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)

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

A single, major 21 S messenger ribonucleoprotein (mRNP complex) was isolated and purified by sucrose gradient centrifugation after EDTA treatment of high salt washed polysomes from 15 day embryonic chick lenses. A 17 S mRNA was released from the 21 S subunit of delta crystallin. Similar results were obtained with the 17 S mRNA released from the 21 S mRNP complex.
Mol Biol Rep 1976 Sep
PMID:Synthesis of delta crystallin from embryonic chick lens messenger ribonucleoprotein complex. 103 4

Proteins present in messenger ribonucleoprotein particles were labeled with [35S]-methionine in Ehrlich ascites tumor cells in which synthesis of new ribosomes was inhibited. Poly(A)-protein complexes were isolated from free and membrane-bound polyribosomes by sucrose gradient centrifugation and affinity chromatography on oligo(dT)-cellulose. Both classes of Poly(A)-protein particles contain a poly(A) chain of about 70 adenyl residues and a protein with a molecular weight of 76000 attached to it.
Mol Biol Rep 1976 Sep
PMID:Characterization of poly(A)-protein complexes isolated from free and membrane-bound polyribosomes of Ehrlich ascites tumor cells. 103 5

The accessibility of single-stranded sequences in 16S RNA in free state and in ribonucleoprotein particles (RNP) to complementary binding with isoplith fractions of oligonucleotides was studied. RNP had different protein composition and corresponded to intermediate stages of E. coli 30S subunit assembly in vitro. Gel-filtration was used to detect the most strong binding. It was found that S4 essentially inhibited the hexamer binding to RNA. 'Core' proteins bound to 16S RNA strongly increased the shielding of single-stranded regions while 'split' proteins insignificantly changed the hexamer binding. Nevertheless evidence is presented that 'split' proteins might also interact directly with 16S RNA in the 30S subunit.
Mol Biol Rep 1975 Jul
PMID:Complementary binding of oligonucleotides with 16S RNA and ribosomal ribonucleoproteins. 109 38

When Escherichia coli 50-S ribosomal subunits are treated with increasing concentrations of urea partial deproteination occurs. Furthermore, we observed that the number of sulfhydryl groups which react with Ellman's reagent is a sigmoidal function of the urea concentration. These results are similar to those previously reported for the 30-S subunit (Acharya, A.S. and Moore, P.B. (1973) J. Mol. Biol. 76, 207-221). For both subunits we identify the proteins which dissociate (split proteins) or are recoverable in a ribonucleoprotein particle (core proteins) under the action of 6 M urea in a buffer of moderate ionic strength.
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PMID:Characterization of the particles produced by exposure of ribosomal subunits to urea. 110 83

A ribonucleoprotein was released from carefully purified rat liver mitochondrial polyribosomes after dissociation with 1 M potassium chloridepuromycin. This ribonucleoprotein was characterized by a sedimentation coefficient ranging from 10-14 S and buoyant density of 1.48 g cm(-3) in cesium chloride equilibrium centrifugation differing in these parameters from the subunits of mitochondrial ribosomes. Poly(A)-containing RNA constituted more than 30% of the total RNA content in this non-ribosomal ribonucleoprotein.
Mol Biol Rep 1975 Jul
PMID:Messenger RNA-containing ribonucleoprotein from mitochondrial polyribosomes of rat liver. 116 Aug 79

Nuclear ribonucleoprotein particles were isolated from chick erythroblast nuclei. The particles were found to sediment as heterogeneous material. The major fraction of the rapidly synthesized RNP sedimented at 30 S, whereas the nuclei were found to contain a major, apparently more stable, RNP component sedimenting at about 40 S. The RNA isolated from the RNP particles was assayed for globin messenger activity in a wheat germ cell-free system. RNP sedimenting at relatively low S values (approx. 15 S) as well as RNP-particles of larger size code for globin. In addition to globin, the RNA of the particles codes also for other, not yet identified, proteins.
Mol Biol Rep 1975 Oct
PMID:Globin messenger sequences in nuclear ribonucleoprotein particles of avian erythroblasts. 119 11

The formation of polyribosomes in mouse liver cells at the reduced-rate translation was studied by treatment with cycloheximide (CHI) and aurintricarboxylic (ATA) acid. An increase of polypeptide synthesis time by 1.7-2.7 times (0.5 mg CHI per 25 g of weight or 15 mg ATA per 25 g) leads to a delay of the entrance of newly formed cytoplasmic D-RNA into polyribosomes. These results are in agreement with the model of polyribosome formation from ribonucleoprotein precursors containing cytoplasmic D-RNA. On the other hand, in the presence of a CHI dose (5 mg/25 g) causing a dramatic (240-fold) increase of polypeptide synthesis time, the kinetics of entrance of newly formed D-RNA into polyribosomes does not differ from the normal one, and amount of the incorporated mRNA is even somewhat higher than under normal conditions. It is suggested that in this situation ribosomes are moving along the newly formed mRNA, and their movement is not accompanied by the synthesis of completed polypeptide chain.
Mol Biol (Mosk)
PMID:[The interaction between newly-formed mRNA and ribosomal particles during retarded translation]. 122 68

The rapidly labelled postribosomal ribonucleoprotein (RNP) found in the cytoplasm of mouse plasmacytoma cells were investigated. It has been shown that 45S and 80S particles contain relatively high molecular weight (approximately 12-17S) pulse-labelled RNA similar to the polyribosomal mRNA. No other postribosomal RNP was found which would contain an RNA with similar sedimentation characteristics. In CsC1 density gradients, the postribosomal RNP gives two peaks. One of them, the rapidly labelled component (rho 1.52 g/cm3) is found only in 45S RNP. The other rapidly labelled component (rho 1.36-1.41 g/cm3) is revealed in all investigated regions of sucrose gradients. The latter contains relatively low molecular weight RNA (approximately7-9S). These RNP are supposed to be informosome-like particles. The components with a buoyant density of 1.52 g/cm3 may represent an mRNP-45S subparticles complex. The rapidly labelled mRNA of 80S particles is released after EDTA treatment in the form of mRNP with a buoyant density of 1.45-1.47 g/cm3.
Mol Biol (Mosk)
PMID:[Ribonucleoproteins containing mRNA in the cytoplasm of mouse plasmacytoma cells]. 122 72

Nuclear ribonucleoprotein particles were examined by electron microscopy after negative staining. The results confirmed the polymeric nature of the particles. The constitutive units were distributed into 4 size classes (diameters varying from 100 to 300 A, approximately) indicating that the monoparticle population was heterogenous. When examined on ultrathin sections, the particles had a fibrillar appearance.
Mol Biol Rep 1976 Apr
PMID:Size heterogeneity of the structural units of brain nuclear ribonucleoprotein particles. 127 63


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