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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nuclear ribonucleoprotein (RNP) complexes that contain the U1 and U2 RNA of chromatin of Novikoff hepatoma cells were extracted with 0.01 M Tris-HCl (pH 8.0) after the nuclei were initially washed with 0.075 M NaCl and 0.025 M EDTA (pH 8.0). These RNP complexes were purified by chromatography on Sepharose 6B columns and centrifugation on sucrose density gradients. The identity of the U1 and U2 RNA in these particles was established by their electrophoretic mobility in polyacrylamide gels and their T1 RNase fingerprints which were identical with those of authentic U1 and U2 RNA (R. Reddy et al. (1974), J. Biol. Chem.249, 6486-6494; H. Shibata et al. (1974), Mol. Cell. Biochem. 4, 3-19). The nuclear riboncleoproteins had a buoyant density of 1.47 g/ml in CsCl gradients. Two-dimensional polyacrylamide gel electrophoresis of their proteins showed these RNP complexes contain 10 polypeptide spots, of which two are phosphorylated in vivo.
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PMID:Nuclear ribonucleoprotein complexes containing U1 and U2 RNA. 16 94

Particles carrying heterogeneous nuclear RNA (30 S-particles) were prepared from rat liver and Zajdela hepatoma ascites cell nuclei after ultrasonic disruption. The ribonucleoprotein structures were disintegrated in the presence of 100mM spermidine. Using chromatography on Sepharose-polyadenylate a protein component has been obtained which possessed high affinity for heterogeneous nuclear RNA, polyuridylate and polyadenylate, and double-stranded DNA. This protein was the main species of the ribonucleoprotein studied; it showed bands with molcular weights of 37000 and 40000 respectively in SDS gel electrophoresis. The RNA-binding proteins isolated from liver and hepatoma had identical molecular weights and the same affinity for Sepharose-polyadenylate used in the isolation.
Mol Biol Rep 1977 Sep
PMID:Preparation in undenatured form of the main protein bound to heterogeneous nuclear RNA in liver and hepatoma cells. 19 32

A review is made of the experimental results obtained by the author and co-workers on the study of the structural organization of the RNA and the protein in ribosomes by the method of joint use of light, X-ray and neutron scattering and by the method of contrast variation in neutron scattering. Two rules are formulated for the folding of the ribonucleoprotein strand in ribosomes: (1) in each ribosomal subparticle the RNA is concentrated predominantly closer to the center of the particle whereas the protein has a more peripherical localization; (2) the compact ("crystallic") packing of hydrated RNA helices is an essential feature of the nucleus (nuclei) organization of the particles. An analysis of the experimental data on neutron scattering by ribosomal proteins has been done and the globulin conformation in solution of some of these proteins has been established. The widespread concept according to which the majority of ribosomal proteins on the ribosome and in solution are enlongated expanded structures is disputed. It is suggested that all, or almost all, ribosomal proteins are usual globular proteins recognizing the specific sequence of RNA on the periphery of the particles, and , hence, that the formation of functional centrers on the ribosome is, in principle, analogous to the formation of functional centers of other complex proteins with a quaternary structure.
Mol Biol (Mosk)
PMID:[Internal structure of ribosomes using different types of emission]. 38 92

Cold-sensitive mutants of Saccharomyces cerevisiae isolated by tritium suicide were screened for defects in ribosome biosynthesis. The biochemical defects of mutant dip-1 (defective in processing) were characterized; it is defective in ribosome biosynthesis at the level of production of the primary 35S transcript. At restrictive conditions mutant dip-1 accumulates abnormal rRNA in addition to wild-type rRNA. In the mutant the first observable transcription product was a 14SRNA species which had sequence homologies to 18S rDNA and was the major rRNA component of the 40S ribosomal subunit. In addition, the ribonucleoprotein particles of dip-1 harbored RNA molecules with homologies to yeast rDNA which comprises the spacer region between 18S and 25S rDNA cistrons. Possible causes for the defective production of rRNA and its assembly into subunits are discussed.
Mol Gen Genet 1979 Oct 01
PMID:A cold-sensitive mutant of Saccharomyces cerevisiae defective in ribosome processing. 39 31

The intracellular influenza virus-containing structures involved in RNA synthesis in the cytoplasm and in the nucleoplasm of infected chicken fibroblasts were studied. Two approaches were used: (1) short pulse labeling of infected cell with [3H]uridine; (2) determination in vitro of polymerase activity of intracellular virus-specific structures. Both methods revealed functionally active virus-specific structures in the nucleoplasm and showed that a functionally active virus-specific structure was localized in the nucleoplasm of infected cells. This structure contained proteins of the viral ribonucleoprotein, but sedimented somewhat faster (at 60--90S in velocity sucrose and glycerol gradients). Meanwhile, polymerase-containing structures in the cytoplasm of infected cells sedimented in the position of viral ribonucleoproteins (25--60S).
Mol Biol (Mosk)
PMID:[Intracellular structures of influenza virus]. 65 75

