Interaction, topography and function of ribosomal components

Bielka, H

doi:10.1007/978-3-642-68272-8_9

The Eukaryotic Ribosome 1982

DOI: 10.1007/978-3-642-68272-8_9

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Interaction, topography and function of ribosomal components

H Bielka¹

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Cited by 7 publications

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“…Progress has been slower with eukaryotic ribosomal subunits because of their complexity. Attempts to produce core particles which can reconstruct active subunits have mainly been based on the utilization of high salt concentrations (for reference see [2]). Recently 2,3-dimethylmaleic anhydride (DMMA), a reagent for protein which at pH 8.2 substitutes a negatively charged residue for each amino group and is easily removed at pH 6.0, has been used to dissociate proteins from yeast 60s ribosomal subunits reversibly [3,4].…”

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confidence: 99%

Partial reassembly of active 60S ribosomal subunits from rat liver following treatment with dimethylmaleic anhydride

Conquet

Lavergne

Paleologue

et al. 1987

European Journal of Biochemistry

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Rat liver 60s ribosomal subunits were treated with dimethylmaleic anhydride, a reagent for protein amino groups, at a 1/15000 mol/mol ratio. This caused the dissociation of specific proteins, which were separated from the 56s residual core particles by centrifugation and identified by two-dimensional gel electrophoresis. The core particles lacking 30% of the total proteins retained most of the initial activity measured by the puromycin reaction but only small percentages of activities measured by polyphenylalanine synthesis, elongation-factor-2(EF-2)-dependent GTP hydrolysis and EF-Zmediated GDP binding. Upon reconstitution, the complementary amount of split proteins was incorporated into ribosomal particles, which had almost the same catalytic activities and biophysical properties (density, sedimentation coefficient and capability to reassociate to 40s subunits) as the original subunits.

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mentioning

confidence: 99%

Partial reassembly of active 60S ribosomal subunits from rat liver following treatment with dimethylmaleic anhydride

Conquet

Lavergne

Paleologue

et al. 1987

European Journal of Biochemistry

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The acidic ribosomal proteins of different yeast species. Phosphorylation by ribosome‐associated protein kinases

Cytryńska

Wojda

Jakubowicz

1995

J. Basic Microbiol.

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Two major ribosomal proteins of Mr 13 kDa and 38 kDa were identified as phosphorylation substrates for ribosome-bound protein kinases from different yeast species. The phosphorylation level was much higher in ribosomes from the cells collected at the exponential growth phase, than in those from the stationary phase. Isoelectrofocusing of the protein band of 13 kDa and subsequent silver staining allowed to identify from four in the case of Pichia stipitis up to ten in Saccharomyces cerevisiae. Saccharomycodes Ludwigii, Torulopsis utilis and Kloeckera apiculata individual peptides. In the most of the yeast species studies five phosphorylated peptides were observed. However, only one or two such phosphopeptides were detected in Pichia stipitis and Trichosporon cutaneum ribosomes, respectively. The same phosphoprotein forms were identified in the in vivo 32P-labelling experiments.

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Phosphorylation of ribosomal proteins by ribosome‐associated protein kinases of Trichosporon cutaneum

Wojda

Cytryńska

Jakubowicz

1996

J. Basic Microbiol.

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Four ribosomal proteins of Mr 13 kDa, 15 kDa, 19 kDa and 38 kDa were identified as phosphorylation substrates for protein kinases tightly associated with Trichosporon cutaneum ribosomes. It was found that proteins of 13 kDa, 19 kDa and 38 kDa were phosphorylated by multifunctional casein kinase II while the protein of 15 kDa by casein kinase I. Proteins of 13 kDa and 38 kDa were detected in the large subunits while 15 kDa and 19 kDa in the small ribosomal subunits. By using isoelectrofocusing the protein of 13 kDa was resolved into two individual phosphorylated forms. The phosphorylation level of both forms was much higher in ribosomes from the cells collected at the exponential growth phase than in those from the stationary phase. The same phosphoprotein forms were identified in ribosomes from in vitro and in vivo [32P]-labelling experiments.

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Interaction, topography and function of ribosomal components

Cited by 7 publications

References 167 publications

Partial reassembly of active 60S ribosomal subunits from rat liver following treatment with dimethylmaleic anhydride

Partial reassembly of active 60S ribosomal subunits from rat liver following treatment with dimethylmaleic anhydride

The acidic ribosomal proteins of different yeast species. Phosphorylation by ribosome‐associated protein kinases

Phosphorylation of ribosomal proteins by ribosome‐associated protein kinases of Trichosporon cutaneum

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