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)

Total poly(A)-mRNA from polyribosomes of MOPC 21 mouse myeloma were investigated. Poly(A)-mRNA was released by two successive chromatography on oligo (dT)-cellulose. A 14S fraction of total poly(A)-mRNA was obtained and partially purified by sucrose gradient centrifigation followed by acrylamide gel electrophoresis. As estimated from the electrophoretic analysis, the 14S mRNA has three components, one of which appears to be 18S rRNA and two others--mRNAs with molecular weight of 5.2.10(5) and 3.8.10(5), respectively. Total poly(A)-mRNA and partially purified 14S mRNA were active when employed as a template in a reverse transcription and cell-free system from wheat germ. DNA complementary to the 14S mRNA was prepared with avian myeloblastosis virus RNA-dependent DNA polymerase. This cDNA was heterogeneous in size with the average size of about 800 nucleotides when analyzed by gel electrophoresis in 98% formamide. The maximal length was about 1100 nucleotides that consistent with full template length. About half of the translation product directed by the 14S mRNA migrated as mature L-chain Ig (upon polyacrylamide gel electrophoresis in sodium dodecylsulfate). The presented data suggested that 14S mRNA species contain mRNA L-chain Ig.
Mol Biol (Mosk)
PMID:[mRNA of mouse plasmacytoma. Reverse transcription and translation in cell-free systems]. 8 67

Poly(A) containing rat liver 21S RNA homogeneous in polyacrylamide gel electrophoresis under denaturing conditions and stimulating the synthesis of ceruloplasmin in a cell-free proteinsynthesizing system, was used as a template for reverse transcription in the presence of T10 primer and highly purified reverse transcriptase from avian myeloblastosis virus. The cDNA made this way was characterized by means of hybridization kinetics with mRNA, by melting of the hybrids formed and by chain length measurements. To increase the degree of representativity, the ceruloplasmin mRNA was fragmented by mild alkaline treatment, enzymatically polyadenylated and transcribed. The cDNA made was fully characterized and the kinetic complexity measured by hybridization with the mRNA was found to be equal to 2300 nucleotides as compared with the value of 3000 nucleotides is expected from gel electrophoresis data. The observed difference may indicate the presence of repeated sequences in the given mRNA. The sufficient representativitness of the synthesized cDNA and its specificity with respect to ceruloplasmin mRNA allows to use it as a molecular probe to study the ceruloplasmin gene structure.
Mol Biol (Mosk)
PMID:[Enzymatic synthesis and characterization of DNA complementary to ceruloplasmin mRNA from rat liver]. 9 44

Progesterone causes in goblet cells of oviducts of estrogen hormone-stimulated immature quails selectively gene activation without affecting DNA synthesis. This biological model has been used to study the influence of poly ADP-ribosylation during the processes of DNA transcription. Administration of progesterone in vivo causes an increase of the activity of RNA polymerase I and II in isolated nuclei. This increase is accompanied by a marked decrease of the specific activity of poly (ADP-Rib) polymerase. After in vitro ADP-ribosylation of nuclear proteins the template capacity of chromatin for ""exogenous'' RNA synthesis (with E. coli DNA-dependent RNA polymerases) as well as for ""endogenous'' RNA synthesis with DNA dependent RNA polymerases II is not affected, whereas the data presented seem to indicate that the capacity for RNA synthesis mediated by ""endogenous'' DNA-dependent RNA polymerase I might be inhibited after ADP-ribosylation. Evidence is presented to show that a considerable amount of poly (ADP-Rib), synthesized by poly (ADP-Rib) polymerase in isolated nuclei, is linked with RNA polymerase I. The rate of synthesis of poly (ADP-Rib) is dependent on the incubation temperature (optimum at 25 degrees C) and it can be inhibited by the specific inhibitors of poly (ADP-Rib) polymerase nicotineamide, thymidine and formycin B. Poly (ADP-Rib) is probably associated with RNA polymerase I through a covalent linkage. ADP-ribosylated RNA polymerase I has been purified 550 fold with respect to the nuclear extract corresponding to a 4,000 fold purification from the whole cell homogenate. The ratio between poly (ADP-Rib), formed during preincubation of nuclei with NAD, and RNA polymerase I remains almost constant during the purification procedures. The extent of ADP-ribosylation of RNA polymerase I decreases during gene expression. Thus we conclude that poly ADP-ribosylation of this enzyme is one of the regulatory mechanisms by which specificity of DNA transcription is achieved.
Mol Cell Biochem 1976 Sep 30
PMID:Poly ADP-ribosylation of DNA-dependent RNA polymerase I from quail oviduct. Dependence on progesterone stimulation. 18 9

The distribution of poly(A)+ mRNA among polysomes, monosomes, and ribosome-free supernatant fractions after mengovirus infection of Ehrlich ascites tumor (EAT) cells was investigated employing sucrose gradient centrifugation of their corresponding postnuclear supernatants. Poly(A)+ mRNA was isolated from sucrose gradient fractions and quantitated in a cell-free protein synthesizing system from uninfected EAT cells. It was also localized by annealing [3H]-poly(U) to the poly(A)-tracts of mRNA present in the sucrose gradient fractions. Both experiments revealed a gradual shift of host poly(A)+ mRNA from large to small polysomes and monosomes, respectively, with the time postinfection. The greatest part of host template RNA appears to remain ribosome-bound and only a fraction seems to be detached from the ribosomes in the course of mengovirus infection. At the end of the infectious cycle, 8 h postinfection, approximately 70% of the poly(A)+ mRNA detected in uninfected cells is still biologically active, but not translated in vivo, in agreement with data from the [3H]poly(U)hybridization experiment.
Mol Biol Rep 1978 Feb 28
PMID:Localization of host poly(A)+ mRNA in the ribosome profile of mengovirus-infected Ehrlich ascites tumor cells. 20 76

