Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.7.11.1 (protein kinase)
81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Arginine-rich histones H2A, H2B, H3 and H4 contain two regions of interaction with cyclic nucleotide-dependent protein kinases: a substrate phosphorylation site and a region which noncompetitively inhibits cyclic nucleotide binding to the protein kinases. We have compared the interaction of cyclic nucleotide-dependent protein kinases with these two sites in histones which are organized in nucleosome structures with the interaction of the enzymes with free histones. Whereas histones in solution are readily phosphorylated by cyclic GMP-dependent protein kinase and the catalytic subunit of cyclic AMP-dependent protein kinase, mononucleosomes are not phosphorylated by these enzymes. Histones extracted from mononucleosomes can be phosphorylated, indicating that the lack of phosphorylation of nucleosomes is not due to covalent modification of the histones but to their organization within the nucleosome structure. Whereas histones in solution are effective noncompetitive inhibitors of cyclic GMP binding to cyclic GMP-dependent protein kinase and of cyclic AMP binding to the regulatory subunits of cyclic AMP-dependent protein kinase, mononucleosomes do not affect cyclic nucleotide binding. These studies indicate that histones which are organized in nucleosome structures are neither substrates nor modifiers of cyclic nucleotide-dependent protein kinases.
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PMID:Comparison of the interaction of cyclic nucleotide-dependent protein kinases with mononucleosomes and free histones. 627 7

Study of the protein kinase activity pattern of four human adrenocortical carcinoma showed that in all the samples examined a histone kinase (HK III) activity was present at high level, whereas it was barely detectable in normal tissue. HK III was separated from other known adrenocortical protein kinases by diethylaminoethyl cellulose chromatography. Isolated HK III exhibited a histone (H2B) protamine-phosphotranferase selectivity and used adenosine triphosphate but not guanosine triphosphate as phosphate donor. Serine was identified as the only target amino acid phosphorylated in the protein substrate. HK III showed an apparent molecular weight of 65,000 upon gel filtration and an apparent sedimentation coefficient of 3.7S. HK III activity was cyclic adenosine 3':5'-monophosphate independent and was not influenced by calcium, calmodulin, polyamines, and heparin. The significance of HK III activity in adrenocortical carcinoma extracts at a high level as compared to that of normal tissue remains to be clarified with regard both to its possible relationship with tumoral cell growth and differentiation processes and to its potential interest as a marker of human tumoral tissue activity.
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PMID:Characterization of a cyclic nucleotide-independent protein kinase highly active in human adrenocortical carcinoma. 629 59

Among the components of the two cyclic nucleotide system of Ceratitis capitata pharate adults, two cAMP-dependent protein kinase activities have been identified and purified through a sequence of chromatographic procedures. The properties of both protein kinases, A-1 and A-2, were studied and characterized in comparison with those of other sources. Protein kinase A-2 from Ceratitis capitata corresponds to type I from mammals mainly concerning about the dissociating effect of histones. Protein kinase A-2 exhibited a molecular weight of 39,000 in the presence of cAMP, whereas in the absence of the cyclic nucleotide two components of 80,000 and 159,000 were present and attributed to the forms RC and R2C2, respectively. Protein kinase activities A-1 and A-2 were markedly inhibited by increasing ionic strength whereas the activity (-cAMP/+cAMP) ratio for protein kinase A-2 increased versus NaCl concentration. Histones H1 and H2B were the best substrates for both A-1 and A-2 activities; the high mobility group of insect proteins (HMG) were also notably phosphorylated by A-2 preparation. Among the cyclic nucleotides assayed for the protein kinase activity A-2, cAMP induced a high activation at the lowest concentrations although high cAMP concentrations decreased the protein kinase activity, possibly through binding to the catalytic site. The protein kinase A-2 preparations exhibited a complex kinetics due to the presence of two forms with different affinity for ATP; these forms may be related to the aggregation properties of the enzyme.
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PMID:cAMP-dependent protein kinases from the insect Ceratitis capitata. 629 4

A protein kinase has been characterized among the proteins tightly bound to DNA. It is not extracted with 1 M NaCl and is released by extensive DNase I digestion. This enzyme is able to phosphorylate nucleosomal histones, essentially H2B and H3, and several non-histone proteins associated with DNA, on serine residue(s). It does not phosphorylate protamine, casein, phosvitin and the chromosomal non-histone proteins extracted with 1 M NaCl and is cAMP independent. This protein kinase can be distinguished from the previously described enzymes.
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PMID:A new cAMP independent protein kinase tightly bound to DNA, in rat liver nuclei. 631 66

