Single serine phosphorylation within the acidic domain of Chandipura virus P protein regulates the transcription in vitro

Virology
D ChattopadhyayD Chattopadhyay

Abstract

Bacterially expressed unphosphorylated P protein of Chandipura Virus was found to be efficiently phosphorylated in vitro by casein kinase II (CKII). The phosphorylated form of the P protein supported the transcription in vitro but the unphosphorylated form could not. Kinetic data suggests that CKII incorporates one molecule of phosphate. Western blotting with monoclonal antibody against phosphoserine and phosphoaminoacid analysis confirmed that the phosphate accepting residue was serine. Comparison with P protein of other viruses and tryptic digest of the phosphorylated protein predicted the ser62 was the probable site for phosphorylation. This was further confirmed by substituating ser62 with alanine by site-directed mutagenesis. CKII was unable to phosphorylate the mutated P protein which in turn could not support the transcription in vitro. The phosphorylated P protein eluted from the gel filtration at the position of its dimer in contrast to the unphosphorylated protein which eluted as monomer.

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Citations

Aug 9, 2007·Virus Genes·Marcos Fabián BilenPablo Daniel Ghiringhelli
Jul 6, 2012·Archives of Virology·Kapila KumarSanjay Gupta
Apr 4, 2009·Journal of Molecular Biology·Francine C A GerardMarc Jamin
Jul 5, 2007·Bioscience Reports·Soumen BasakDhrubajyoti Chattopadhyay
Jun 23, 2012·Acta Tropica·Sunil MenghaniPramod Khedekar
Mar 13, 2003·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Flavio Meggio, Lorenzo A Pinna
Aug 21, 2007·Biochemistry·Francine C A GerardMarc Jamin

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