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dc.contributor.authorLeite, Ariely Barbosa [UNIFESP]
dc.contributor.authorGomes, Antoniel Augusto Severo
dc.contributor.authorSousa, Ana Caroline de Castro Nascimento [UNIFESP]
dc.contributor.authorFontes, Marcos Roberto de Mattos
dc.contributor.authorSchenkman, Sergio [UNIFESP]
dc.contributor.authorMoretti, Nilmar Silvio [UNIFESP]
dc.date.accessioned2021-11-29T16:05:51Z
dc.date.available2021-11-29T16:05:51Z
dc.date.issued2020
dc.identifier.urihttps://repositorio.unifesp.br/xmlui/handle/11600/62326
dc.description.abstractPost-translational modifications provide suitable mechanisms for cellular adaptation to environmental changes. Lysine acetylation is one of these modifications and occurs with the addition of an acetyl group to Nε-amino chain of this residue, eliminating its positive charge. Recently, we found distinct acetylation profiles of procyclic and bloodstream forms of Trypanosoma brucei, the agent of African Trypanosomiasis. Interestingly, glyco- lytic enzymes were more acetylated in the procyclic, which develops in insects and uses oxidative phosphorylation to obtain energy, compared with the bloodstream form, whose main source of energy is glycolysis. Here, we investigated whether acetylation regulates the T. brucei fructose 1,6-bisphosphate aldolase. We found that aldolase activity was reduced in procyclic parasites cultivated in the absence of glucose and partial recovered by in vitro deacetylation. Similarly, acetylation of protein extracts from procyclics culti- vated in glucose-rich medium, caused a reduction in the aldolase activity. In addition, aldolase acetylation levels were higher in procyclics cultivated in the absence of glucose compared with those cultivated in the presence of glucose. To further confirm the role of acetylation, lysine residues near the catalytic site were substituted by glutamine in recom- binant T. brucei aldolase. These replacements, especially K157, inhibited enzymatic activ- ity, changed the electrostatic surface potential, decrease substrate binding and modify the catalytic pocket structure of the enzyme, as predicted by in silico analysis. Taken together, these data confirm the role of acetylation in regulating the activity of an enzyme from the glycolytic pathway of T. brucei, expanding the factors responsible for regulating important pathways in this parasite.pt_BR
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)pt_BR
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)pt_BR
dc.languageengpt_BR
dc.publisherPortland Presspt_BR
dc.relation.ispartofBiochemical Journalpt_BR
dc.rightsAcesso restritopt_BR
dc.subjectT bruceipt_BR
dc.subjectAldolasept_BR
dc.subjectAcetylationpt_BR
dc.titleEffect of lysine acetylation on the regulation of Trypanosoma brucei glycosomal aldolase activitypt_BR
dc.typeArtigopt_BR
dc.description.sponsorshipIDFAPESP: 2018/09948-0pt_BR
dc.description.sponsorshipIDCNPq: 424729/2018pt_BR
dc.identifier.doihttps://doi.org/10.1042/BCJ20200142pt_BR
unifesp.campusEscola Paulista de Medicina (EPM)pt_BR
unifesp.graduateProgramMicrobiologia e Imunologiapt_BR
unifesp.knowledgeAreaOutrapt_BR
dc.contributor.authorLatteshttp://lattes.cnpq.br/2131472726202687pt_BR
unifesp.departamentoMicrobiologia, Imunologia e Parasitologiapt_BR


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