The src gene product of Rous sarcoma virus (pp60(src)) was highly purified from a rat tumor cell line and shown to have physiological actin transformation activity in a cellular microinjection assay that measures the dissolution of actin microfilament bundles in vivo. The purified pp60(src) fraction consisted of two major proteins, seen on silver-stained sodium dodecyl sulfate-polyacrylamide gels: a 60,000-dalton (60K) protein, identified as pp60(src) by immunoprecipitation with tumor-bearing rabbit immunoglobulin G (IgG) and peptide mapping, and an unrelated 65K protein. There was no evidence for proteolytic cleavage of pp60(src). A 7,000-fold purification of the tyrosine-specific protein kinase activity of pp60(src) was achieved by this procedure. Purified pp60(src) phosphorylated tumor-bearing rabbit IgG heavy chains, casein, histones H1 and H2B, tubulin, and microtubule-associated proteins when assayed in vitro. When incubated with [gamma-(32)P]ATP in the absence of exogenous phosphoacceptor substrates, purified pp60(src) became labeled with (32)P at the tyrosine residues exclusively. Phosphatase and cyclic AMP-dependent protein kinase activities were undetectable in the purified fraction. Microinjection of highly purified pp60(src) into the cytoplasm of normal Swiss 3T3 mouse fibroblasts caused rapid and reversible dissolution of actin stress fibers, as visualized by indirect immunofluorescence with actin antibodies. The actin-disrupting activity was thermolabile and sensitive to inhibition by coinjection of tumor-bearing rabbit IgG, and purified to about the same extent (8,000-fold) as did the IgG kinase activity of pp60(src), thus implicating pp60(src) as the active agent. Examination of actin-associated proteins as substrates for the pp60(src) kinase in vitro showed that vinculin was phosphorylated directly by pp60(src), although to a small extent. Actin, myosin, and tropomyosin were not phosphorylated. Thus, pp60(src) purified by this procedure retains native functional properties and provides a useful probe for analyzing transformation-dependent changes in actin cytoarchitecture.
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PMID:Highly purified pp60src induces the actin transformation in microinjected cells and phosphorylates selected cytoskeletal proteins in vitro. 640 62

When a mixture of DNA-free core histones (H) from calf thymus is phosphorylated by the catalytic subunit of cAMP-dependent protein kinase, phosphate is incorporated primarily into H2B and, to a lesser extent, into H3 and H4. In contrast, when the phosphorylation of the DNA-free histones is compared to the phosphorylation of histones in long chromatin or in nucleosome core, only one of the core histones, H3, is phosphorylated. The site of modification of H3 has been identified as serine 10, which is located in the highly charged basic NH2-terminal region of the molecule. The other sites of phosphorylation in H2B nd H4 are completely masked when the histones are complexed with DNA. It is only when the nucleosome core structure is perturbed that these additional sites become accessible to the kinase. If long chromatin which contains H1 is phosphorylated, histone 1 is also phosphorylated by catalytic subunit at serine 38. However, the addition of excess H1 to H1-depleted long chromatin inhibits the phosphorylation of H3. In addition to the histones, the high mobility group (HMG) protein, HMG 14, was also found to be a good substrate for the kinase. Phosphorylation of HMG 17 in comparison was much less.
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PMID:The in vitro phosphorylation of chromatin by the catalytic subunit of cAMP-dependent protein kinase. 707 64

Chloride channels were previously purified from bovine kidney cortex membranes using a drug affinity column. Reconstitution of the purified proteins into artificial liposomes and planar bilayers yielded chloride channels. A 64-kDa protein, p64, identified as a component of this chloride channel was used to generate antibodies which depleted solubilized kidney membranes of all chloride channel activity. This antibody has now been used to identify a clone, H2B, from a kidney cDNA library. Antibodies, affinity-purified against the fusion protein of H2B also depleted solubilized kidney cortex from all chloride channel activity. The predicted amino acid sequence of p64 shows that it contains two and possibly four putative transmembrane domains and potential phosphorylation sites by protein kinase A, protein kinase C, and casein kinase II. There was no significant homology to other protein (or DNA) sequences in the data base. The protein is expressed in all cells tested. Expression of its mRNA in Xenopus laevis oocytes led to the insertion of a protein with the appropriate molecular mass in microsomes but not in the plasma membrane. It is likely that p64 represents the chloride channel of intracellular organelles.
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PMID:Molecular cloning and characterization of p64, a chloride channel protein from kidney microsomes. 768 8

