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:2.7.7.6 (RNA polymerase)
34,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The monoclonal antibody P11 is directed against a 38 000 dalton protein of Drosophila melanogaster. On polytene chromosomes this protein is present in a subset of the RNA polymerase II-containing loci. Here we show by density centrifugation and enzyme-linked immunosorbent assay tests that the P11 antigen is part of nuclear ribonucleoprotein (RNP) complexes. Indirect immunofluorescence shows that, after prolonged heat-shock, the P11 antigen is present only in the heat-shock puff 93 D. Identical distribution patterns were obtained with another monoclonal antibody, Q18. Unlike P11, this antibody also cross-reacts with D. hydei and D. virilis polytene chromosomes, where the puffs 48 B and 20 CD, respectively, are the only loci prominently stained after heat-shock. The small and giant RNP complexes previously described in these puffs were also observed in puff 93 D. Both types of particle contain the P11 antigen as shown by immunoelectron microscopy. We suggest that the P11 antigen is associated with a special class of RNPs which are possibly involved in the storage of primary transcription products inside the nucleus.
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PMID:Heat-shock puff 93 D from Drosophila melanogaster: accumulation of a RNP-specific antigen associated with giant particles of possible storage function. 641 25

7-3 RNA (also known as K-RNA and 7SK-RNA) is a distinct small RNA found in insect to mammalian cells. Previous studies showed that this RNA is not capped, contains no modified nucleotides, is conserved through evolution, is synthesized by RNA polymerase III, and, in part, is associated by polyribosomes. In this study, the complete nucleotide sequence of 7-3 RNA was determined by RNA-sequencing methods, and the sequence is compared with several small RNAs and repetitive DNA sequences for homology. This 330-nucleotide-long RNA contained pppGp as its 5' terminus and exhibited heterogeneity with respect to the 3'-terminal AoH. The nucleotide sequence is: (sequence in text) The RNA is G-C rich, and evidence is presented that 7-3 RNA is in a ribonucleoprotein particle in the cytoplasm.
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PMID:Primary and secondary structure of 7-3 (K) RNA of Novikoff hepatoma. 643 39

Substrate RNAs are only efficiently spliced in HeLa whole-cell extract when they possess capped 5' termini. This cap requirement is observed with substrate RNAs prepared by transcription with either mammalian RNA polymerase II or bacterial RNA polymerase. Addition of less than 10 microM of cap analogs such as m7G(5')ppp(5')N or m7GTP strongly inhibits splicing of capped RNAs. This observation, as well as experiments following the fate of substrate RNA, indicates that the dependence of splicing on a cap structure is not due to an effect on RNA stability. More interestingly, cap analogs inhibit splicing when added at the start of the reaction but not at later times of incubation. This suggests that the cap recognition might be an important step in the formation of a specific ribonucleoprotein complex required for splicing.
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PMID:Recognition of cap structure in splicing in vitro of mRNA precursors. 656 84

DNA-dependent RNA polymerase was partially purified from wheat germ extract and tested for inhibition by antinuclear autoantibodies from the sera of patients with connective tissue diseases. The enzyme was inhibited by anti-DNA and by autoantibodies to the nuclear ribonucleoprotein nRNP. Autoantibodies to other ribonucleoproteins (Sm, Ro, La) did not cause inhibition. The enzyme preparation was shown to contain material with Ro and La antigenic activity but there was no nRNP or Sm detectable by immune precipitation. Previous work [3] has shown inhibition of prokaryotic (E. coli) RNA polymerase by anti-DNA, and our results show that the eukaryotic enzyme, in this case from wheat germ, is also inhibited. The results are consistent with the suggestion that inhibition by anti-DNA is due to template masking. Inhibition of RNA polymerase by antibodies to cellular ribonucleoprotein suggests that the antigen is in some way associated with the activity of the enzyme.
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PMID:Effects of antinuclear autoantibodies on RNA polymerase. 660 60

Anti-La antibodies are frequently found in patients with autoimmune diseases; the antigen was reported to be a 50,000-Da protein (Rinke, J., and Steitz, J. A. (1982) Cell 29, 149-159). Because this protein was associated with many nascent RNA polymerase III transcripts, it was suggested to be an RNA polymerase III transcription factor. The present study was designed to analyze 4.5 I ribonucleoprotein, an RNA polymerase III transcript which contains the La antigen. It was found that the 3'-end 20-30-nucleotide portion was the most protected portion of 4.5 I RNA when 4.5 I ribonucleoprotein was digested with T1 RNase. When U2 RNA (an RNA polymerase II transcript) and 4.5 I RNA were incubated with the S-100 fraction of Novikoff hepatoma cells, the 4.5 I RNA bound La antigen but the U2 RNA did not. When partial and complete T1 RNase digestion fragments of 4.5 I RNA were incubated with the S-100 fraction, the 3'-end fragments bound preferentially to the La antigen. However, the fragments of 4.5 I RNA bound less efficiently to La antigen than whole 4.5 I RNA. These results indicate that the 3'-end of 4.5 I RNA is the La antigen binding site in this molecule and suggest that the overall conformation of RNA aids in the binding of La antigen.
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PMID:Identification of a La protein binding site in a RNA polymerase III transcript (4.5 I RNA). 686 91

