Journal
BIOSCIENCE TRENDS
Volume 5, Issue 1, Pages 17-22Publisher
IRCA-BSSA
DOI: 10.5582/bst.2011.v5.1.17
Keywords
Histone deacetylase 8; S-nitrosylation; nitric oxide; S-nitrosoglutathione; S-nitrosocysteine
Categories
Funding
- State Key Laboratory of Microbial Technology, School of Life Sciences in Shandong University
- National High Technology Research and Development Program of China (863 project) [2007AA02Z314]
- Important National Science & Technology Specific Projects of China [2009ZX09103-118]
Ask authors/readers for more resources
Histone deacetylase (HDAC) 8 is a zinc ion dependent enzyme involved in removing the acetyl group from the core histones and other proteins which belong to Class I HDACs. It was reported that nitric oxide (NO) is a key regulator of HDAC function and S-nitrosylation of HDAC2 induces chromatin remodelling in neurons. This work reports the successful recombinant expression of human HDAC8 in Escherichia coli with two plasmids and the purification and S-nitrosylation in vitro. It was found that HDAC8 can be S-nitrosylated by the NO donor S-nitrosoglutathione (GSNO) in vitro, and the activity of HDAC8 was significantly inhibited when incubated with GSNO and S-nitrosocysteine in a time-and dosage-dependent manner, but sodium nitroprusside (SNP), and dithiothreitol cannot reverse this inhibition. These observations support and extend the concept that NO may regulate HDAC8 function by S-nitrosylation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available