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

Ladomery, Michael; Lyons, Scott; Sommerville, John

Authors

Scott Lyons

John Sommerville



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.

Citation

Ladomery, M., Lyons, S., & Sommerville, J. (1997). Xenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes. Gene, 198(1-2), 275-280. https://doi.org/10.1016/S0378-1119%2897%2900325-9

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