The selection at 22 degrees C of yeast cordycepin (3'-deoxyadenosine) sensitive mutants which would be temperature-sensitive at 37 degrees C allowed the obtention of mutants specifically impaired in processing of Poly(A)-containing RNAs at 37 degrees C. The mutants displaying this phenotype belong to two different loci. The biochemical study of the physiological function which is blocked by the mutation has revealed that the level of radioactive Poly(A)-containing RNAs found in a 5 min pulse after a 10 min shift at 37 degrees C is 6 times less in the mutants than in the wild type without reduction of the non Poly(A)-containing RNAs fraction. Further studies have shown no alteration in the two Poly(A) polymerases activities and suggest strongly a faster decay of Poly(A)-containing RNAs in the mutants.
Mol Gen Genet 1978 Oct 04
PMID:Yeast temperature-sensitive mutants specifically impaired in processing of poly(A)-containing RNAs. 36 72

Highly purified preparations of mRNA coding for ceruloplasmin (CP) ere isolated from rat liver polyribosomes using indirect immunoprecipitation of CP polysomes and poly(U)-sepharose chromatography of polysomal RNA. The homogeneity of CP mRNA was as high as 86--90%. The molecular weight of CP mRNA is 1.3 . 10(6) daltons which is in excess when compared to the minimal size of mRNA necessary to code for CP precursor (about 700 amino acid residues). The base composition of CP mRNA is of AU-type. The experiments on end-labeling with [3H]borohydride after periodate oxidation whowed that CP mRNA contains 3'-terminal poly(A). Poly(U)-sepharose chromatography with stepwise temperature elution revealed length heterogeneity of poly(A) consisting of particular, different thermal subfractions of CP mRNA contain poly(A) consisting of 38, 90 and 165 adenylate residue. 5'-end of CP mRNA is block with inverted 7-methylguanosine (m7G) which is reducible with [3H]borohydride after periodate oxidation. This m7G residue is a component of RNAse- and alkali-resistant oligonucleotide, which structure according to net charge value and its shifts after various enzymatic treatments, is m7G5'ppp5'XmpAp.
Mol Biol (Mosk)
PMID:[Physico-chemical characteristics of highly purified ceruloplasmin mRNA from rat liver]. 50 63

Poly(A)RNA extracted from the anterior lobe of bovine-pituitary tissue was transcribed into its complementary DNA with reverse transcriptase. This 3H-labeled cDNA was hybridized with its template RNA. Hybridization kinetics revealed at least 3 abundance classes with the highest abundance class consisting of only a few different sequences. Bovine-liver poly(A)RNA did not contain this highest abundance class when hybridized to the cDNA probe complementary to pituitary poly(A)RNA. This result suggested that the highest abundance class found in bovine-pituitary poly(A)RNA was specific for that tissue and most likely contained the mRNA sequences for the major pituitary hormones.
Mol Cell Endocrinol 1979 Nov
PMID:Sequence complexity of bovine pituitary poly(A)RNA. 51 Jul 72

Some properties of a submitochondrial cell-free system for protein synthesis are described. The system was prepared from rat liver mitochondria lysed with Triton X-100, and the lysate was characterized by a linear rate of [14C]amino acid incorporation for 15-20 min with subsequent decline in activity. The incorporation reaction was inhibited by chloramphenicol and was insensitive to cycloheximide. Poly(U) addition stimulated [14CA1phenylalanine incorporation by the preincubated submitochondrial system. Upon the addition of 7.5S mRNA that was isolated from mitochondria the major translation product was identified as a hydrophobic poly-peptide which in some properties (solubility in chloroform-methanol mixture) was similar to one of polypeptides synthesized by the sub-mitochondrial system on endogeneous mRNAs.
Mol Cell Biochem 1977 Feb 04
PMID:On the cell-free system of protein synthesis from mammalian mitochondria. 85 30

Poly(A)-containing 9S RNA from chick reticulocytes was electrophoresed on formamide-polyacrylamide gels. The molecular weight was determined to be 211 000 +/- 10 000 daltons. The RNA was separated into three different fractions with respect to molecular weight. These RNAs were translated in a wheat germ cell-free system. The lower molecular weight RNA directed up to 95% alpha-chain synthesis, compared to 60% for the higher molecular weight RNA. This was accompanied by a relative increase for beta-chain synthesis with increasing molecular weight. It could also be shown by hybridization with labelled poly(U) that the average poly(A) length decreased from about 83 nucleotides for fraction I to 36 nucleotides for fraction III. Our results suggest that fractionation of avian 9 S globin mRNA by electrophoresis on formamide-polyacrylamide gels is dependent upon two parameters, namely differences in the lengths of the non-poly(A)-containing portion of the alpha and beta mRNAs and differences in the poly(A) lengths.
Mol Biol Rep 1976 Nov
PMID:Molecular weights, poly(A)--content, and partial separation of chick globin mRNAs. 101 77

Poly(A) containing ribonucleoprotein particles were prepared from rat liver nuclei and polyribosomes. The particles have sedimentation coefficients of 14 S and 9 S, respectively. In CS2SO4 density gradients the particles banded at densities of 1.28-1.29 g cm-3. Both nuclear and polyribosomal poly(A)-RNP contain in addition to some minor polypeptides, two main polypeptides having molecular weights of 63 000 and 90 000 dalton, respectively indistinguishable from each other according to their electrophoretic mobilities.
Mol Biol Rep 1976 Nov
PMID:Nuclear and polyribosomal ribonucleoprotein particles containing poly (A) in rat liver cells. 101 81


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