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)
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.
| 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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