Protein kinases CKI and CKII are implicated in modification of ribosomal proteins of the yeast Trichosporon cutaneum

• Autorzy: Wojda I. , Cytrynska M. , Frajnt M. , Jakubowicz T.
• Języki publikacji: EN

Abstrakty

EN

Phosphorylation of acidic ribosomal proteins P1/P2-P0 is a common phenomenon in eukaryotic organisms. It was found previously that in Trichosporon cutaneum, un­like in other yeast species, in addition to the two acidic ribosomal proteins, two other proteins of 15 kDa and 19 kDa of the small ribosomal subunit were phosphorylated. Here we describe two protein kinases: CKI and CKII, which are engaged in the modifi­cation of T. cutaneum ribosomal proteins. The acidic ribosomal proteins and the pro­tein of 19 kDa were modified by CKII associated with ribosomes, while the protein of 15 kDa was modified by CKI. Protein kinase CKI was purified from cell-free extract (CKIC) and from ribosomal fraction (CKIR). The molecular mass of CKIC was estab­lished at 33 kDa while that of CKIR at 35-37 kDa. A protein of 40 kDa copurified with CKIR but not CKIC. Heparin significantly in­creased 40 kDa protein phosphorylation level by CKIR. Microsequencing analysis re­vealed the presence of CKI recognition motifs in the N-terminal fragment of the 40 kDa protein.

Słowa kluczowe

EN

yeast; tRNA; phosphorylation; ribosomal phosphoprotein; Trichosporon cutaneum; mRNA; biosynthesis; protein; ribosomal protein; rRNA molecule; protein kinase; modification

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2002
• Tom: 49
• Numer: 4
• Opis fizyczny: p.947-957,fig.

Twórcy

autor

Wojda I.

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

autor

Cytrynska M.

autor

Frajnt M.

autor

Jakubowicz T.

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