Please use this identifier to cite or link to this item: http://repositorio.uisek.edu.ec/handle/123456789/2842
Title: INTERACTION OF TUBULIN AND PROTEIN KINASE CK2 IN TRYPANOSOMA EQUIPERDUM
Authors: Boscán, Beatriz E.
Uzcanga, Graciela L
Calabokis, Maritza
Camargo, Rocío
Aponte, Frank
Bubis, José
Keywords: PROTEÍNA QUINASA CK2
INTERACCIONES PROTEÍNA-PROTEÍNA
TRANSDUCCIÓN DE SEÑALES
TRYPANOSOMA EQUIPERDUM
TUBULINA
Issue Date: 28-May-2017
Publisher: Universidad Internacional SEK
Citation: PUB B650i/2017
Abstract: A polypeptide band with an apparent molecular weight of 55,000 was phosphorylated in vitro in whole-cell lysates of Trypanosoma equiperdum. This band corresponds to tubulin as demonstrated by immunoprecipitation of the phosphorylated polypeptide from T. equiperdum extracts when anti-α and anti-β tubulin monoclonal antibodies were employed. A parasite protein kinase CK2 was in charge of modifying tubulin given that common mammalian CK2 inhibitors such as emodin and GTP, hindered the phosphorylation of tubulin and exogenously added casein. Interestingly, a divalent cation-dependent translocation of the T. equiperdum tubulin and the CK2 responsible for its phosphorylation was noticed, suggesting a direct interaction between these two proteins. Additionally, this fraction of tubulin and its kinase coeluted using separations based on parameters as different as charge (DEAE-Sepharose anionexchange chromatography) and size (Sephacryl S-300 gel filtration chromatography). Analyses by non-denaturing polyacrylamide gel electrophoresis and immunoblot of the purified and radioactively labeled fraction containing both tubulin and the CK2 enzyme, established the phosphorylation of a single band that was recognized by anti-CK2 α-subunit and anti-tubulin antibodies. All these findings revealed a physical association between a pool of tubulin and a CK2 in T. equiperdum.
URI: https://repositorio.uisek.edu.ec/handle/123456789/2842
ISSN: 2017-0019
Appears in Collections:Publicaciones UISEK

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