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Protein Engineering, Vol. 13, No. 6, 437-444, June 2000
© 2000 Oxford University Press

N-terminal region of P protein of Chandipura virus is responsible for phosphorylation-mediated homodimerization

T. Raha1, E. Samal1,2, A. Majumdar1, S. Basak1, D. Chattopadhyay1,3 and D.J. Chattopadhyay1,4

1 Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology, Department of Biochemistry, University College of Science, University of Calcutta, 35, Ballygunge Circular Road, Calcutta 700019, West Bengal, India

The phosphoprotein P of Chandipura (CHP) virus, an Indian isolate of rhabdovirus, was found to support transcription upon phosphorylation by casein kinase II (CKII). A phosphorylation-induced change in the protein conformation was found to occur at the N-terminal region of the protein. Biochemical studies for further characterization of this phosphorylation-based conformational alteration demonstrated that phosphorylation leads to the transition from an `open' to `closed' structure of the protein. The phosphate group introduced by CKII was found to be resistant to phosphatases. This phosphorylation-based structural alteration changes the accessible hydrophobic surface area of the protein and also the available digestion sites of different proteases. The phosphorylated form of P protein was found to be a dimer by His-tag dilution assay. Using the same approach it was found that the N-terminal 46 amino acids are responsible for P–P dimerization, only after phosphorylation.


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