Canonical histone H2Ba and H2A.X dimerize in an opposite genomic localization to H2A.Z/H2B.Z dimers in Toxoplasma gondii

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Date
2014-10
Authors
Bogado, Silvina S.
Dalmasso, Carolina
Ganuza, Agustina
Kim, Kami
Sullivan, William J., Jr.
Angel, Sergio O.
Vanagas, Laura
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American English
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Department of Pharmacology and Toxicology, IU School of Medicine
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Elsevier
Abstract

Histone H2Ba of Toxoplasma gondii was expressed as recombinant protein (rH2Ba) and used to generate antibody in mouse that is highly specific. Antibody recognizing rH2Ba detects a single band in tachyzoite lysate of the expected molecular weight (12kDa). By indirect immunofluorescence (IFA) in in vitro grown tachyzoites and bradyzoites, the signal was detected only in the parasite nucleus. The nucleosome composition of H2Ba was determined through co-immunoprecipitation assays. H2Ba was detected in the same immunocomplex as H2A.X, but not with H2A.Z. Through chromatin immunoprecipitation (ChIP) assays and qPCR, it was observed that H2Ba is preferentially located at promoters of inactive genes and silent regions, accompanying H2A.X and opposed to H2A.Z/H2B.Z dimers.

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Toxoplasma, Epigenetics, Canonical histones, Nucleosome, ChIP, Chromatin
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Bogado, S. S., Dalmasso, C., Ganuza, A., Kim, K., Sullivan, W. J., Angel, S. O., & Vanagas, L. (2014). Canonical histone H2Ba and H2A.X dimerize in an opposite genomic localization to H2A.Z/H2B.Z dimers in Toxoplasma gondii. Molecular and Biochemical Parasitology, 197(0), 36–42. http://doi.org/10.1016/j.molbiopara.2014.09.009
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Molecular and Biochemical Parasitology
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PMC
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https://hdl.handle.net/1805/10744
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https://doi.org/10.1016/j.molbiopara.2014.09.009
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William J. Sullivan, Jr.