Post-translational modifications of Trypanosoma cruzi histone H4

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dc.contributor.authorChagas da Cunha, Julia Pinheiro
dc.contributor.authorNakayasu, Ernesto Satoshi
dc.contributor.authorAlmeida, Igor Correia de
dc.contributor.authorSchenkman, Sergio
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Texas
dc.date.accessioned2016-01-24T12:41:38Z
dc.date.available2016-01-24T12:41:38Z
dc.date.issued2006-12-01
dc.description.abstractHistone tails provide sites for a variety of post-translational modifications implicated in the control of gene expression and chromatin assembly. As both histones and control of gene expression in trypanosomes are highly divergent compared to most eukaryotes, post-translational modifications of Trypanosoma cruzi histones were investigated. After in vivo incubation of live parasites with radiolabeled precursors, histone H4 mainly incorporates [H-3]-acetyl, and to a lesser extent [H-3]-methyl residues. in contrast, histone H3 preferentially incorporates [H-3]-methyl residues. the modifications of histone H4 were further characterized by mass spectrometry. MALDI-TOF-TOF-MS analysis revealed that peptides from histone H4 amino-terminus, obtained by either endoproteinase Glu-C or endoproteinase Arg-C digestion, contain isoforms with 14 and 42 Da additions, suggesting the presence of simultaneous acetylations and/or methylations. Tandem mass spectrometry analysis demonstrated that the N-terminal alanine is methylated, and lysine residues at positions 4, 10, 14 and 57 are acetylated; lysine at position 18 is mono-methylated, while arginine at position 53 is dimethylated. Immunoblotting analyses using specific antibodies raised against synthetic and acetylated peptides of T cruzi histone H4 indicate that lysine 4 is acetylated in the majority of histone H4, while other acetylations at the N-terminus portion of histone H4 are less abundant. (c) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliationUniv Texas, Dept Biol Sci, El Paso, TX 79968 USA
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent268-277
dc.identifierhttp://dx.doi.org/10.1016/j.molbiopara.2006.08.012
dc.identifier.citationMolecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 150, n. 2, p. 268-277, 2006.
dc.identifier.doi10.1016/j.molbiopara.2006.08.012
dc.identifier.issn0166-6851
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/29295
dc.identifier.wosWOS:000242476900016
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofMolecular and Biochemical Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectTrypanosoma cruzien
dc.subjecthistone H4en
dc.subjectchromatinen
dc.subjectacetylationen
dc.subjectmethylationen
dc.subjectmass spectrometryen
dc.titlePost-translational modifications of Trypanosoma cruzi histone H4en
dc.typeinfo:eu-repo/semantics/article
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