Trypanosoma cruzi: in vitro phosphorylation of tubulin by a protein kinase CK2-like enzyme |
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Authors: | Casas Beatriz Calabokis Maritza Kurz Liliana Galán-Caridad José M Bubis José Gonzatti Mary I |
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Institution: | Departamento de Biología Celular, Universidad Simón Bolívar, Apartado 89.000, Caracas, Venezuela. |
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Abstract: | One predominant 55-kDa polypeptide was phosphorylated in vitro in Trypanosoma cruzi homogenates prepared from three differentiation stages: epimastigotes, trypomastigotes, and spheromastigotes. Anti-alpha and anti-beta tubulin monoclonal antibodies immunoprecipitated the phosphorylated 55-kDa polypeptide from epimastigote extracts. Phosphoserine was the only residue phosphorylated in vitro in the 55-kDa polypeptide and in immunoprecipitated alpha tubulin. The phosphorylation of both the 55-kDa polypeptide and exogenously added casein was inhibited with GTP, heparin, and 2,3-bisphosphoglycerate in a dose-dependent manner, indicating the involvement of a CK2-like protein kinase. Moreover, when tubulin was isolated from an epimastigote homogenate by ultracentrifugation, followed by DEAE-Sephacel chromatography, a protein kinase that phosphorylated tubulin and casein co-purified with this cytoskeletal component. This result suggests an association between tubulin and its corresponding protein kinase in T. cruzi. |
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