Histone deacetylase

Histone deacetylases ( HDACs short ) are enzymes that modify histones. They regulate not only direct the transcription of genetic information and epigenetic repression, but they are also involved in the control of cell cycle and the development of the organism. HDACs are part of larger protein complexes. They come in all living beings, and humans in all tissue types before.

Function

HDACs remove acetyl groups from acetylated lysine on the N -terminal Histonende. Deacetylation by the amino acid lysine gets a positive electric charge again. This increases the affinity of the Histonendes for the negatively charged phosphate backbone of the DNA. By the following blocking of the DNA transcription factors, the DNA transcription is downregulated. This is usually accompanied by the formation of mainly inactive heterochromatin.

HDACs also play a role in the induced by the retinoblastoma protein suppression of cell proliferation. The retinoblastoma protein is part of a complex of HDACs directed to deacetylate to chromatin there lysines.

HDAC classes in higher eukaryotes

The human HDACs are classified according to sequence and Domänverwandschaft to their orthologs in yeast into four classes:

• Class I

• Class II

• Class III

• Class IV

Together with the Azetylpolyamin amidohydrolases and acetoin Utilization proteins include histone deacetylases to histone deacetylase superfamily.

HDAC inhibitors

HDAC inhibitors (eg vorinostat ) are being studied as potential drugs in cancer research. Richon et al. have demonstrated that HDAC inhibitors can induce the CDK inhibitor 1. According to the latest research could be demonstrated that many cancer cells, including cells of breast, liver, or kidney cancer, exceptionally produce much HDAC11. Investigations are now establish to what extent HDAC11 could act as a target for new cancer therapies.