Background
Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins (1). Eight members of HDAC family have been identified in the past several years (2,3). These HDACs are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns (3). Recently, a new member of this family, HDAC-11, has been cloned by Gao et al (4). HDAC-11 transcripts were limited to kidney, heart, brain, skeletal muscle, and testis. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo. |
Reference
1. Gao L, Cueto MA, Asselbergs F, and Atadja P. J. Biol. Chem. 28: 25748-25755 (2002).
2. Meinke PT and Liberator P. Curr Med Chem, 8(2):211-235 (2001).
3. Nakayama T and Takami Y. J Biochem (Tokyo) 2001, 129 (4):491-499 (20001).
4. Cress, W.D. and Seto, E. J. Cell. Physiol. 184, 1-16 (2000).
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