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PMID:11739383

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Citation

Fischer, DD, Cai, R, Bhatia, U, Asselbergs, FA, Song, C, Terry, R, Trogani, N, Widmer, R, Atadja, P and Cohen, D (2002) Isolation and characterization of a novel class II histone deacetylase, HDAC10. J. Biol. Chem. 277:6656-66

Abstract

A novel histone deacetylase, HDAC10, was isolated from a mixed tissue human cDNA library. HDAC10 was classified as a class II subfamily member based upon similarity to HDAC6. The genomic structure of HDAC10 was found to consist of 20 exons. HDAC10 has two sequence variants, HDAC10v1 and HDAC10v2, and two transcripts were detectable by Northern blot analysis. HDAC10v1 and HDAC10v2 were found to be identical through exon 17 but diverged after this exon. HDAC10v2 has an 82-bp alternate exon that generates a frameshift and shortens the sequence by 11 amino acids. In this study, the characterization of HDAC10v1 was performed. HDAC10v1 has an N-terminal catalytic domain, two putative C-terminal retinoblastoma protein binding domains, and a nuclear hormone receptor binding motif. The HDAC10v1 enzyme was found to be catalytically active based upon its ability to deacetylate a (3)H-acetylated histone H4 N-terminal peptide. Immunofluorescence detection of transfected HDAC10v1-FLAG indicated that the enzyme is a nuclear protein. Furthermore, coimmunoprecipitation experiments indicated that HDAC10v1 associated with HDAC2 and SMRT (silencing mediator for retinoid and thyroid hormone receptors). In addition, based upon the public data base, a single nucleotide polymorphism was found in the C terminus of HDAC10 which changes a Gly residue to Cys, suggesting that HDAC10 molecules containing these single nucleotide polymorphisms may be folded improperly. HDAC10 extends the HDAC superfamily and adds to a growing number of HDACs that have been found to have splice variants, suggesting that RNA processing may play a role in mediating the activity of HDACs.

Links

PubMed Online version:10.1074/jbc.M108055200

Keywords

Amino Acid Sequence; Base Sequence; Catalytic Domain; Cell Line; DNA, Complementary/genetics; Female; Gene Library; Genetic Variation; Histone Deacetylases/genetics; Histone Deacetylases/isolation & purification; Histone Deacetylases/metabolism; Humans; Male; Molecular Sequence Data; Organ Specificity; Polymerase Chain Reaction; Sequence Alignment; Sequence Homology, Amino Acid; Sequence Homology, Nucleic Acid; Tumor Cells, Cultured

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:HDAC1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q92769

F

Seeded From UniProt

complete

HUMAN:HDAC1

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9Y618

F

Seeded From UniProt

complete

HUMAN:HDAC2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13547

F

Seeded From UniProt

complete

HUMAN:HDA10

involved_in

GO:0016575: histone deacetylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:HDA10

located_in

GO:0005634: nucleus

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:HDA10

enables

GO:0004407: histone deacetylase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:NCOR2

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13547

F

Seeded From UniProt

complete


See also

References

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