Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1999-12-28
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1362-4962
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4344-52
pubmed:dateRevised
2008-11-20
pubmed:meshHeading
pubmed-meshheading:10536141-Acetylation, pubmed-meshheading:10536141-Acetyltransferases, pubmed-meshheading:10536141-Amino Acid Sequence, pubmed-meshheading:10536141-Animals, pubmed-meshheading:10536141-Chromatin, pubmed-meshheading:10536141-Cloning, Organism, pubmed-meshheading:10536141-Gene Expression Regulation, Enzymologic, pubmed-meshheading:10536141-Genetic Complementation Test, pubmed-meshheading:10536141-Histone Acetyltransferases, pubmed-meshheading:10536141-Histones, pubmed-meshheading:10536141-Humans, pubmed-meshheading:10536141-Molecular Sequence Data, pubmed-meshheading:10536141-Plasmodium falciparum, pubmed-meshheading:10536141-Point Mutation, pubmed-meshheading:10536141-Protozoan Proteins, pubmed-meshheading:10536141-Saccharomyces cerevisiae, pubmed-meshheading:10536141-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10536141-Sequence Homology, Amino Acid, pubmed-meshheading:10536141-Toxoplasma, pubmed-meshheading:10536141-Transcription Factors
pubmed:year
1999
pubmed:articleTitle
Cloning and analysis of a Toxoplasma gondii histone acetyltransferase: a novel chromatin remodelling factor in Apicomplexan parasites.
pubmed:affiliation
Zentrum für Molekulare Biologie Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't