Phosphoprotein P of Rinderpest virus binds to plus sense leader RNA: regulation by phosphorylation.
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.
Raha
Tamal
T
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012.
Kaushik
Rajnish
R
Shaila
M S
MS
D020121:5' Untranslated Regions / Q000378:metabolism*; D016679:Genome, Viral; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D012367:RNA, Viral / Q000378:metabolism*; D012302:Rinderpest virus / Q000235:genetics* / Q000502:physiology; D014158:Transcription, Genetic; D014779:Virus Replication
D020121:5' Untranslated Regions; D010750:Phosphoproteins; D012367:RNA, Viral