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)

As part of a study of transcriptional regulation by viral proteins, we examined whether an acidic region from a regulatory protein of an RNA virus could function as a trans-activator. The NH2-terminal highly acidic domain I of the phosphoprotein (P) of vesicular stomatitis virus (VSV) was fused to the DNA-binding domain of the yeast trans-activator, GAL4. In transient transfection assays, the resulting chimeric protein failed to activate transcription of a reporter CAT gene. However, mutation of basic amino acid residues located at positions 6 and 8 or the alteration of eight amino acids within the acidic domain to eight different amino acids converted the chimeric protein into a transcriptional activator comparable to wild-type GAL4. When subjected to SDS-polyacrylamide gel electrophoresis, the P proteins containing trans-activation-positive mutations in domain I showed an altered mobility, suggesting that these mutations may have caused a conformational change that is critical for trans-activation. Since the acidity of P domain I is not sufficient to activate transcription, additional features of this region must play an important role in GAL4-mediated trans-activation. None of the trans-activation-positive mutants supported VSV RNA transcription in vitro. These results suggest that the amino acid residues within P domain I that can be made to function in the trans-activation of DNA-dependent RNA transcription are distinct from those involved in VSV RNA-dependent RNA transcription.
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PMID:Alteration of specific amino acid residues in the acidic domain I of VSV phosphoprotein (P) converts a GAL4-P(I) hybrid into a transcriptional activator. 165 11

Past studies of norepinephrine-stimulated protein phosphorylation in intact C-6 glioma cells had identified a 58,000 molecular weight, 5.7 isoelectric point protein (58K-5.7) as a cyclic AMP-dependent phosphoprotein and had shown that 58K-5.7 was one of the most abundant proteins of the nuclear fraction. Initial experiments of present studies showed that the 58K-5.7 protein remained with the nuclear ghost, or matrix structure, after removal of chromatin. Based on the size, acidity, abundance, nonsolubilization by nonionic detergent and salt, and solubilization by urea, the hypothesis was advanced that the 58K-5.7 protein was the vimentin-type intermediate filament protein. The hypothesis was tested by two types of immunochemical experiments. Antisera against hamster vimentin reacted selectively with only the 58K-5.7 protein in polyacrylamide gels of urea-solubilized cellular residues (i.e., nonionic detergent and 0.6 M salt-insoluble material) as determined by immunoautoradiography. Antisera against the pure 58K-5.7 protein of C-6 cells bound selectively to a fibrous array of cellular material typical of vimentin filaments as determined by indirect immunofluorescence. It is concluded that the 58K-5.7 protein is vimentin.
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PMID:Vimentin: a phosphoprotein under hormonal regulation. 702 79

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

In order to investigate signalling pathways involved in the control of granule cell differentiation, survival and other functions by depolarization or activation of NMDA receptors we have characterized protein phosphorylation in cerebellar granule cells. Cultures of cerebellar granule cells were incubated with 32P orthophosphate and then challenged with NMDA, K+ or the Ca2+ ionophore ionomycin, agents which raise [Ca2+]i and stimulate differentiation and survival. Upon separation of labelled phosphoproteins by two-dimensional gel electrophoresis three differences were found in response to all of these agents. These were an increase in acidity of two phosphoproteins of 87 and 48 kDa (p87 and p48) and increased 32P-incorporation into a phosphoprotein of 120 kDa (p120). Treatment with PMA which stimulates neurite outgrowth but not survival affected p87 (increased its acidity) but not p48. The acidic shift of p87, therefore, is not sufficient to stimulate granule cell survival. The identification of p87 as the actin-binding MARCKS protein and the demonstration of its presence in neurites and growth cones of granule cells suggests that it may be involved in NMDA-stimulated neurite outgrowth. The phosphoproteins p120 and p48 may potentially be involved in events linking the rise in [Ca2+]i to increased granule cell survival or other aspects of granule cell differentiation.
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PMID:Phosphoproteins of cultured cerebellar granule cells and response to the differentiation-promoting stimuli NMDA, high K+ and ionomycin. 826 Nov 32