Histone deacetylase inhibitors mediate post-transcriptional regulation of p21WAF1 through novel cis-acting elements in the 3' untranslated region.

Histone deacetylase inhibitors (HDACIs) are promising anti-tumor agents that selectively induce cell cycle arrest, differentiation and/or apoptosis of tumor cells. Fundamentally, HDACIs are proposed to function by activating the transcription of genes, including the potent cyclin dependent kinase inhibitor p21(WAF1). However, HDACIs primarily increase p21(WAF1) expression at the post-transcriptional level in HepG2 cells, implying that these anti-tumor agents regulate genes at multiple levels.

Determination of protein lysine deacetylation.

Histone deacetylases (HDACs) are members of a diverse family of enzymes that catalyze the removal of an acetyl moiety from an acetyl-lysine-containing substrate. HDACs target a variety of substrates, including histone and nonhistone proteins, to mediate alterations in protein localization, stability, and activity. In addition, HDACs have been shown to modulate changes in gene expression, primarily through the recruitment of transcriptional cofactors to promoter regions.

The modification of Sp3 isoforms by SUMOylation has differential effects on the SRC1A promoter.

Previously, we had described a housekeeping like promoter that regulates expression of the SRC gene in many cell types. This promoter was found to be regulated by Sp1 and hnRNP-K. However, at that time we could find little evidence supporting a significant role for Sp3 in SRC activation.