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)

Proteins of yeast cytoplasmic ribosomes were analyzed by two different methods of two dimensional gel electrophoresis: run at pH 8.6 in 1-D1 and at pH 4.6 in 2-D (Method A); run at pH 5.0 in 1-D and in the presence of sodium dodecyl sulfate in 2-D (Method B). The numbers of proteins estimated were 28 (Method A) and 29 or 30 (Method B) in the 40S small subunit, and 40 (Method A) and 41 (Method B) in the 60S large subunit, respectively. Molecular weights of proteins in the small and the large subunits were found to be less than 40,000 and 60,000 respectively.
Mol Gen Genet 1976 Apr 23
PMID:Study on proteins from yeast cytoplasmic ribosomes by two-dimensional gel electrophoresis. 0 66

Electrophoresis of ribosomal proteins according to Kaltschmidt and Wittmann, 1970a, b (pH 8.6/pH 4.5 urea system) yielded 29 proteins for the small subunits and 35 and 37 proteins for the large subunits of Krebs II ascites and HeLa ribosomes, respectively. Analysis of the proteins according to a modified technique by Mets and Bogorad (1974) (pH 4.5/pH 8.6 SDS system) revealed 28 and 29 proteins in the small subunits and 37 and 38 proteins in the large subunits of Krebs II ascites and HeLa ribosomes. The molecular weights of the individual proteins were determined by: 1. "three-dimensional" gel electrophoresis; 2. two-dimensional gel electrophoresis at pH 4.K/pH 8.6 in SDS. The molecular weights for 40S proteins ranged from 10,000 to 39,000 dalton (number average molecular weight: 21,000). The molecular weights for the 60S proteins ranged from 14,000 to 44,000 dalton (number average molecular weight: 23,000) using the "three-dimensional" technique. A molecular weight range from 10,000 to 38,000 dalton (number average molecular weight: 21,000) was obtained for the 40S subunits, whereas the molecular weights for the 60S ribosomal proteins (average molecular weight: 26,000) ranged from 12,000 to 69,000 dalton using the pH 4.5/pH 8.6 SDS system. The molecular weights Krebs II ascites and HeLa ribosomal proteins are compared with those obtained by other authors for different mammalian species.
Mol Gen Genet 1978 Apr 17
PMID:Characterisation of ribosomal proteins from HeLa and Krebs II mouse ascites tumor cells by different two-dimensional polyacrylamide gel electrophoresis techniques. 2 16

Antibodies were prepared in rabbits and sheep to rat liver ribosomes, ribosomal subunits, and to mixtures of proteins from the particles. The antisera were characterized by quantitative immunoprecipitation, by passive hemagglutination, by immunodiffusion on Ouchterlony plates, and by immunoelectrophoresis. While all the antisera contained antibodies specific for ribosomal proteins, none had precipitating antibodies against ribosomal RNA. Rat liver ribosomal proteins were more immunogenic in sheep than rabbits, and the large ribosomal subunit and its proteins were more immunogenic than those of the 40S subparticle. Antisera specific for one or the other ribosomal subunit could be prepared; thus it is unlikely that there are antigenic determinants common to the proteins of the two subunits. When ribosomes, ribosomal subunits, or mixtures of proteins were used as antigens the sera contained antibodies directed against a large number of the ribosomal proteins.
Mol Gen Genet 1978 Oct 30
PMID:Immunochemical analysis of the structure of eukaryotic ribosomes: antigenic properties of rat liver ribosomes and ribosomal proteins and characterization of the antisera. 8 54

The rat liver 5S RNA when denaturated by urea or EDTA, or even without any special treatment, undergoes conformational changes leading to the formation of three electrophoretically distinct isomeres of the molecules with relative mobilities 0.39, 0.44 and 0.47. The band with the slowest mobility corresponds apparently to the native 5S RNA since it is specific for both freshy isolated and renaturated 5S RNA. Moreover, it was found that denaturation of the immobilized 5 S RNA decreases significantly its ability to form a complex with the rat liver 60S ribosomal subunit proteins L6, L7, L8, L18 and L35.
Mol Biol (Mosk)
PMID:[Conformational isomers of rat liver 5S ribosomal RNA]. 9 31

When supplemented with Escherichia coli stringent factor, 80S ribosomes from various sources failed to support guanosine tetra- and pentaphosphate ((p)ppGpp) synthesis. In contrast, ribosomal proteins from 80S, 60S or 40S particles (mouse embryos, rabbit reticulocytes) crossreacted with the E. coli stringent factor. Significant stimulation of (p)ppGpp synthesis was achieved with a concentration as low as 5 micrograms of ribosomal proteins/ml. These observations may provide additional crtieria to detect homologies between eukaryotic and prokaryotic ribosomal proteins.
Mol Gen Genet 1978 Nov 09
PMID:Eukaryotic ribosomal proteins stimulate Escherichia coli stringent factor to synthesize guanosine 5'-diphosphate, 3'-diphosphate (ppGpp) and guanosine 5'-triphosphate, 3'-diphosphate (ppGpp). 21 1

