Histone acetylation and transcriptional regulatory mechanisms

Article Abstract:

More is known about molecular mechanisms by which histone acetylation affects transcriptional activity in living cells. Identification of proteins with intrinsic histone acetylase and deacetylase activity has been a factor in increasing knowledge about the causal relationship between histone acetylation and gene expression. Histone acetylases and deacetylases give an important link between chromatin structure and transcription output. Experimental intervention is possible. Chromatin is not just a structure that compacts DNA in the nucleus and acts as a passive substrate, but plays a role in transcription through histone acetylation.

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DNA damage activates p53 through a phosphorylation-acetylation cascade

Article Abstract:

DNA damage appears to enhance p53 activity as a transcription factor partly through carboxy-terminal acetylation that is itself directed by amino-terminal phosphorylation. The activation involves a phosphorylation-acetylation cascade. In vitro p53 is acetylated at different sites by two histone acetyltransferases (HATs), p300 and PCAF, coactivators. At both sites the acetylations enhance sequence-specific DNA binding.

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Nucleosome stability mediated by histone variants H3.3and H2A.Z

Article Abstract:

The study was undertaken to determine the unique properties possessed by nucleosomes their sensitivity of transcription and disruption when mediated by histone variants.

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