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Adobe Flash Player and Adobe AIR. These features require the latest version of the Adobe Flash Player to work. Your safety and security are extremely important to us, please make sure you are running the latest version. Leggi Annunci PersonalizzatiNucleoside triphosphate pyrophosphatase from the amoeba Dictyostelium discoideum and Saccharomyces cerevisiae can be selectively repressed by the polyribosomal protein Sup45.
Nucleoside triphosphate pyrophosphatase (EC 18.104.22.168) activity is very low in the polyribosome fraction compared to the monosome fraction of Dictyostelium discoideum. The inhibition was observed whether the enzyme was purified by DEAE-cellulose chromatography or by ion-exchange chromatography on SP-Sepharose. When the preparation containing in addition 2.5 mg of ribosomes was fractionated by sucrose density-gradient centrifugation, the enzyme activities were found in the peak of large polyribosomes. Addition of purified Sup45 protein repressed the activities which were found at low ribosome concentrations. Measurements of low molecular weight nucleotides by ion exchange chromatography on octyl-agarose indicated the inhibition of ATP-ase at 50% at 0.3 mumol of Sup45 protein and at 0.07 mumol of Sup45 protein. These data suggest the role of Sup45 as a regulatory factor of nucleoside triphosphate pyrophosphatase. In the case of yeast cells, where the existence of a protein of 60 kDa which represses the expression of several genes (Sonenshein, J., et al., 1983, J. Biol. Chem. 258, 11525-11530) has been reported, it is possible that this protein is identical with Sup45.;
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