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Query: UNIPROT:P06889 (Mol)
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Antibodies to the RNase-sensitive RNP and to the RNase-resistant Sm nuclear antigens were used to affinity purify these antigens from a saline extract of rabbit thymus acetone powder. Determination of the protein subunits recovered by either glycine-HCl, pH 2.8, or 2.5 M MgCl2 elution on gradient sodium dodecyl sulfate-polyacrylamide electrophoresis containing mercaptoethanol revealed that RNP was composed of five proteins with mol. wts from 10,000 to 15,000 whereas Sm contained the same or similar five chains plus six additional subunits with mol. wts from 21,000 to 42,000. RNase treatment of the thymus extract increased the recovery in Sm of the same bands compared to untreated extract. Thus, RNP and Sm appear to have different numbers of protein components and RNP may be a subset of Sm. Sucrose gradient centrifugation of the 125I-labeled, pH 2.8 eluted antigens gave peaks of 3 and 6S for RNP and Sm, respectively. Sucrose gradient centrifugation of the crude untreated thymus extract followed by quantitative single radial immunodiffusion analysis of each fraction produced a broad peak from 16S to the top of the gradient while pretreatment of the extract with RNase resulted in a discrete 6S peak. These results indicate that in rabbit thymus acetone powder native RNP and Sm exist as larger polydisperse complexes with additional material including RNA and that after acid elution or RNase treatment the antigens are found in a smaller monodisperse form.
Mol Immunol 1982 Jun
PMID:Characterization of RNP and Sm ribonucleoprotein nuclear antigens. 681 Jan 1

During or immediately after transcription of chromatin the high molecular weight pre-mRNA is complexes with proteins and low molecular weight RNA (lmwRNA). In the presence of a cytosolic RNase inhibitor pre-mRNA-protein complexes, designated as polyparticles, can be isolated from rat liver nuclei. The polyparticles are characterized by a maximum of their sedimentation coefficient of around 90 S, a protein to RNA ratio of 4.1, and a density in CsCl of 1.4 g/cm3. A set of 6--10 basic proteins of molecular weights between 30 and 45 kd as well as a multitude of polypeptides of higher molecular weights is associated with the rapidly labeled, polydisperse, high molecular weight RNA and several lmwRNA species. In order to study the structure of these very complex nuclear RNP complexes, the polyparticles were incubated at various concentrations of sodium chloride, urea or proteinases of different specificities (trypsin, chymotrypsin, proteinase K), recentrifuged through a sucrose layer and analyzed with respect to their sedimentation behavior, their protein to RNA ratios and their protein- and RNA components. Rhe results of these experiments led us to the proposal of a structural model which is presented here.
Mol Biol Rep 1981 May 22
PMID:The structure of ribonucleoprotein particles from rat liver nuclei. 701 68

A method of electrophoresis of nuclear 30S particles is described. In contrast to the earlier methods based on the fixation of RNP particles with formaldehyde and bifunctional agents with subsequent treatment with sodium dodecylsulphate, the new method treats intact particles in the presence of 1% triton X-100. One of the advantages of the proposed method is the possibility of using the polyacrylamid gel electrophoresis with high resolution capacity in addition to agarose gel electrophoresis. The developed method gives a possibility to estimate the homogeneity and nativity of RNP particles without additional separation by sucrose gradient or purification in nuclear extracts. There is a correlation between the distribution of the particles in the sucrose gradient and the picture of the mobility of these particles in agarose gel.
Mol Biol (Mosk)
PMID:[Homogeneity of the 30S fraction of nuclear ribonucleoprotein particles. Electrophoresis of intact particles]. 707 Mar 73

