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Papers In Press, published online ahead of print November 28, 2001
J. Biol. Chem, 10.1074/jbc.M109861200
Submitted on October 11, 2001
Revised on November 27, 2001
Accepted on November 27, 2001

Molecular cloning and characterization of a novel histone deacetylase HDAC10

Amaris R. Guardiola and Tso-Pang Yao

Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710

Corresponding Author: yao00001{at}mc.duke.edu

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 deacetylases, 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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