The DNA-binding and phosphorylation properties of a rapidly phosphorylated nuclear 42-kDa phosphoprotein and of its two structurally related proteins, pp43 and pp44 in Chironomus tentans salivary glands were investigated. pp42, pp43 and pp44 bind promoter probes of the ecdysterone controlled I-18C gene and of the joint histone H2A/H2B genes in a sequence-selective and single-stranded DNA (ssDNA) specific manner. Rapid phosphorylation appears to give pp42 and pp43 uniquely hydrophilic characters making them soluble in the aqueous phase during phenol treatment. Dephosphorylation of the nuclear proteins markedly stimulates the ssDNA-binding activity of pp42 but not of pp43 and pp44. All three phosphoproteins are sensitive to heparin and the transcription inhibitor 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB) in vitro, but their sensitivity to heparin is more than one order of magnitude lower than that of casein kinase II. The heparin sensitivity of pp42 and pp43 is, however, similar to that described for a previously identified nuclear 42-kDa phosphoprotein in a Chironomus tentans epithelial cell line, casein kinase N42 (CKN42). pp42 and pp43 bind with high affinity to a Phosvitin-Sepharose matrix, like casein kinase I, II and N42, and can be eluted with high salt buffers from the affinity column. In intact salivary gland cells, microinjected (gamma-32P)GTP labels pp42 in a heparin sensitive manner, and this GTP-phosphorylation of pp42 could be competed out by a large excess of phosvitin. (gamma-32P)ATP-based phosphorylation of pp42 was uninfluenced by phosvitin in intact cells. The experimental data suggest that the salivary gland 42-kDa phosphoprotein, pp42, is a ssDNA-binding protein with characteristics of the epithelial CKN42.
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PMID:The salivary gland 42-kDa phosphoprotein is a single-stranded DNA-binding protein with characteristics of the epithelial casein kinase N42 in Chironomus tentans. 787 7

Histones H2A and H2B were found to be glycyrrhizin (GL)-binding proteins, because (i) the two histones H2A-H2B pairs were isolated selectively from the crude histone preparations of calf thymus by means of GL-affinity column chromatography (HPLC); (ii) phosphorylation of these two histones by A-kinase was remarkably stimulated by native GL or oGA (a derivative of glycyrrhetinic acid) at 20 microM; and (iii) in the crude histone preparations of calf thymus, these two histones were selectively phosphorylated by A-kinase in the presence of both dsDNA and 20 microM oGA or 20 microM GL. The provided data suggest that the GL-induced selective phosphorylation of histones H2A and H2B by A-kinase may be implicated in the transcriptional activation involved in the biological activities of the drug.
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PMID:The biological significance of glycyrrhizin- and glycyrrhetinic acid derivative-induced selective phosphorylation of histones H2A and H2B by A-kinase in vitro. 807 23

We have reported previously that histone H1 is capable of binding nucleotides such as ATP, GTP, ADP, and GDP in a specific manner. It is demonstrated here using labeling with the uv-crosslinkable ATP analog 8-azido-[alpha-32P]ATP that this ability is a unique characteristic of H1 among the histone proteins. Phosphate analogs such as AlF-4 efficiently counteract the labeling of H1, while they do not compete for labeling of histones H2A, H2B, H3, and H4. Consistent with the assumption that this labeling is due to specific binding, nucleotides competed for the labeling of H1 in a manner similar to labeling of the catalytic subunit of cAMP-dependent protein kinase, casein kinase-II, and heat shock protein-90, all of which are ATP/GTP-binding proteins. The site of nucleotide interaction was subsequently located in a Gly-rich region of H1 which displays homology with the protein kinases, using either radioactive labeling with nucleotide analogs and endoproteinase Glu-C digestion or synthetic peptides corresponding to the putative binding site. The results imply that specific protein structures are involved in nucleotide binding to H1 and that the ability of H1 to bind nucleotides may provide a mechanism for the regulation of eukaryotic gene expression.
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PMID:Nucleotide recognition by histone H1 involves specific protein structures. 777 3


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