Document Detail

Molecular cloning and characterization of a novel histone deacetylase HDAC10.
MedLine Citation:
PMID:  11726666     Owner:  NLM     Status:  MEDLINE    
The growing number of proteins controlled by reversible acetylation suggests the existence of a large number of acetyltransferases and deacetylases. Here, we report the identification of a novel class II histone deacetylase, HDAC10. Homology comparison indicates that HDAC10 is most similar to HDAC6. Both contain a unique, putative second catalytic domain not found in other HDACs. In HDAC10, however, this domain is not functional. This tandem organization of two catalytic domains confers resistance to the inhibitors trapoxin B and sodium butyrate, which potently inhibit the deacetylase activity of all other HDAC members. Thus, HDAC10 and HDAC6 share unusual structural and pharmacological characteristics. However, unlike HDAC6, which is normally a cytoplasmic deacetylase, HDAC10 resides in both the nucleus and cytoplasm. In the nucleus, when tethered to a promoter, HDAC10 represses transcription independent of its deacetylase activity, indicating that HDAC10 contains a distinct transcriptional repressor domain. These observations suggest that HDAC10 might uniquely play roles both in the nucleus, as a transcriptional modulator, and in the cytoplasm in an unidentified role. Together, our results identify HDAC10 as a novel deacetylase with distinct structure, pharmacology and localization and further expand the complexity of the HDAC family.
Amaris R Guardiola; Tso-Pang Yao
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't     Date:  2001-11-28
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Feb 
Date Detail:
Created Date:  2002-01-28     Completed Date:  2002-02-28     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3350-6     Citation Subset:  IM    
Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
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MeSH Terms
Amino Acid Sequence
Catalytic Domain
Cell Line
Chromosome Mapping
Chromosomes, Human, Pair 22
Cloning, Molecular
DNA Primers
Gene Expression Regulation
Histone Deacetylases / chemistry,  genetics*,  metabolism
Molecular Sequence Data
Polymerase Chain Reaction
Recombinant Proteins / chemistry,  metabolism
Repressor Proteins / metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Transcription, Genetic
Reg. No./Substance:
0/DNA Primers; 0/Recombinant Proteins; 0/Repressor Proteins; EC protein, human; EC protein, human; EC Deacetylases

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