Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Murine splenocytes release a novel repressing activity of Concanavalin A-induced lymphocyte DNA synthesis. This activity was purified by gel filtration, ion exchange and thin layer chromatography. It was characterized to be a heat-stable peptide whose molecular weight was estimated to be about 1 000 daltons. The strong inhibition by this peptide was observed when added at early periods of the cell culture. This factor does not affect early RNA synthesis in lymphocytes, but nucleotide (UTP) incorporation at early periods was considerably decreased. In addition, although the factor inhibits drastically lymphocyte DNA synthesis, the cell viability is not changed significantly. These results suggest that the peptide suppresses the cell membrane function at early periods and specifically blocks the concomitant DNA synthesis.
Mol Biol Rep 1984 Jul
PMID:Murine splenocytes release an inhibitory peptide of lymphocyte DNA synthesis into serum-free culture medium. 620 87

Ribonuclease (RNase) was isolated and purified from the excretory gland cells of Stephanurus dentatus by (NH4)2SO4 fractionation, column chromatography on phosphocellulose and affinity chromatography using 5' -UTP-agarose. The purified enzyme hydrolyzed yeast RNA, cyclic nucleotides, and polynucleotides. Hydrolysis products of RNA and synthetic substrates were analyzed by column chromatography and/or thin-layer chromatography and the results indicated that S. dentatus RNase should be classified as an endoribonuclease (EC 3.1.27.1). Experimentally infected pigs produced antibodies against the RNase as shown by immunodiffusion and immunoelectrophoresis. The RNase was also secreted by adult worm into an in vitro maintenance medium. The RNase may function in the worm to degrade TNA as a source of nucleotides for metabolic purposes.
Mol Biochem Parasitol 1982 Feb
PMID:Purification and properties of a ribonuclease from the excretory gland cells of Stephanurus dentatus. 621 Aug 45

It is thought that eucaryotic elongation factor eEF-Ts catalyzes the replacement of GDP for GTP on eucaryotic elongation factor eEF-Tu. We have found that eEF-Ts displays a strong nucleoside diphosphate phosphotransferase activity. This transferase activity resides in a dimer molecule of a subunit molecular weight close to 30,000. The transfosforylating activity of eEF-Ts results in a stimulatory effect of ATP, GTP, UTP and CTP on protein synthesis provided that GDP is present. The specificity for guanine nucleotides in protein synthesis resides only in eEF-Tu.
Mol Biol Rep 1981 Aug 14
PMID:Protein synthesis in artemia salina. Eucaryotic elongation factor eEF-Ts is a transphosphorylase. 627 May 47

The cytoplasmic glucocorticoid receptor of X. laevis liver has a high affinity for [3H]dexamethasone (Kd, 0.3 x 10(-8) M), and its binding specificity for a variety of steroids is similar to that found for mammalian glucocorticoid receptors. The ability of this receptor to bind [3H]-dexamethasone is stable at 0 degrees C but is rapidly lost at 10 and 20 degrees C. Alkaline phosphatase increases, whereas molybdate and tungstate decrease, the rate at which the binding activity is lost. These results are consistent with the loss of binding activity being due to dephosphorylation of the receptor. Binding of [3H]dexamethasone to the receptor does not alter the rate at which the binding activity is lost but does increase the stabilizing effect of molybdate. 100 mM molybdate lowers the apparent affinity of the receptor for [3H]dexamethasone, suggesting that molybdate can interact with the X. laevis glucocorticoid receptor. Addition of UTP, but not ATP, GTP or CTP, reactivates the receptor-binding activity, which indicates that the receptor may be phosphorylated by a UTP-dependent protein kinase.
Mol Cell Endocrinol 1982 Apr
PMID:Glucocorticoid receptor of X. laevis: possible effect of phosphorylation on hormone binding. 628 68

