Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0847097 (acidity)
 15,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Chandipura (CHP) virus, a member of the vesiculovirus genus within the Rhabdoviridae family, was first isolated from human patients in India. The full length phosphoprotein P gene of CHP have been cloned and expressed in Escherichia coli using the T7 polymerase-based pET-3 series of expression vectors. Under optimal conditions of induction with IPTG, the recombinant P protein constituted 35% of the total bacterial protein. The bacterially expressed protein was found to be phosphate-free. Deletion analysis suggested that the anomalous mobility of the P protein was due to its high acidity. The expressed protein can be phosphorylated in vitro by the extracts prepared from baby hamster kidney cells or rabbit reticulocytes. The cellular kinase involved in phosphorylation appears to be casein kinase II.
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PMID:Cloning of the chandipura virus phosphoprotein encoding gene and its expression in Escherichia coli. 778 87

We described previously (Takamatsu et al., 1998. Microbiol. Immunol. 42: 761-771) the rabies virus P protein as being composed of several components of different sizes, among which the full-sized major components were termed as p40 and p37 according to their electrophoretic mobilities, and radiolabeling studies with [32P]phosphate implied that p40 was a hyperphosphorylated form. We further examined here these proteins by two-dimensional (2-D) gel electrophoresis and immunoblotting, showing that a major component, p37, was composed of multiply modified subcomponents of different pIs (termed p37-1, p37-2, p37-3, etc., based on their acidity) in the virion and infected cells, but the unmodified precursor (termed p37-0) was little in amount. The viral nucleocapsid (NC)-bound P proteins were composed of multiple forms of p37 (the major one was p37-1) and also a minor component, p40-1. P proteins which were bound to newly synthesized free N proteins were mostly composed of p37-1, indicating that hyperphosphorylation of P proteins occurred after their being used for the encapsidation. Treatment of the infected cells with okadaic acid induced accumulation of the more acidic forms of P proteins, suggesting that heterogeneity in the full-sized P proteins is a reflection of their dynamic aspects of multiple cycles of phosphorylations and dephosphorylations in the cell. Two-D gel analyses demonstrated also that p40 was not so acidic as we expected, and implied that our previous data of apparent hyperphosphorylation of p40 was due to very frequently recycled utilization of the protein, and preformed non-labeled P proteins were also 32P-phosphorylated in a radiolabeling period and were converted to the p40.
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PMID:Studies on the rabies virus RNA polymerase: 3. Two-dimensional electrophoretic analysis of the multiplicity of non-catalytic subunit (P protein). 1222 32