to the plus sense leader RNA depending on its phosphorylation status. We have also demonstrated that P protein is released from the le RNA:P protein complex upon phosphorylation in vitro. Finally, we have identified that the C-terminal 358-389 amino acid residues of P protein is involved in le RNA binding. The leader RNA binding may signify a hitherto unidentified role for P protein in the viral RNA synthesis. Moreover, our results indicate a possible role for P protein in the transcription-replication switch through leader RNA binding.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Rinderpest Virus; Phosphoprotein; Leader RNA; Replication and Transcription
ID Code:49285
Deposited On:19 Jul 2011 14:00
Last Modified:19 Jul 2011 14:00

Repository Staff Only: item control page