Xenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes

Ladomery, Michael; Lyons, Scott; Sommerville, John

Abstract

Modification of core histones can alter chromatin structure, facilitating the activation and repression of genes. A key example is the acetylation of N-terminal lysines of the core histones. Recently, the mammalian histone deacetylase HD1 was cloned from Jurkat T cells, and shown to be 60% identical to the yeast global gene regulator Rpd3 (Taunton et al., 1996). Here we report the cloning of HDm, a maternally expressed putative deposition histone deacetylase from Xenopus laevis. Comparison of the amino acid sequences of histone deacetylases from diverse eukaryotes shows high levels of identity within a putative enzyme core region. Further alignment with other types of protein: acetoin-utilizing enzymes from eubacteria; acetylpolyamine hydrolases from mycoplasma and cyanobacteria; and a protein of unknown function from an archaebacterium, reveals an apparently conserved core, and suggests that histone deacetylases belong to an ancient family of enzymes with related functions.

• Journal Article Type: Article
• Online Publication Date: Dec 18, 1998
• Publication Date: Oct 1, 1997
• Journal: Gene
• Print ISSN: 0378-1119
• Publisher: Elsevier
• Peer Reviewed: Peer Reviewed
• Volume: 198
• Issue: 1-2
• Pages: 275-280
• DOI: https://doi.org/10.1016/S0378-1119%2897%2900325-9
• Keywords: chromatin structure, histone deposition, development, enzyme family
• Public URL: https://uwe-repository.worktribe.com/output/1101906
• Publisher URL: http://dx.doi.org/10.1016/S0378-1119(97)00325-9