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J. Biol. Chem., Vol. 277, Issue 5, 3350-3356, February 1, 2002
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From the Department of Pharmacology and Cancer Biology, Duke
University Medical Center, Durham, North Carolina 27710
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.
To whom correspondence should be addressed: Dept. of Pharmacology
and Cancer Biology, P. O. Box 3813, Duke University Medical Center,
Durham, NC 27710. Tel.: 919-613-8654; Fax: 919-681-8461; E-mail:
yao00001@mc.duke.edu.
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