dc.creatorBatista, Cassiano Martin
dc.creatorKalb, Ligia Cristina
dc.creatorMoreira, Claudia Maria do Nascimento
dc.creatorBatista, Guilherme Tadashi Hono
dc.creatorEger, Iriane
dc.creatorSoares, Maurilio José
dc.date2016-09-19T14:54:29Z
dc.date2016-09-19T14:54:29Z
dc.date2013
dc.date.accessioned2023-09-26T22:16:27Z
dc.date.available2023-09-26T22:16:27Z
dc.identifierBATISTA, Cassiano Martin et al. Identification and subcellular localization of TcHIP, a putative Golgi zDHHC palmitoyl transferase of Trypanosoma cruzi. Exp. Parasitol. n. 134, p. 52-60, 2013.
dc.identifier0014-4894
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/15844
dc.identifier10.1016/j.exppara.2013.01.023
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8877157
dc.descriptionCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Fundação Oswaldo Cruz (Fiocruz)
dc.descriptionProtein palmitoylation is a post-translational modification that contributes to determining protein localization and function. Palmitoylation has been described in trypanosomatid protozoa, but no zDHHC palmitoyl transferase has been identified in Trypanosoma cruzi, the etiological agent of Chagas disease in Latin America. In this study we identify and show the subcellular localization of TcHIP (Tc00.1047053508199.50), a putative T. cruzi zDHHC palmitoyl transferase. Analysis of the deduced protein sequence indicates that it contains ankyrin repeats (Ank and Ank2) and the zDHHC conserved domain, typical of zDHHC palmitoyl transferases. A TcHIP polyclonal antiserum obtained from mice immunized with the purified recombinant protein was used to study the presence and subcellular localization of the native enzyme. In western blots this antiserum recognized a protein of about 95 kDa, consistent with the predicted molecular mass of TcHIP (95.4 kDa), in whole extracts of T. cruzi epimastigotes, metacyclic trypomastigotes and intracellular amastigotes. Immunolocalization by confocal microscopy showed TcHIP labeling at the Golgi complex, co-localizing with the T. cruzi Golgi marker TcRab7-GFP. Transfectant T. cruzi epimastigotes containing a construct encoding TcHIP fused to proteins A and C (TcHIP/AC) were obtained. In western blotting experiments, the TcHIP polyclonal antiserum recognized both native and TcHIP/AC proteins in extracts of the transfectants. Confocal microscopy showed co-localization of native TcHIP with TcHIP/AC. These findings demonstrate the presence of a putative zDHHC palmitoyl transferase (TcHIP) containing ankyrin and zDHHC domains in different developmental forms of T. cruzi, and its association with the Golgi complex.
dc.formatapplication/pdf
dc.languagepor
dc.publisherAnton Aebischer, Bernd Kalinna
dc.rightsrestricted access
dc.subjectTrypanosoma cruzi
dc.subjectzDHHC palmitoyl transferase
dc.subjectGolgi complex
dc.subjectExpression
dc.subjectImmunolocalization
dc.subjectComplexo de Golgi
dc.subjectRegulação da Expressão Gênica
dc.subjectFatores Imunológicos
dc.titleIdentification and subcellular localization of TcHIP, a putative Golgi zDHHC palmitoyl transferase of Trypanosoma cruzi
dc.typeArticle


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