Biochemical properties of human full-length aryl hydrocarbon receptor (AhR)
- 23 May 2020
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 168 (3), 285-294
- https://doi.org/10.1093/jb/mvaa047
Abstract
The aryl hydrocarbon receptor (AhR) is a very unstable protein. AhR binds to the molecular chaperone complex (HSP90-p23-XAP2) to maintain a stable structure in the cytoplasm. After binding to ligands, such as dioxin, AhR translocates from the cytoplasm to the nucleus with a molecular chaperone complex. The protein forms a heterodimer with Arnt after nuclear transfer, functions as a transcription factor by binding to a xenobiotic responsive element (XRE), and induces the cytochrome P450 1A1 (CYP1A1). Because of the unstable protein, expression of the full-length AhR in the E. coli expression system is very difficult. Many studies investigated AhR using AhR domains in vitro. We expressed and purified the human full-length AhR in E. coli expression system. Furthermore, specific antibodies were prepared. Purified full-length AhR could bind to ligand. In the presence of ligand, α-helix and random coil of AhR increased and β-sheet decreased on CD spectrum. Full-length AhR could bind to HSP90, XAP2 and p23 in the presence or absence of ligand. We now show the biochemical properties of full-length AhR.Keywords
This publication has 28 references indexed in Scilit:
- Role of aryl hydrocarbon receptor in cancerBiochimica et Biophysica Acta (BBA) - Reviews on Cancer, 2013
- Structure and Dimerization Properties of the Aryl Hydrocarbon Receptor PAS-A DomainMolecular and Cellular Biology, 2013
- New Aryl Hydrocarbon Receptor Homology Model Targeted To Improve Docking ReliabilityJournal of Chemical Information and Modeling, 2011
- Principles of Ligand Binding within a Completely Buried Cavity in HIF2α PAS-BJournal of the American Chemical Society, 2009
- Recombinant expression of aryl hydrocarbon receptor for quantitative ligand-binding analysisAnalytical Biochemistry, 2009
- Hydroxylation of HIF-1: Oxygen Sensing at the Molecular LevelPhysiology, 2004
- The Basic Helix-Loop-Helix/PAS Factor Sim Is Associated with hsp90:Online Journal of Public Health Informatics, 1995
- Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.Proceedings of the National Academy of Sciences of the United States of America, 1995
- Constitutive Function of the Basic Helix-Loop-Helix/PAS Factor Arnt.Online Journal of Public Health Informatics, 1995
- P450 GENES: STRUCTURE, EVOLUTION, AND REGULATIONAnnual Review of Biochemistry, 1987