Abstract:
:Histone acetylation plays an important role in regulating chromatin structure and thus gene expression. Here we describe the functional characterization of HDAC4, a human histone deacetylase whose C-terminal part displays significant sequence similarity to the deacetylase domain of yeast HDA1. HDAC4 is expressed in various adult human tissues, and its gene is located at chromosome band 2q37. HDAC4 possesses histone deacetylase activity intrinsic to its C-terminal domain. When tethered to a promoter, HDAC4 represses transcription through two independent repression domains, with repression domain 1 consisting of the N-terminal 208 residues and repression domain 2 containing the deacetylase domain. Through a small region located at its N-terminal domain, HDAC4 interacts with the MADS-box transcription factor MEF2C. Furthermore, HDAC4 and MEF2C individually upregulate but together downmodulate c-jun promoter activity. These results suggest that HDAC4 interacts with transcription factors such as MEF2C to negatively regulate gene expression.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Wang AH,Bertos NR,Vezmar M,Pelletier N,Crosato M,Heng HH,Th'ng J,Han J,Yang XJdoi
10.1128/mcb.19.11.7816subject
Has Abstractpub_date
1999-11-01 00:00:00pages
7816-27issue
11eissn
0270-7306issn
1098-5549journal_volume
19pub_type
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