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J Biol Chem. 2002 Feb 1;277(5):3350-6. Epub 2001 Nov 28.

Molecular cloning and characterization of a novel histone deacetylase HDAC10.

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  • 1Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.


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.

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