Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/66535
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Type: Journal article
Title: Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR
Author: Hao, N.
Whitelaw, M.L.
Shearwin, K.E.
Dodd, I.B.
Chapman-Smith, A.
Citation: Nucleic Acids Research, 2011; 39(9):3695-3709
Publisher: Oxford University Press (OUP)
Issue Date: 2011
ISSN: 1362-4962
0305-1048
Statement of
Responsibility: 
Nan Hao, Murray L. Whitelaw, Keith E. Shearwin, Ian B. Dodd and Anne Chapman-Smith
Abstract: The basic helix-loop-helix (bHLH).PAS dimeric transcription factors have crucial roles in development, stress response, oxygen homeostasis and neurogenesis. Their target gene specificity depends in part on partner protein choices, where dimerization with common partner Aryl hydrocarbon receptor nuclear translocator (Arnt) is an essential step towards forming active, DNA binding complexes. Using a new bacterial two-hybrid system that selects for loss of protein interactions, we have identified 22 amino acids in the N-terminal PAS domain of Arnt that are involved in heterodimerization with aryl hydrocarbon receptor (AhR). Of these, Arnt E163 and Arnt S190 were selective for the AhR/Arnt interaction, since mutations at these positions had little effect on Arnt dimerization with other bHLH.PAS partners, while substitution of Arnt D217 affected the interaction with both AhR and hypoxia inducible factor-1α but not with single minded 1 and 2 or neuronal PAS4. Arnt uses the same face of the N-terminal PAS domain for homo- and heterodimerization and mutational analysis of AhR demonstrated that the equivalent region is used by AhR when dimerizing with Arnt. These interfaces differ from the PAS β-scaffold surfaces used for dimerization between the C-terminal PAS domains of hypoxia inducible factor-2α and Arnt, commonly used for PAS domain interactions.
Keywords: Cell Line; Animals; Mice; Receptors, Aryl Hydrocarbon; Two-Hybrid System Techniques; Amino Acid Substitution; Evolution, Molecular; Protein Structure, Tertiary; Dimerization; Aryl Hydrocarbon Receptor Nuclear Translocator; Basic Helix-Loop-Helix Transcription Factors; Transcriptional Activation
Rights: © The Author(s) 2011. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
RMID: 0020108738
DOI: 10.1093/nar/gkq1336
Grant ID: http://purl.org/au-research/grants/arc/DP0559011
http://purl.org/au-research/grants/arc/DP0665185
Appears in Collections:Molecular and Biomedical Science publications

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