Post-translational modifications of Trypanosoma cruzi histone H4

Post-translational modifications of Trypanosoma cruzi histone H4

Author Chagas da Cunha, Julia Pinheiro Google Scholar
Nakayasu, Ernesto Satoshi Google Scholar
Almeida, Igor Correia de Google Scholar
Schenkman, Sergio Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Univ Texas
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.
Keywords Trypanosoma cruzi
histone H4
mass spectrometry
Language English
Date 2006-12-01
Published in Molecular and Biochemical Parasitology. Amsterdam: Elsevier B.V., v. 150, n. 2, p. 268-277, 2006.
ISSN 0166-6851 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 268-277
Access rights Closed access
Type Article
Web of Science ID WOS:000242476900016

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