Halogenated benzimidazole inhibitors of phosphorylation, in vitro and in vivo, of the surface acidic proteins of the yeast ribosomal 60S subunit by endogenous protein kinases CK-II and PK60S

• Autorzy: Szyszka R. , Boguszewska A. , Shugar D. , Grankowski N.
• Języki publikacji: EN

Abstrakty

EN

Several halogeno benzimidazoles and 2-azabenzimidazoles, previously shown to be relatively selective inhibitors of protein kinases CK-I and/or CK-II from various sources, including CK-II from yeast [Szyszka et al. (1995) Biochem. Biophys. Res. Commun. 208, 418-4241 inhibit also the yeast ribosomal protein kinase PK60S. The most effective inhibitor of CK-II and PK60S was tetrabromo-2-azabenzimidazole (TetraBr-2-azaBz), which was competitive with respect to ATP (and GTP in the case of CK-II) with Ki values of 0.7 uM for CK-II, and 0.1 pM for PK60S. PK60S phosphorylates only three (YPlp, YP1(J', YP2a) out of five polypeptides of ppl3 kDa acidic proteins of 60S subunit phosphorylated by CK-II [Szyszka et al. (1995) Acta Biochim. Polon. 42, 357-3621. Accordingly, TetraBr-2-azaBz inhibits phosphorylation only of these polypeptides, catalysed by PK60S. Addition of TetraBr-2-azaBz to cultures of yeast cells, at concentrations which were without effect on cell growth, led to inhibition of intracellular phosphorylation of ribosomal acidic proteins, paralleling that observed in vitro. TetraBr-2-azaBz is shown to be a useful tool for studies on the intracellular regulation of phosphorylation of the ribosomal 60S acidic proteins, which are involved in formation of active ribosomes.

Słowa kluczowe

EN

yeast; acidic protein; phosphorylation; halogenated benzimidazole inhibitor; in vivo; in vitro; ribosomal acidic protein; protein kinase

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1996
• Tom: 43
• Numer: 2
• Opis fizyczny: p.389-396,fig.

Twórcy

autor

Szyszka R.

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

autor

Boguszewska A.

autor

Shugar D.

autor

Grankowski N.

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