Post-translational modifications of Trypanosoma cruzi histone H4

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dc.contributor.author Chagas da Cunha, Julia Pinheiro
dc.contributor.author Nakayasu, Ernesto Satoshi
dc.contributor.author Almeida, Igor Correia de
dc.contributor.author Schenkman, Sergio
dc.date.accessioned 2016-01-24T12:41:38Z
dc.date.available 2016-01-24T12:41:38Z
dc.date.issued 2006-12-01
dc.identifier http://dx.doi.org/10.1016/j.molbiopara.2006.08.012
dc.identifier.citation Molecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 150, n. 2, p. 268-277, 2006.
dc.identifier.issn 0166-6851
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/29295
dc.description.abstract Histone 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.format.extent 268-277
dc.language.iso eng
dc.publisher Elsevier B.V.
dc.relation.ispartof Molecular and Biochemical Parasitology
dc.rights Acesso restrito
dc.subject Trypanosoma cruzi en
dc.subject histone H4 en
dc.subject chromatin en
dc.subject acetylation en
dc.subject methylation en
dc.subject mass spectrometry en
dc.title Post-translational modifications of Trypanosoma cruzi histone H4 en
dc.type Artigo
dc.rights.license http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Univ Texas
dc.description.affiliation Universidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.description.affiliation Univ Texas, Dept Biol Sci, El Paso, TX 79968 USA
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Dept Microbiol Immunol & Parasitol, BR-04023062 São Paulo, Brazil
dc.identifier.doi 10.1016/j.molbiopara.2006.08.012
dc.description.source Web of Science
dc.identifier.wos WOS:000242476900016



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