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

Quantitative characteristics of nucleolus-organizing regions of chromosomes (NORs, or fibrillar centers, FCs) and some other nucleolar components have been studied with the aid of complete series of ultrathin sections of PK-cells. It has been found that: 1) the number of FCs per cell in the G0-period, in the G2-period and at metaphase is equal to 7.0, 33.7 and 8.0, respectively; 2) volumes of individual FCs in the G0-period (0.033 micron 3), G2-period (0.014 micron 3) and at metaphase (0.025 micron 3) are different; 3) the total volume of FCs, calculated for a haploid set of chromosomes, do not differ in the G0 (0.105 micron 3) and G2 (0.107 micron 3) periods, but exceed twice the FCs volume at metaphase (0.04-0.05 micron 3). These data show that the activation and inactivation of ribosomal genes in interphase PK-cells are not accompanied by a change in the total volumes of FCs and are probably connected with the "fragmentation" and fusion of FCs. Complete inactivation of ribosomal genes at mitosis leads to a decrease in the total volumes of FCs; 4) the nucleolus volume is proportional to the volume of the dense fibrillar RNP-component; in the G2-period the nucleolus volume also correlates with the number of FCs (r = 0.99); 5) the volume of the dense fibrillar component within individual fibrillar complexes--the structures corresponding to one nucleolus-organizing region--is not constant. This is an indirect evidence for the differences in the functional activity of NORs of different chromosomes.
Mol Biol (Mosk)
PMID:[Morphometric study of nucleolus-organizing regions of chromosomes from swine embryo kidney cells during Go-, G2-period and mitosis]. 318 28

The organization of select proteins within ribonucleoprotein particles containing heterogeneous nuclear and uridine-rich small nuclear RNAs (hnRNP and UsnRNP respectively) was examined by chemical cross-linking and ribonuclease digestion using diagonal two dimensional PAGE and immunoblotting detection systems. Monoclonal antibodies specific for A2, C1 and C2 hnRNP proteins, detected these proteins at gel coordinates which suggested homotypic dimers and trimers of A2 and homotypic trimers, hexamers and larger multimers of C1 and C2. Ribonuclease digestion did not alter the cross-linking properties of hnRNP C1 and C2 proteins but did result in loss of A2 homotypic dimers and trimers. Blots simultaneously reacted with hnRNP specific monoclonal antibodies and autoimmune patient serum (RNP/Sm), or monoclonal antibodies reactive with the U1 snRNP specific 63 kDa protein and/or the UsnRNP common proteins B', B and D revealed no complexes which would indicate interactions between hnRNPs and UsnRNPs. The U1 UsnRNP specific 63 kDa protein appeared not to be cross-linked to UsnRNP common B', B and D proteins. The data also suggested that UsnRNP common protein D was cross-linkable to UsnRNP common proteins D', E and G but not to B' and B. The cross-linking properties of D were unaffected by ribonuclease digestion. In contrast, ribonuclease digestion resulted in an inability to cross-link select complexes containing either B' and B, or p63. The data suggest that both hnRNPs and UsnRNPs are comprised of RNA-dependent and RNA-independent protein-protein interactions.
Mol Cell Biochem 1988 Nov
PMID:Reversible chemical cross-linking and ribonuclease digestion analysis of the organization of proteins in ribonucleoprotein particles. 323 Dec 14

A study of the distribution in heterogeneous nuclear RNP (hnRNP) of the different forms of the first intervening sequence (IVSI) from the E3 transcription unit of adenovirus serotype 2 suggests a three-step pathway for IVS excision and degradation. First, the lariat IVS is formed in a large RNP of the size of premessenger RNP where it is resistant to nuclease attack. Second, the lariat IVS is released from this large structure as a small RNP where it is very susceptible to enzymic degradation. Third, the lariat IVS is linearized after the release of the small RNP. Our studies suggest that only the intact lariat and linear IVS are involved in the excision-degradation pathway in vivo, whereas the lariat nicked in its circular part and the IVS trimmed at its 3' end are not pre-existing but generated during isolation of hnRNA or hnRNP.
J Mol Biol 1987 Oct 20
PMID:In-vivo degradation pathway of an excised intervening sequence. 343 Jun

Changes of RNP and Sm antigenic reactivities of a nuclear extract after enzymatic treatments were studied and quantified by the ELISA test. After RNase treatment of the nuclear extract, about a 300% increase of the Sm antigenic reactivity and more than a 95% decrease of RNP antigenic reactivity was found. Data from RNP-depleted nuclear extracts and column fractionation show that the increase in Sm antigenic reactivity after RNase treatment mainly comes from the RNP-Sm complex.
Mol Immunol 1987 Jun
PMID:Effect of enzymatic treatments on RNP and Sm antigenic reactivities--I. Loss of RNP but increase of Sm antigenic reactivity after RNase treatment of nuclear extract. 349 83

Chicken erythroid nuclei were prepared using four published methods. Our findings indicate that nuclei prepared by nitrogen cavitation are less likely to be contaminated with plasma membrane fragments than those made by procedures involving cell disruption by hypotonic lysis. However, globin gene sequences were much less sensitive to DNase I digestion in nuclei prepared by nitrogen cavitation. This suggests that the conformation of chromatin was altered by the cavitation procedure. Analysis of the proteins solubilized during limited DNase I digestion of nuclei prepared by both hypotonic lysis and cavitation revealed no appreciable differences in HMG proteins but a notable difference in the RNP-associated proteins and core histones.
Mol Cell Biochem 1987 Mar
PMID:Comparison of chicken erythroid cell nuclear isolation methods using morphological, immunochemical and biochemical criteria. 358 29

