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.
Xenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes
Gene 198: 275-280 (1997)
- PMID/doi: 9370292
Authors: Ladomery M, Lyons S, Sommerville J
Keywords: CYTOPLASMIC POLYADENYLATION,BACILLUS-SUBTILIS,ESCHERICHIA-COLI,GENE-EXPRESSION,REPRESSOR SIN3,YEAST,CHROMATIN,TRANSCRIPTION,DEGRADATION,ACTIVATION