Two yeast DNA pools inserted in a hybrid Escherichia coli-yeast vector pFL1 were used to transform E. coli and yeast aspartate-transcarbamylase-less strains to prototrophy. From the first pool--a BamHI yeast DNA digest--a 6.4 kb BamHI fragment was recovered that gave good complementation of the E. coli auxotrophy but poor complementation of the yeast auxotrophy. From the second pool--a partial Sau3A yeast DNA digest--five independent plasmids complementing either E. coli, yeast, or both were recovered. Each of the five plasmids possessed sequences in common with the 6.4 kb BamHI fragment. One of these plasmids, which complemented the two URA2 activities in yeast and which produced a carbamyl-phosphate synthetase, aspartate-transcarbamylase complex sensitive to UTP feedback inhibition contained the full URA2 gene. A restriction map of the URA2 gene has been constructed and seven different consecutive segments have been recloned in pBR322 to measure their hybridization with URA2 messenger RNA, allowing us to estimate the limits of the gene.
Mol Gen Genet 1982
PMID:Cloning and restriction mapping of the yeast URA2 gene coding for the carbamyl phosphate synthetase aspartate-transcarbamylase complex. 628 48

Guanylyltransferase, an enzyme that catalyzes formation of mRNA 5'-terminal caps, was isolated from HeLa cell nuclei. The partially purified preparation, after incubation with [alpha-32P]GTP, yielded a single radiolabeled polypeptide by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The guanylylated product was stable at neutral and alkaline pHs and had a pI of 4 by isoelectric focusing. An apparent molecular weight of approximately 68,000 was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions. The formation of a covalently linked, radiolabeled GMP-protein complex and the associated release of PPi required the presence of [alpha-32P]GTP and divalent cations and incubation between pH 7 and 9. Reaction with [beta-32P]GTP, [alpha-32P]CTP, [alpha-32P]UTP, or [alpha-32P]ATP did not label the approximately 68,000-dalton polypeptide. Phosphoamide linkage of the GMP-enzyme complex was indicated by its sensitivity to cleavage by acidic hydroxylamine or HCl and not by NaOH or alkaline phosphatase. Both formation of the GMP-enzyme intermediate and synthesis of cap structures of type GpppApG from GTP and ppApG were remarkably temperature independent; the rates of enzyme activity at 0 to 4 degrees C were 30% or more of those obtained at 37 degrees C. Radiolabeled GMP-enzyme complex, isolated by heparin-Sepharose chromatography from reaction mixtures, functioned effectively as a GMP donor for cap synthesis with 5'-diphosphorylated oligo- and polynucleotide acceptors. Alternatively, protein-bound GMP could be transferred to PPi to form GTP. The formation of a guanylylated enzyme intermediate appears to be characteristic of viral and cellular guanylyltransferases that modify eucaryotic mRNA 5' termini.
Mol Cell Biol 1982 Aug
PMID:Covalent guanylyl intermediate formed by HeLa cell mRNA capping enzyme. 629 Aug 77

Two UTP-utilizing uridylyltransferases which react with both glucose 1-phosphate and galactose 1-phosphate were isolated from cell-free extracts of Entamoeba histolytica. The more specific of these enzymes, glucose-1-phosphate uridylyltransferase, acts preferentially on glucose 1-phosphate, having a maximum velocity 20-fold greater with this substrate than with galactose 1-phosphate. It was purified 200 fold with a 25% yield and has a molecular weight of 45 000. This enzyme requires a reducing agent for stability. The less specific transferase reacts with both hexose phosphates, having a maximum velocity of 1.35 times greater with galactose 1-phosphate. It was purified 1000 fold with a 20% yield, and has a molecular weight of 40 000. The common Leloir enzyme, UDP glucose-hexose-1-phosphate uridylytransferase (EC 2.7.7.12), was not found in this organism. To avoid confusion with the Leloir enzyme our experience suggests that the less specific enzyme, which is presently referred to in the literature as galactose-1-phosphate uridylyltransferase (EC 2.7.7.10), should be named UTP:hexose-1-phosphate uridylyltransferase (EC 2.7.7.?). The more specific enzyme (EC 2.7.7.9) should be more clearly named UTP:glucose-1-phosphate uridylyltransferase.
Mol Biochem Parasitol 1983 Feb
PMID:Separation and characterization of two UTP-utilizing hexose phosphate uridylyltransferases from Entamoeba histolytica. 630 12

