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Cho, H. et al. A human RNA polymerase II complex containing factors that modify chromatin structure.
We recently illustrated that not only does PARP1 influence AS through its enzymatic activity, but also through its ability to modify chromatin structure.
In this review, we analyze how these elements modify chromatin structure in a hierarchical manner by acting on the nuclear machinery.
BS69 contains regions of similarity to the PHD finger, the bromodomain, and the MYND domain, all of which are found in other proteins present in high molecular weight complexes that regulate transcription and/or modify chromatin structure.
Moreover, these sequences act cooperatively in reporter gene constructs and recruit proteins that modify chromatin structure.
Instead, five encode proteins involved in transcription that bind DNA, modify chromatin structure or are regulatory subunits of RNA polymerase II.
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Co-regulator proteins in turn help connect DNA-binding TFs to the general transcriptional machinery or locally modify chromatin structures to facilitate transcriptional activation [ 18, 19].
Due to their capability of modifying chromatin structure and thereby regulating gene transcription, histone deacetylases (HDACs) have been reported to play important roles in osteogenesis and considered a promising potential therapeutic target for bone diseases, including osteoporosis.
Regarding HATs, they regulate gene expression by catalyzing acetylation of the N-terminal region of histones, thereby modifying chromatin structure in a manner that facilitates transcriptional activation [18].
For example, subtle genetic mutations in CBP may be amplified if a person has a specific environmental exposure to an agent that modifies chromatin structure.
From these results it was concluded that FOXA and HNF1 proteins are critical regulators of HNF6 expression and that binding of FOXA2 modifies chromatin structure to permit access of other transcription factors, as detailed in the study of Cirillo et al. [19].
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