The CD spectra of Influenza virus RNA and RNP were examined in the ultraviolet region (220--320 nm) at different temperatures, NaCl and urea concentrations. The magnitude of the positive band for RNP decreases gradually upon increasing the temperature, indicating that rather weak interaction between RNA and protein occurs. However the temperature drastically affects the intensity of the negative band about 222 nm. In the temperature range where the protein melts the positive band at longer wavelengths shows a temperature dependence that is similar for RNP and free RNA. Addition of NaCl results in an increase in intensity and blue shift of the positive CD band of RNP. In the presence of 1 M NaCl the CD spectrum of RNP is very close to that of protein-free RNA. Urea concentrations up to 10 M has little effect on the CD spectrum of RNP. These results suggest that only ionic but not hydrophobic and hydrogen bondings are involved in the RNA-protein interaction in Influenza virus RNP.
Mol Biol (Mosk)
PMID:[Circular dichroism spectra study on the ribonucleoprotein structure of influenza virus]. 707 Mar 80

Transcription of ribosomal genes of a loach Misgurnus fossilis L. was studied by electron microscopy. Relative transcriptional activity in nucleoli at different vitellogenic stages was determined by direct calculation of the number of operating ribosomal genes in the nucleoli. Morphologic studies showed that the transcribing regions of mean length 2.3 +/- 0.2 mkm are separated by spacers of variable lengths. Both short (1.2--1.4 micrometer) and long (2.4--2.6 micrometer) spacers were visualised. The lateral RNP fibrils have granular structure, each granule containing 300--350 RNA bases. It was found that chromatin has nucleosomal structure in spacer regions and is of non-beaded, smooth structure in transcribing regions. The data obtained allow to suggest that in transcribing regions chromatin undergoes structural transition before the transcription process.
Mol Biol (Mosk)
PMID:[Electron microscopic study of transcription of loach oocyte ribosomal genes]. 724 38

Comparisons of relative lengths of lampbrush loops, nascent RNP transcripts and hnRNA molecules from oocytes of amphibia with different C-values show that there is an increasing trend in loop, and transcriptional unit, length with increase in genome size but no increasing trend with respect to RNA contour length. The formation of duplex regions and circles in RNP fibrils indicates that RNA processing may occur within the nascent fibrils. The hnRNA molecules from oocytes of the various amphibia readily form intermolecular duplex structures. These complementary sequences have a low kinetic complexity and are transcribed from highly repetitive sequences distributed throughout the genome. Their possible function is considered.
Mol Biol Rep 1981 May 22
PMID:Structural organization of nascent transcripts and hnRNA molecules in amphibian oocytes. 725 7

The proteins of 30S RNP particles containing pre-mRNA (hnRNA) were cross-linked with bifunctional reagents (dimethylsuberimidate and dimethyl-3,3'dithiobispropionimi-date). Further treatment with 1 or 2 M NaCl dissociates all RNA from protein. However, a significant part of protein particles--informofers, being cross-linked survived high salt treatment. Their sedimentation coefficients were close to those of original particles. No RNA could be detected in the informofers even after labeling the cells with a precursor for a long period of time. Sodium dodecylsulfate or urea dissociated cross-linked informofers into oligomeric polypeptides. They could be dissociated by beta-mercaptoethanol treatment if a reversible cross-linking reagent has been used. The resulting polypeptides were represented by informatin. RNP particles (30S RNP or polyparticles) were reconstituted upon mixing or cross-linked informofers with pre-mRNA and removal of 2 M NaCl. The reconstituted particles were indistinguishable from the original ones by several tests.
Mol Biol (Mosk)
PMID:[Nuclear RNP containing pre-mRNA. 16. Cross-linked informofers]. 733 70