Rat liver nuclear 30 S ribonucleoprotein particles containing pre-mRNA and nuclear sap proteins have been shown to modify in vitro the synthetic dinucleotide ppGpC in the presence of GTP and S-adenosyl-L-methionine (SAM) by the formation of a blocked and methylated (capped) structure 7(meG(5')ppp(5'-GmepC. In the absence of SAM the predominant reaction was GpppGpC. Our results indicate that the 30S ribonucleoprotein particles (informofers) as well as the proteins of the nuclear sap possess both guanylyltransferase, N7-, and 2-o-methyltransferase activities.
Mol Biol Rep 1978 Jun 16
PMID:Methylated cap formation by enzymes bound to nuclear informofer particles. 68 86

Duck- and rabbit globin messenger ribonucleoprotein complexes isolated by oligo(dT) cellulose chromatography reveal an identical protein pattern-two main proteins of molecular weights of 73,000 and 49,000 daltons and minor components-whether the complexes have been liberated from polyribosomes with the EDTA- or the puromycin-high-salt method. In the globin messenger ribonucleoprotein particles of both species predominantly the protein with a molecular weight of 73,000 daltons is attached to poly(A)-containing regions of the messenger RNAs.
Mol Biol Rep 1975 Dec
PMID:EDTA-and puromycin-derived duck- and rabbit globin-messenger ribonucleoprotein complexes isolated by oligo (dT)-cellulose chromatography. 81 7

Rat liver mitochondrial polyribosomes were isolated free from cytoplasmic ribonucleoprotein contaminations in a number of criteria (sedimentation and buoyant density patterns, ribosomal RNA composition). Heterogeneous poly A containing RNA from mitochondrial polysomes was purified by two-stage cellulose chromatography. This RNA was in vitro labelled with 125I up to specific activity approximately 10(6)-10(7) cts.min-1.microng-1 and used for hybridization experiments with separate complementary strands of mitochondrial DNA and nuclear DNA fragments. The proportions of mitochondrial poly A containing RNA that is complementary to heavy and light strands of mtDNA were respectively 31.5% and 8.3%. Besides, a significant RNA fraction was complementary to unique sequences of nuclear DNA (2-3 copies per haploid genome). The hybrids that were formed possessed a high Tm indicative of a perfect base pairing. A dual intracellular origin of mitochondrial messenger RNA is discussed.
Mol Cell Biochem 1977 Feb 04
PMID:Polyribosomes and messenger RNA from rat liver mitochondria. 85 43

A novel method of RNA fractionation based on a gradual release of the RNA molecules from ribonucleoprotein complexes has been used for the analysis of ribosomal and non-ribosomal complexes of rat liver cytoplasm. Adsorption of native ribonucleoproteins on a Celite column (occuring through only the protein moiety) followed by a consequent dissociation of RNP complexes brought about by various agents results in RNA fractionation in accordance with the tightness of the RNA-protein bonds. The cytoplasmic ribosomal and rapidly labelled non-ribosomal RNA species are separated into several fractions identified as 18S and 28S rRNA's, mRNA and messenger-like RNA. A relatively small fraction (about 10% of the total) of rRNA tenaciously bound to protein has been also revealed.
Mol Biol (Mosk)
PMID:[Study of ribonucleoprotein particles by the method of RNA chromatography on a column of nucleoprotein-celite]. 95 23

Polyribosomal messenger RNA from HeLa cells contain 3'-OH-terminal polyadenylate sequences approximately 133 nucleotides in length (weight average). When analyzed at the ribonucleoprotein level of organization these poly(A)-rich sequences are found to contain tightly bound proteins. These proteins remain associated with the poly(A)-rich RNA during affinity chromatography of RNase A and T1-digested polyribosomes on poly(U)-Sepharose in 0.5 M NaCl, and co-elute from the column with the RNA at 50% formamide. Controls establish that the co-purification of the proteins with poly(A) on poly(U)-Sepharose requires the molecular integrity of the poly(A). Polyacrylamide gel electrophoresis resolves the poly(A)-specific proteins into two components of 74,000 and 62,000 molecular weight. The larger protein is the same size as that previously reported to be associated with poly(A)-rich sequences in HeLa heterogeneous nuclear RNA (Kish, V.M., and Pederson, T. (1975), J. Mol. Biol. 95, 227-238). It is concluded that both HeLa nuclear and polyribosomal poly(A) sequences have a protein (62,000 molecular weight) associated with poly(A) appears to be confined only to messenger RNA.
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PMID:Poly (A)-rich ribonucleoprotein complexes from HeLa cell messenger RNA. 97 46


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