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Expression, Purification, and S-nitrosylation of Recombinant Histone Deacetylase 8 in Escherichia Coli

Expression, Purification, and S-nitrosylation of Recombinant Histone Deacetylase 8 in Escherichia Coli

J H Feng, F B Jing, H Fang, L C Gu, W F Xu

Biosci Trends. 2011;5(1):17-22.

PMID: 21422596

Abstract:

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42413434	HDAC-8 human			Price

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