Differential phosphorylation of ribosomal acidic proteins from yeast cell by two endogenous protein kinases: casein kinase-2 and 60S kinase

• Autorzy: Szyszka R. , Boguszewska A. , Grankowski N. , Ballesta J.P.G.
• Języki publikacji: EN

Abstrakty

EN

The native 80S ribosomes isolated from Saccharomyces cerevisiae (strain W303) cells was phosphorylated by two endogenous protein kinases: multifunctional casein kinase-2 (CK-2) and specific 60S kinase. Three acidic proteins within the 60S ribosomal subunit: YP1(3, YPlp' and YP2a are phosphorylated by both kinases. The other two proteins: YPla and YP2(3 are predominantly phosphorylated by CK-2 but not by 60S kinase. This was confirmed in the experiment with the recombinant protein, YP2P, as a substrate, which is practically not phosphorylated by specific 60S kinase. These results together with the previous data based on the target amino-acid se­quences suggest that, in addition to the multifunctional casein kinase-2 and specific 60S kinase, there exist probably other protein kinase(s) which phosphorylate the ribosomal acidic proteins in the cell.

Słowa kluczowe

EN

phosphorylation; casein kinase II; yeast cell; ribosomal acidic protein; specific 60S kinase; Saccharomyces cerevisiae

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1995
• Tom: 42
• Numer: 3
• Opis fizyczny: p.357-362,fig.

Twórcy

autor

Szyszka R.

• Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland

autor

Boguszewska A.

autor

Grankowski N.

autor

Ballesta J.P.G.

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