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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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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.
Some recent studies also revealed that epigenetic modifications can regulate autophagy gene expression as well as autophagy levels in both normal and cancer cells.
These modifications can regulate chromatin structure directly and frequently act as binding sites for the recruitment of other non-histone proteins to chromatin.
These modifications can regulate HMGB1 trafficking from the cytoplasm to the nucleus, its retention by apoptotic DNA, or its active release by inflammatory cells.
Since both CpG and non-CpG methylated sites were located within the promoter region of the PH and in CSBI-III, it is plausible that epigenetic modifications can regulate replication and/or transcription of the mtDNA.
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