The major cold-shock protein of Bacillus subtilis, CspB, is a member of a protein family widespread among prokaryotes and eukaryotes that share the highly conserved cold-shock domain (CSD). The CSD domain is involved in transcriptional and translational regulation and was shown to bind the Y-box motif, a cis-element that contains the core sequence ATTGG, with high affinity. The three-dimensional structure of CspB, a prototype of this protein family, revealed that this hydrophilic CSD domain creates a surface rich in aromatic and basic amino acids that may act as the nucleic acid-binding site. We have analysed the potential role of conserved aromatic and basic residues in nucleic acid binding by site-directed mutagenesis. In gel retardation and ultraviolet cross-linking experiments, the ability of CspB mutants to bind single-stranded oligonucleotides (ssDNA) that contain the Y-box motif was investigated. Single substitutions of three highly conserved phenylalanine residues (Phe-15, Phe-17, Phe-27) by alanine and substitution of one histidine (His-29) by glutamine, all located within the putative RNA-binding sites RNP-1 and RNP-2, abolished the nucleic acid-binding activity of CspB. Conservative substitutions of Phe-15 to tyrosine (F15Y) showed a small increase in binding affinity, whereas separate replacement of Phe-17 and Phe-27 by tyrosine caused a reduction in binding activity. These and other substitutions including the conserved basic residues Lys-7, Lys-13 and Arg-56 as well as the aromatic residues Trp-8 and Phe-30 strongly suggest that CspB uses the side-chains of these amino acids for specific interaction with nucleic acids. Ultraviolet cross-linking experiments for CspB mutants with ssDNA supported the idea of specific CspB/nucleic acid interaction and indicated an essential role for the aromatic and basic residues in this binding. In addition, two-dimensional nuclear magnetic resonance studies with F17A, K13Q, F15Y and F27Y revealed that the mutants have the same overall structure as the wild-type CspB protein.
Mol Microbiol 1995 May
PMID:Mutational analysis of the putative nucleic acid-binding surface of the cold-shock domain, CspB, revealed an essential role of aromatic and basic residues in binding of single-stranded DNA containing the Y-box motif. 747 64

Here we show that small RNAs homologous to short interspersed repetitive DNA sequences: ID, B1, B2--in rat cells and Alu in human cells are complexed with specific proteins to form small nuclear and cytoplasmic RNP particles (alpha RNP) with common properties. alpha-RNP differ from other ribonucleoproteins by composition and properties. alpha RNA molecules are apparently transcribed by RNA polymerase III. alpha-RNAs are capable of stable antisense hybridization with specific messenger RNAs. Expression of alpha-RNA is specifically regulated by gene regulatory factors. The data obtained support the suggestion that alpha-RNA may belong to the group of regulatory eukaryotic RNAs and that alpha-RNP might be involved in the coordinative control of the expression of the sets of genes with SINE-homologous sequences in regulatory regions.
Mol Biol (Mosk)
PMID:[A new class of RNP particles containing small RNA homologous to short dispersed DNA repetitive sequences]. 747 43

RNase P in both prokaryotes and eukaryotes is a ribonucleoprotein that cleaves tRNA precursors to generate the 5' termini of the mature tRNAs. Many patients with autoimmune diseases produce antibodies against a 40 kDa protein (designated To or Th antigen) which is an integral component of eukaryotic RNaseP as well as nucleolar 7-2 RNP which is identical to the mitochondrial RNA processing (MRP) RNP. Interestingly, the To antigen found in human cells and the C5 protein, the only protein component of E. coli RNaseP, are antigenically related. In this study, we show that a 56 nucleotide-long sequence, corresponding to nucleotides 20-75 near the 5' end of human RNaseP RNA, is sufficient to bind the To antigen. We previously showed that the human To antigen binds to a short distinct structural domain near the 5' end of human 7-2/MRP RNA. There is no obvious primary sequence homology between the To antigen binding sites in RNaseP RNA and 7-2/MRP RNA; however, these sequences are capable of assuming a similar secondary structure which corresponds to the recently proposed 'cage' structure for RNaseP RNAs and 7-2/MRP RNA (Forster and Altman (1989) Cell 62: 407-409). These data are supportive of the idea that these two RNAs may have evolved from a common progenitor molecule.
Mol Cell Biochem 1994 Jan 12
PMID:Human RNaseP RNA and nucleolar 7-2 RNA share conserved 'To' antigen-binding domains. 751 16


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