Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family.

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Citation

Gao L, Cueto MA, Asselbergs F, Atadja P

Cloning and functional characterization of HDAC11, a novel member of the human histone deacetylase family.

J Biol Chem. 2002 Jul 12;277(28):25748-55. Epub 2002 Apr 10.

PubMed ID
11948178 [ View in PubMed
]
Abstract

We have cloned and characterized a human cDNA that belongs to the histone deacetylase family, which we designate as HDAC11. The predicted HDAC11 amino acid sequence reveals an open reading frame of 347 residues with a corresponding molecular mass of 39 kDa. Sequence analyses of the putative HDAC11 protein indicate that it contains conserved residues in the catalytic core regions shared by both class I and II mammalian HDAC enzymes. Putative orthologues of HDAC11 exist in primate, mouse, Drosophila, and plant. Epitope-tagged HDAC11 protein expressed in mammalian cells displays histone deacetylase activity in vitro. Furthermore, HDAC11's enzymatic activity is inhibited by trapoxin, a known histone deacetylase inhibitor. Multiple tissue Northern blot and real-time PCR experiments show that the high expression level of HDAC11 transcripts is limited to kidney, heart, brain, skeletal muscle, and testis. Epitope-tagged HDAC11 protein localizes predominantly to the cell nucleus. Co-immunoprecipitation experiments indicate that HDAC11 may be present in protein complexes that also contain HDAC6. These results indicate that HDAC11 is a novel and unique member of the histone deacetylase family and it may have distinct physiological roles from those of the known HDACs.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Histone deacetylase 6Q9UBN7Details
Histone deacetylase 11Q96DB2Details