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It has been previously described that post-translational modifications can regulate MeCP2 protein function.
The knowledge of H2A modifications is still very limited, and the characterisation of novel histone markers is fundamental to understand how post-translational modifications can regulate gene expression.
These modifications can regulate HMGB1 trafficking from the cytoplasm to the nucleus, its retention by apoptotic DNA, or its active release by inflammatory cells.
These modifications can regulate chromatin structure directly and frequently act as binding sites for the recruitment of other non-histone proteins to chromatin.
Some recent studies also revealed that epigenetic modifications can regulate autophagy gene expression as well as autophagy levels in both normal and cancer cells.
Histone modifications can regulate gene expression by influencing interactions between DNA and histones, for example by acetylation and methylation of conserved lysine residues in the amino-terminal tail domains [ 100].
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Posttranslational modification can regulate protein-protein interaction, modulate enzymatic activities, and influence cellular localization and protein stability [13].
O-GlcNAc modification can regulate the activity of many transcription factors (Issad and Kuo, 2008).
This modification can regulate the recognition of phosphorylated [ST]P sites by phosphatases.
It has been suggested that not only nucleosome position, but also nucleosomal histone modification, can regulate transcription [ 3, 25- 27].
The general understanding is that by altering the state of the CGI chromatin, histone modification can regulate access of the transcription machinery to particular DNA sequences [ 8].
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