title: N-terminal region of P protein of Chandipura virus is responsible for phosphorylation-mediated homodimerization.
abstract: 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.
authors.affiliation: 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.
authors.forename: T
authors.initials: T
authors.lastname: Raha
authors.forename: E
authors.initials: E
authors.lastname: Samal
authors.forename: A
authors.initials: A
authors.lastname: Majumdar
authors.forename: S
authors.initials: S
authors.lastname: Basak
authors.forename: D
authors.initials: D
authors.lastname: Chattopadhyay
authors.forename: D J
authors.initials: DJ
authors.lastname: Chattopadhyay
mesh_terms: D001665:Binding Sites / Q000235:genetics; D047390:Casein Kinase II; D002918:Chymotrypsin / Q000737:chemistry; D019281:Dimerization; D018832:Molecular Chaperones; D016297:Mutagenesis, Site-Directed; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000737:chemistry* / Q000235:genetics; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry; D010766:Phosphorylation; D011485:Protein Binding / Q000235:genetics; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry; D018116:Vesiculovirus / Q000502:physiology*; D015678:Viral Structural Proteins / Q000737:chemistry* / Q000235:genetics
chemical_list: D018832:Molecular Chaperones; C412837:P protein, Chandipura virus; D010750:Phosphoproteins; D015678:Viral Structural Proteins; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D010744:Phosphoric Monoester Hydrolases; D002918:Chymotrypsin; D014357:Trypsin