Separation of the proteins from rat liver 40S and 60S ribosomal subunits and polysomes was done in four different two-dimensional polyacrylamide gel electrophoresis systems. The first dimension was run at acidic or basic pH, the second dimension either with sodium dodecyl sulphate or at acidic pH in 18% acrylamide. The position of each individual protein of both subunits and polysomes was determined in each system. This identification resulted from a new method avoiding any pervious purification of individual proteins. The new "proposed uniform nomenclature for mammalian ribosomal proteins" (McConkey et al. in press) was used for numbering the proteins in the four systems.
Mol Gen Genet 1979 Mar 20
PMID:Spot position of rat liver ribosomal proteins by four different two-dimensional electrophoreses in polyacrylamide gel. 28 54

Ribosomal proteins of the dimorphic fungus Mucor racemosus were isolated and characterized by 2-dimensional gel electrophoresis. Proteins from ribosomes of the yeast and mycelial phase were compared, and were found to be qualitatively indistinguishable. The only consistent difference in the patterns of proteins was in a protein of the 40S subunit, S-6. This protein was phosphorylated in yeast and hyphae forms, but not in asexual sporangiospores. Studies on protein S-6 showed that it contained 3 phosphate residues per molecule of protein when maximally phosphorylated. In this form 3 different tryptic peptides were shown to contain a single phosphoserine. The S-6 protein also existed in forms containing 1 or 2 phosphates per molecule, depending on growth conditions.
Mol Gen Genet 1979 Aug
PMID:Ribosomal proteins of the dimorphic fungus, Mucor racemosus. 29 24

Ribosomal proteins S1, S2, S16 and S23 were localized on the surface of the small subunit (40S) of rat liver ribosomes by immune electron microscopy. Antibodies against the single proteins were raised in rabbits and chicken and purified by affinity chromatography. 40S-IgG-40S complexes were obtained by incubation of 40S subunits with non-cross-reacting antibodies specific for each of the four proteins and subsequent sucrose density gradient centrifugation. The location of the proteins was determined by means of antibody binding sites visualized in negative contrast in the electron microscope. The four investigated proteins are mainly located in the head region of the small subunit. Exposed antigenic determinants of proteins S1 and S2 were found to be located at different sites of the small subunit whereas proteins S16 and S23 were mapped in a limited region only.
Mol Gen Genet 1979 Oct 03
PMID:Localization of proteins S1, S2, S16 and S23 on the surface of small subunits of rat liver ribosomes by immune electron microscopy. 29 97

Protein synthesis by ribosomes from several cryptopleurine-resistant yeast mutants is also resistant to emetine and tubulosine. These mutants can be classified into two different types: Class I mutants which display high levels of resistance to emetine and tubulosine and Class II mutants that are only weakly resistant to tubulosine and are slightly more sensitive to emetine than those of Class I. Apparently all mutants have similar levels of resistance to cryptopleurine. The distinct phenotypes of Class I and Class II strains are expressed through their 40S ribosomal subunit. Genetic analysis has shown that the mutations to cryptopleuring resistance are allelic and that in a particular case (strain CRY6) the pleiotropic phenotype is a result of the expression of the cry1 locus. It is suggested that Class I and Class II mutants arise from two independent mutational events within The cry1 allel. In heterozygous (+/cry1) diploids both the sensitive and the resistant genes are expressed as shown by studies of the action of cryptopleurine on polyphenylalanine-synthesizing systems derived from each parental sensitive and resistant haploid strain and heterozygous diploid strains. The apparent dominance of sensitivity over resistance which may be observed in vivo in heterozygous (+/cry1) diploids has been explained in terms of the mode of action of the inhibitors.
Mol Gen Genet 1977 Nov 18
PMID:Genetics and biochemistry of cryptopleurine resistance in the yeast Saccharomyces cerevisiae. 34 Sep 10

We have measured the synthesis and stability of ribosomal proteins in a temperature sensitive strain of yeast which at the restrictive temperature is specifically blocked in the processing of 27S ribosomal precursor RNA. We find that in the absence of 60S ribosomal subunit assembly, the synthesis of all the ribosomal proteins studied continued. However, the proteins of the 60S subunit fail to accumulate and are rapidly degraded.
Mol Gen Genet 1977 Dec 09
PMID:Synthesis and turnover of ribosomal proteins in the absence of 60S subunit assembly in Saccharomyces cerevisiae. 34 Sep 29


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