Targeting chromatin disruption: transcription regulators that acetylate histones

Article Abstract:

DNA packaging proteins assist in the regulation of transcription by targeting proteins that alter chromatin structure. The regulatory role of DNA packaging proteins is, in turn, linked to histone acetylization levels and transcriptional activity as these two factors determine nucleosomal composition. Research shows that the regulator protein GCN5 plays a vital role in histone acetylation during the transcription stage. Analysis of the acetylation mechanism also suggests that there are several other regulatory proteins that have the ability to modify histones.

DNA

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A positive role for histone acetylation in transcription factor access to nucleosomal DNA

Article Abstract:

The presence of tetrameric or octameric histones within the 5S RNA gene inhibits the binding of transcription factor (TF) IIIA. The influence of nucleosome modification on the association of sequence-specific DNA-binding proteins with chromatin was investigated. The results showed that acetylation of the core histones relieves the inhibition of TFIIIA binding. It is proposed that acetylation of the core histones comprises a major positive regulatory mechanism that maintains accessibility of chromatin to regulatory molecules.

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Stabilization of chromatin structure by PRC1, a polycomb complex

Article Abstract:

Certain PcG proteins are believed to physically spread along the chromatin to produce a repressed state wherever they are present. However, these proteins are also found to be able to repress access to DNA over a wide region through mechanisms that do not require continual stable binding of PcG proteins to the repressed region. Findings indicate that several different types of repressive complexes, such as deacetylases, interact with histone tails.

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