Histone Deacetylases

Supporting information

Histone deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general, they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways.

There are three classes of HDACs; classes 1, 2 and 4, which are closely related Zn²⁺-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is affected by protein-protein interactions (for example HDAC-14.3.3 complexes are retained in the cytosol) and by the class to which they belong (class 1 HDACs are predominantly nuclear whilst class 2 HDACs shuttle between the nucleus and cytosol). HDACs have a role in cell growth arrest, differentiation and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents.

Histone acetylation is upregulated during memory formation but downregulated in numerous neurodegenerative diseases, such as Alzheimer's disease and Huntington's disease. As a result, HDAC inhibitors are also of great interest in neuroscience research.

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Gene	Species	Gene Symbol	Gene Accession No.	Protein Accession No.

HDAC1	Human	HDAC1	NM_004964	Q13547
	Mouse	Hdac1	NM_008228	O09106
	Rat	Hdac1	NM_001025409	Q4QQW4
HDAC2	Human	HDAC2	NM_001527	Q92769
	Mouse	Hdac2	NM_008229	P70288
	Rat	Hdac2	NM_053447	Q99PA1
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Literature for Histone Deacetylases

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