Comparative Proteomic Analysis of Lysine Acetylation in Trypanosomes

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dc.citation.issue1
dc.citation.volume17
dc.contributor.authorMoretti, Nilmar Silvio [UNIFESP]
dc.contributor.authorCestari, Igor
dc.contributor.authorAnupama, Atashi
dc.contributor.authorStuart, Ken
dc.contributor.authorSchenkman, Sergio [UNIFESP]
dc.coverageWashington
dc.date.accessioned2020-07-02T18:52:11Z
dc.date.available2020-07-02T18:52:11Z
dc.date.issued2018
dc.description.abstractProtein acetylation is a post-translational modification regulating diverse cellular processes. By using proteomic approaches, we identified N-terminal and epsilon-lysine acetylated proteins in Trypanosoma cruzi and Trypanosoma brucei, which are protozoan parasites that cause significant human and animal diseases. We detected 288 lysine acetylation sites in 210 proteins of procyclic form, an insect stage of T. brucei, and 380 acetylation sites in 285 proteins in the form of the parasite that replicates in mammalian bloodstream. In T. cruzi insect proliferative form we found 389 epsilon-lysine-acetylated sites in 235 proteins. Notably, we found distinct acetylation profiles according to the developmental stage and species, with only 44 common proteins between T. brucei stages and 18 in common between the two species. While K-ac proteins from T. cruzi are enriched in enzymes involved in oxidation/reduction balance, required for the parasite survival in the host, in T. brucei, most K-ac proteins are enriched in metabolic processes, essential for its adaptation in its hosts. We also identified in both parasites a quite variable N-terminal acetylation sites. Our results suggest that protein acetylation is involved in differential regulation of multiple cellular processes in Trypanosomes, contributing to our understanding of the essential mechanisms for parasite infection and survival.en
dc.description.affiliationUniv Fed Sao Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, R Pedro de Toledo 669 L6A, BR-04039032 Sao Paulo, SP, Brazil
dc.description.affiliationCtr Infect Dis Res, 307 Westlake Ave North,Suite 500, Seattle, WA 98109 USA
dc.description.affiliationUnifespUniv Fed Sao Paulo, Escola Paulista Med, Dept Microbiol Imunol & Parasitol, R Pedro de Toledo 669 L6A, BR-04039032 Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo - FAPESP [2011/51973-3, 2015/22031-0, 2012/09403-8, 2013/20074-9]
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico - CNPq [477143/2011-3, 445655/2014-3]
dc.description.sponsorshipInstitute Nacional de Ciencia e Tecnologia de Vacinas from Brazil
dc.description.sponsorshipNational Institutes of Health [R01 AI078962]
dc.description.sponsorshipAmerican Heart Association fellowship [14POST18970046]
dc.description.sponsorshipIDFAPESP [2011/51973-3, 2015/22031-0, 2012/09403-8, 2013/20074-9]
dc.description.sponsorshipIDCNPq [477143/2011-3, 445655/2014-3]
dc.format.extent374-385
dc.identifierhttp://dx.doi.org/10.1021/acs.jproteome.7b00603
dc.identifier.citationJournal Of Proteome Research. Washington, v. 17, n. 1, p. 374-385, 2018.
dc.identifier.doi10.1021/acs.jproteome.7b00603
dc.identifier.issn1535-3893
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/53929
dc.identifier.wosWOS:000419749800035
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal Of Proteome Research
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectTrypanosoma bruceien
dc.subjectTrypanosoma cruzien
dc.subjectacetylationen
dc.subjectmass spectrometryen
dc.subjectglycolysisen
dc.subjecthistoneen
dc.subjectoxidation/reductionen
dc.titleComparative Proteomic Analysis of Lysine Acetylation in Trypanosomesen
dc.typeinfo:eu-repo/semantics/article
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