Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation
Article Abstract:
The link between histone acetylation and transcription is not yet clear. However, it is believed that acetylation of certain lysine residues results in the weakening of histone-DNA interactions, leading to a less repressive chromatin structure. Evidence for this view is provided by an analysis of the structure of a transcription-associated acetyltransferase type A enzyme from the ciliate Tetrahymena. This enzyme is similar to the yeast protein Gcn5, which is known to be a transcriptional adaptor. Both Gcn5 and the enzyme have potential active sites and a well-conserved bromodomain.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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The TAFII250 subunit of TFIID has histone acetyltransferase activity
Article Abstract:
The transcription-activating factor II 250 (TAFII250) facilitates transcription from natural templates by increasing the accessibility of TFIID promoters. Analysis of TAFII250 by histone-containing gel assay indicated its histone acetyltransferse activity in vitro. Furthermore, TFIID promoters enhance the binding of transcription factors to nucleosomal deoxyribonucleic acid by mediating the removal of the core histone amino termini.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
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