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Titolo:
Cloning and characterization of a novel human histone deacetylase, HDAC8
Autore:
Buggy, JJ; Sideris, ML; Mak, P; Lorimer, DD; McIntosh, B; Clark, JM;
Indirizzi:
AXYS Pharmaceut, S San Francisco, CA 94080 USA AXYS Pharmaceut S San Francisco CA USA 94080 San Francisco, CA 94080 USA
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 350, anno: 2000,
parte:, 1
pagine: 199 - 205
SICI:
0264-6021(20000815)350:<199:CACOAN>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACUTE PROMYELOCYTIC LEUKEMIA; X-CHROMOSOME INACTIVATION; POLYMERASE CHAIN-REACTION; COLON-CANCER-CELLS; SODIUM-BUTYRATE; TRANSCRIPTIONAL REPRESSION; SACCHAROMYCES-CEREVISIAE; HUMAN RPD3; GENE; ACETYLATION;
Keywords:
acetylation; histone H4; trichostatin A;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Buggy, JJ AXYS Pharmaceut, 180 Kimball Way, S San Francisco, CA 94080 USA AXYS Pharmaceut 180 Kimball Way S San Francisco CA USA 94080 USA
Citazione:
J.J. Buggy et al., "Cloning and characterization of a novel human histone deacetylase, HDAC8", BIOCHEM J, 350, 2000, pp. 199-205

Abstract

Histone deacetylases (HDACs) are a growing family of enzymes implicated intranscriptional regulation by affecting the acetylation state of core histones in the nucleus of cells. HDACs are known to have key roles in the regulation of cell proliferation [Brehm, Miska, McCance, Reid, Bannister and Kouzarides (1998) Nature (London) 391, 597-600], and aberrant recruitment of an HDAC complex has been shown to be a key step in the mechanism of cell transformation in acute promyelocytic leukaemia [Grignani, De Matteis, Nervi,Tomassoni, Gelmetti, Cioce, Fanelli, Ruthardt, Ferrara, Zamir et al. (1998) Nature (London) 391, 815-818; Lin, Nagy, Inoue, Shao, Miller and Evans (1998), Nature (London) 391, 811-814]. Here we present the complete nucleotide sequence of a cDNA clone, termed HDAC8, that encodes a protein product with similarity to the RPD3 class (I) of HDACs. The predicted 377-residue HDAC8 product contains a shorter C-terminal extension relative to other members of its class. After expression in two cell systems, immunopurified HDAC8 is shown to possess trichostatin A- and sodium butyrate-inhititable HDAC activity on histone H4 peptide substrates as well as on core histones. Expression profiling reveals the expression of HDACs to various degrees in every tissue tested and also in several tumour lines. Mutation of two adjacent histidine residues within the predicted active site severely decreases activity, confirming these residues as important for HDAC8 enzyme activity. Finally, linkage analysis after radiation hybrid mapping has localized HDAC8 to chromosomal position Xq21.2-Xq21.3. These results confirm HDAC8 as a new member of the HDAC family.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:28:47