Nucleic Acids Research, Vol 27, Issue 22 4344-4352, Copyright © 1999 by Oxford University Press
C Hettmann and D Soldati
The yeast transcriptional adaptor GCN5 functions as a histone
acetyltransferase, directly linking chromatin modification to
transcriptional regulation. Homologues of yeast GCN5 have been found in
Tetrahymena, Drosophila, Arabidopsis and human, suggesting that this
pathway of chromatin remodelling is evolutionarily conserved. Consistent
with this view, we have identified the Toxoplasma gondii homologue,
referred to here as TgGCN5. The gene codes for a protein of 474 amino acids
with an estimated molecular mass of 53 kDa. The protein reveals two regions
of close similarity with the GCN5 family members, the HAT domain and the
bromodomain. Tg GCN5 occurs in a single copy in the T.gondii genome. The
introduction of a second copy of TgGCN5 in T.gondii tachyzoites is toxic
unless the HAT activity is disrupted by a single point mutation. Full
TgGCN5 does not complement the growth defect in a yeast gcn5 (-)mutant
strain, but a chimera comprising the T.gondii HAT domain fused to the
remainder of yGCN5 does. These data show that T.gondii GNC5 is a histone
acetyltransferase attesting to the significance of chromatin remodelling in
gene regulation of Apicomplexa.
ARTICLES
Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: a novel chromatin remodelling factor in Apicomplexan parasites
Zentrum fur Molekulare Biologie Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.
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