The buoyant density in the CsCl gradient of the small nuclear RNP tightly bound to chromatin has been studied. It was shown that the buoyant density of alpha-RNP is characteristic for ribonucleoproteins (p = 1.36-1.50 g/cm3). The alpha-particles are of extraordinary stability. These RNP were shown to remain stable under drastic conditions (high ionic strength, SDS, 6 M urea) and resist unfixed caesium chloride density centrifugation. The alpha-RNA hybridizes with total rat liver DNA at C0t1/2 = 10(3). The oligonucleotide analysis of the alpha-RNA shows that the alpha-RNA is heterogeneous.
Mol Biol (Mosk)
PMID:[The small RNP acceptor of glucocorticoids bound to chromatin in liver cell nuclei]. 368 79

We studied the ultrastructure of lymphocyte nucleoli from rat peripheral blood within the first 6 hrs of their cultivation in the presence of phytohaemagglutinin (PHA). In the mixed population of intact lymphocytes there were observed several types of nucleoli, the localization and the ratio of individual nucleolar components being different. This seems to reflect functional peculiarities of these nucleoli. Some nucleoli are characteristic of the presence of several sites of intranucleolar condensed chromatin. However, all these nucleoli could be related to the so-called ring-shaped nucleoli with a fibrillar center surrounded by fibrillar and granular RNP-components, which points out to their low synthetic activity. The major changes in the nucleoli of stimulated lymphocytes were observed after the action of PHA within 1 hr. These changes were expressed in the elevation of electron density of the fibrillar centre and the loss by it of clear borders and correct shape, in the appearance of large zones of the dense fibrillar component with acquired an increased electron density, and also in the disappearance of condensed chromatin sites. By that time, there was revealed a peculiar shape of nucleoli with a "fragmented" fibrillar centre and the presence of vacuoles and strands consisting of fibrillar and granular RNP-components. The different types of changed nucleoli in the population of stimulated lymphocytes seem to be the consequence of a gradual transition of ring-shaped nucleoli to active nucleolonema-like ones. So, it is obvious that changes in the ultrastructure of nucleoli occur already by 1 hr after the PHA action. This points out to the intensification of pre-rRNA transcription that takes place by that time.
Mol Biol (Mosk)
PMID:[Changes in the ultrastructure of inactive circular nucleoli from mature rat lymphocytes at early stages of blast transformation]. 370 72

The nature of the association of U1 RNA with rapidly sedimenting RNP structures in rat hepatoma nuclei was investigated. The effects of salt and proteinase K treatment on the stability of this 'bound' form of U1 RNA were studied using sucrose density gradient analyses. Quantitation of the amount of U1 RNA remaining associated with large structures after treatment was used to assess the relative contribution of protein-protein (and protein-RNA) versus RNA-RNA interactions. Forty-eight percent of the total nuclear U1 RNA released by sonication was found in a 'bound' form when the sonicate was centrifuged through gradients containing 50 mM NaCl. Fifty percent of this 'bound' U1 RNA remained associated with rapidly sedimenting RNPs when the NaCl concentration was raised to 500 mM. To assess the contribution of protein independent interactions, large RNPs were completely deproteinized and their RNA moieties were then recentrifuged on gradients. By this analysis, 27% of the U1 RNA originally 'bound' to hnRNPs was associated with rapidly sedimenting (greater than 30 S) RNA (at 50 mM NaCl) suggesting their association by RNA-RNA hydrogen bonds. When the concentration of NaCl was 500 mM, 31% of the U1 RNA was associated with large RNA. Hence, approximately 30% of the U1 RNA molecules originally 'bound' (or about 15% of the total nuclear U1 RNA) were found to be associated by RNA-RNA hydrogen bonds while the remainder of the binding of U1 RNP to hnRNP was by protein-protein and/or protein-RNA interactions.
Mol Cell Biochem 1984 Nov
PMID:Interactions of U1 RNP with heterogeneous nuclear RNA in rat Novikoff hepatoma nuclei. 608 66

Small cytoplasmic poly(A) + RNA homologous to a highly repeated sequence B2 of the mouse genome (scB2 RNA) was not found as free RNA within a cell. This RNA is bound to small (12-18S) ribonucleoprotein particles as well as to heavy RNP particles, apparently informosomes. After deproteinization of the heavy RNP the major part of scB2 RNA molecules cosedimented with heavy RNAs. It seems that scB2 RNA is associated with mRNA in informosomes via short complementary regions. About half of the scB2 RNA molecules was revealed in the cytoskeleton fraction. The possibility that scB2 RNAs are involved in mRNA transport or in the regulation of mRNA translation is discussed.
Mol Biol (Mosk)
PMID:[Small cytoplasmic poly(A)+RNA, homologous to the B2 repetitive sequence of the mouse genome, is present in ribonucleoproteins]. 608 69

The activity of antisera against ribonucleoproteins containing U1 small nuclear RNA (Sm and RNP) has been analysed on pol II transcripts in an in vivo system. Xenopus laevis ribosomal protein gene transcripts are accumulated in the form of precursor RNA when either of the two kinds of antisera are injected into the germinal vesicles of X. laevis oocytes before the injection of purified L1 and L14 ribosomal protein genes. No effect on the accumulation of mature histone mRNA is detected when X. laevis histone genes are injected together with the RNP antiserum. These results strongly suggest that U1-RNP complexes play an essential role in intron removal in vivo.
J Mol Biol 1984 Dec 25
PMID:Splicing of Xenopus laevis ribosomal protein RNAs is inhibited in vivo by antisera to ribonucleoproteins containing U1 small nuclear RNA. 608 21


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