The transcriptase activity of influenza A virus ribonucleoproteins was inhibited by 42 to 49% in vitro in the presence of membrane (M) protein. The addition of M protein to the system of ribonucleoprotein preparations isolated from rimantadine-sensitive or rimantadine-resistant influenza virus strains, as well as the addition of M protein isolated from a sensitive strain, in the presence of rimantadine further inhibited the transcriptase activity of such complexes by approximately 40%. In the system containing the same ribonucleoprotein preparations, but with M protein isolated from a rimantadine-resistant influenza virus strain, the transcriptase activity was not sensitive to rimantadine. The data show that M protein can influence the activity of influenza A virus virion transcriptase and that the susceptibility of influenza virus to rimantadine may be due to the peculiarities of M protein.
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PMID:Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine. 689 43

The assembly of heterogeneous nuclear RNA (hnRNA) into ribonucleoprotein (RNP) particles has been investigated during in vitro transcription in isolated nuclei. Approximately 80% of the in vitro transcription observed in mouse Friend erythroleukemia cell nuclei is attributable to the activity of RNA polymerase II. In vitro hnRNA transcripts are assembled into particles having the same properties as the nuclear ribonucleoprotein (hnRNP) particles in which hnRNA is found in vivo. Direct contact of hnRNP proteins with newly transcribed hnRNA was demonstrated by nuclease protection experiments and by the covalent transfer of 32P-labeled nucleotides from [alpha-32P]UTP-labeled hnRNA transcripts to specific proteins by RNA--protein crosslinking followed by nuclease digestion and electrophoresis of the nucleotide-bearing proteins. The availability of an in vitro system for hnRNP assembly opens a new route for investigating the functional relationship between nuclear structure and mRNA processing.
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PMID:Assembly of nuclear ribonucleoprotein particles during in vitro transcription. 695 Nov 90

Autoantibodies from patients with systemic lupus erythematosus and other related diseases have been used to identify and study small RNA-protein complexes from mammalian cells. Properties of three previously described and several new classes of small ribonucleoproteins (RNPs) are reviewed. The sequence of Drosophila U1 RNA reveals that the region proposed to pair with 5' splice junctions is conserved, while that proposed to interact with 3' junctions diverges; this forces some revision of the model for U1 small nuclear (sn)RNP participation in hnRNA splicing. Further characterization of the Ro and La small RNPs has shown that the Ro small cytoplasmic (sc)RNPs are a subclass of La RNPs. Both tRNA and 5S rRNA precursors are at least transiently associated with the La protein. This raises the possibility that the La protein may be an RNA polymerase III transcription factor.
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PMID:Structure and function of small ribonucleoproteins from eukaryotic cells. 716 47

The ribonucleoprotein core of reovirus is a multienzyme complex that transcribes messenger ribonucleic acid (mRNA) from double-stranded RNA templates. So far, the core has resisted attempts to disassemble it and identify the polypeptide species responsible for RNA polymerase activity. As an alternative approach, we tested pyridoxal 5-phosphate (PLP) as a potential affinity labeling reagent for reovirus transcriptase in vitro; PLP has been used as an affinity reagent for cellular and viral nucleic acid polymerases. We found that PLP inhibited reovirus transcriptase reversibly (apparent Ki = 0.2 mM), but the inhibition was noncompetitive with respect to each of the four ribonucleoside triphosphates. This interaction required both the aldehyde and phosphate moieties in PLP, since pyridoxamine and pyridoxal were relatively inactive. To identify the polypeptides involved, we labeled the PLP--core complex by reductive alkylation with [3H]borohydride. At PLP concentrations close to the apparent Ki, labeling was selective for the two largest virion polypeptides, lambda 1 and lambda 2. At saturation, there were only 10 high-affinity PLP binding sites per core in each of the lambda polypeptide species. These findings implicate either or both lambda polypeptide species in viral transcription and they indicate that a special population, representing no more than 10% of the total lambda molecules in each core, participates in RNA synthesis.
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PMID:Pyridoxal phosphate as a probe of reovirus transcriptase. 735 41

Ro ribonucleoprotein particles (Ro RNPs) are complexes of several proteins with a small RNA polymerase III-transcribed Ro RNA. Despite their relative abundance and evolutionary conservation no function has as yet been ascribed to these complexes. Also their subcellular distribution is still largely unknown as immunofluorescence studies concerning their localization have produced conflicting data. We have used cell enucleation to fractionate cells into cytoplasmic and nuclear fractions. Analysis of these fractions revealed an exclusively cytoplasmic localization for the Ro RNPs. The majority of the Ro RNAs are shown to be stably associated with all three known Ro RNP proteins. Although no Ro RNAs could be detected in the nuclear fraction, the Ro RNP-specific proteins were abundantly present. These nuclear non-Ro RNA-associated proteins are shown to be capable of binding Ro RNAs.
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PMID:Subcellular distribution of Ro ribonucleoprotein complexes and their constituents. 750 49


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