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

Ladomery, M., Lyons, S., Sommerville, J. (October 1997) Xenopus HDm, a maternally expressed histone deacetylase, belongs to an ancient family of acetyl-metabolizing enzymes. Gene, 198 (1-2). pp. 275-80. ISSN 0378-1119 (Print)0378-1119 (Linking)

URL: https://www.ncbi.nlm.nih.gov/pubmed/9370292
DOI: 10.1016/s0378-1119(97)00325-9


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.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Base Sequence Biological Evolution Gene Expression Regulation, Developmental Histone Deacetylases/*genetics Molecular Sequence Data Phylogeny Restriction Mapping Sequence Alignment Sequence Homology, Amino Acid Xenopus laevis/*genetics
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > histone deacetylase
CSHL Authors:
Communities: CSHL labs > Lyons lab
Depositing User: Matt Covey
Date: 1 October 1997
Date Deposited: 12 May 2017 19:38
Last Modified: 12 May 2017 19:38
Related URLs:
URI: https://repository.cshl.edu/id/eprint/34716

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