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

BOGADO SS; DALMASSO MC; GANUZA A; KIM K; SULLIVAN WJ; ANGEL SO; VANAGAS L

MOLECULAR AND BIOCHEMICAL PARASITOLOGY

ELSEVIER SCIENCE BV

Lugar: Amsterdam; Año: 2014 vol. 197 p. 36 - 42

0166-6851

tHistone H2Ba of Toxoplasma gondii was expressed as recombinant protein (rH2Ba) and used to generateantibody in mouse that is highly specific. Antibody recognizing rH2Ba detects a single band in tachy-zoite lysate of the expected molecular weight (12 kDa). By indirect immunofluorescence (IFA) in in vitrogrown tachyzoites and bradyzoites, the signal was detected only in the parasite nucleus. The nucleosomecomposition of H2Ba was determined through co-immunoprecipitation assays. H2Ba was detected in thesame 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 andsilent regions, accompanying H2A.X and opposed to H2A.Z/H2B.Z dimers.