XENOPUS HDM, A MATERNALLY EXPRESSED HISTONE DEACETYLASE, BELONGS TO AN ANCIENT FAMILY OF ACETYL-METABOLIZING ENZYMES

Modification of core histones can alter chromatin structure, facilitat ing the activation and repression of genes. A key example is the acety lation of N-terminal lysines of the core histones. Recently, the mamma lian 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 express ed putative deposition histone deacetylase from Xenopus laevis. Compar ison 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-utiliz ing enzymes from eubacteria; acetylpolyamine hydrolases from mycoplasm a and cyanobacteria; and a protein of unknown function from an archaeb acterium, reveals an apparently conserved core, and suggests that hist one deacetylases belong to an ancient family of enzymes with related f unctions. (C) 1997 Elsevier Science B.V.