Isolated nuclei derived from simian virus 40 (SV40)-infected cells and incubated with [alpha-32P]UTP can elongate the in vivo preinitiated SV40 late RNA, synthesizing a viral RNA species 94 nucleotides long (attenuator RNA) as well as longer RNA molecules. In contrast to newly synthesized SV40 RNA, the attenuator RNA is not associated with the nuclear matrix. Pretreating the cells with 5,6-dichloro-1-beta-ribofuranosylbenzimidazole before the incubation of isolated nuclei in vitro, enhances the accumulation of the attenuator RNA, but again it is removed from nuclei by DNase and high salt. In contrast, pretreating the cells with proflavine, an intercalating drug that interferes with RNA secondary structure, prevents the accumulation of the attenuator RNA and increases the amount of the long RNA molecules. These RNA molecules become associated with the nuclear matrix. Isolated nuclear matrices from SV40-infected cells are highly enriched in transcriptionally active ternary complexes. Thus, isolated nuclear matrices that contain from 2 to 6% of SV40 DNA are capable of synthesizing at least 35% of the viral RNA synthesized in isolated nuclei after 2 to 15 minutes incubation with [alpha-32P]UTP. The RNA synthesized in vitro on purified nuclear matrices and isolated nuclei is derived from the same regions of the viral genome, suggesting that there is an association between transcribed DNA sequences and the nuclear matrix. The results suggest a major role for the nuclear matrix in controlling SV40 gene expression.
J Mol Biol 1984 Feb 05
PMID:Control of late simian virus 40 transcription by the attenuation mechanism and transcriptionally active ternary complexes are associated with the nuclear matrix. 631 19

We have previously demonstrated that transcription of the adenovirus type 2 (Ad2) late promoter in vitro under UTP-limiting conditions results in pauses by the elongating RNA polymerase II between positions +6 and +17. We report here the purification of complexes between the paused RNA polymerase and a 260 base-pair Ad2 promoter-bearing DNA fragment. The procedure involves sedimentation through sucrose gradients, electrophoresis in agarose gels, and electroelution from the gels; the final complex pool is completely active in chain elongation. We observe a sharp discontinuity in complex stability during purification as a function of the number of bases added to the growing chains: complexes in which the polymerase has added more than ten bases are stable and are active in chain elongation even after the electroelution step, whereas complexes containing seven or fewer bases dissociate very easily. When purified complexes are extensively digested with proteinase K their electrophoretic mobility is increased considerably, yet they remain fully active in chain elongation. If purified complexes are digested with DNase I their electrophoretic mobility does not change. When the nuclease-treated complexes are allowed to continue chain elongation, they are able to add approximately 20 more bases to the nascent chains.
J Mol Biol 1984 Sep 15
PMID:Purification and characterization of ternary complexes containing accurately initiated RNA polymerase II and less than 20 nucleotides of RNA. 649 55

The transcription of the beta-globin genes in mouse erythroleukemia cells has been examined by hybridizing labeled RNA obtained from isolated nuclei after chain elongation in the presence of [alpha-32P]UTP. There is induction of at least 30-fold of beta maj globin transcription after cells are treated with either dimethylsulfoxide or hexamethylene bisacetamide. The induction requires 36 to 48 hours to be maximal, during which time the cells double about three to four times. During this time, a site in the beta maj DNA region becomes hypersensitive to DNase. The development of this hypersensitive site is co-ordinate with the transcriptional increase. The induced transcripts in the beta-globin region are alpha-amanitin-sensitive (and therefore are RNA polymerase II products). An examination of weak transcriptional signals to DNA fragments upstream of the beta maj globin gene in uninduced mouse erythroleukemia cells and in cells that do not make globin is also reported. The low level of hybridization to the upstream regions in uninduced erythroleukemia cells, in L cells (a fibroblast) and in a strain of erythroleukemia cells that no longer make globin are not equally sensitive to alpha-amanitin as in the induced signal. These experiments help define the inducible transcription unit for beta maj globin mRNA production.
J Mol Biol 1984 Feb 05
PMID:Induced transcription of the mouse beta-globin transcription unit in erythroleukemia cells. Time-course of induction and of changes in chromatin structure. 658 80


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