Characterization of the region of the aryl hydrocarbon receptor required for ligand dependency of transactivation using chimeric receptor between Drosophila and Mus musculus

Biochimica et Biophysica Acta - Gene Regulatory Mechanisms

Volumn 1789, Issue 6-8, 2009, Pages 477-486

  Kudo, Kyoko ^a   Takeuchi, Takeshi ^b   Murakami, Yusuke ^c   Ebina, Masayuki ^a   Kikuchi, Hideaki ^a,c  

^a IWATE UNIVERSITY   (Japan)

^b TOHOKU UNIVERSITY   (Japan)

^c HIROSAKI UNIVERSITY   (Japan)

Author keywords

Aryl hydrocarbon receptor; Drosophila; Hepa 1c1c7; Mouse; S2; TCDD

Indexed keywords

CHIMERIC PROTEIN; HYDROCARBON;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL ANALYSIS; DROSOPHILA; LIGAND BINDING; MOUSE; MUSCLE; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; TRANSACTIVATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BASE SEQUENCE; BINDING SITES; CELL LINE; DNA PRIMERS; DROSOPHILA PROTEINS; LIGANDS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, ARYL HYDROCARBON; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; TETRACHLORODIBENZODIOXIN; TRANSCRIPTIONAL ACTIVATION;

ANIMALIA; DROSOPHILA MELANOGASTER; INVERTEBRATA; MUS MUSCULUS; VERTEBRATA;

EID: 69349089689     PISSN: 18749399     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2009.06.003     Document Type: Article

References (36)

1. Denison M.S., Fisher J.M., and Whitlock J.P. Inducible, receptor-dependent protein-DNA interactions at a dioxin-responsive transcriptional enhancer. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 2528-2532
2. Whitlock J.P., Okino S.T., Dong L., Ko H.P., Clarke Katzenberg R., Ma Q., and Li H. Cytochromes P450 5: induction of cytochrome P4501A1: a model for analyzing mammalian gene transcription. FASEB J. 10 (1996) 809-818
3. Whitlock J.P. Induction of cytochrome P4501A1. Annu. Rev. Pharmacol. Toxicol. 39 (1999) 103-125
4. Denison M.S., and Nagy S.R. Activation of the aryl hydrocarbon receptor by structurally diverse exogenous and endogenous chemicals. Annu. Rev. Pharmacol. Toxicol. 43 (2003) 309-334
5. Safe S.H. Modulation of gene expression and endocrine response pathways by 2,3,7,8-tetrachlorodibenzo-p-dioxin and related compounds. Pharmacol. Ther. 67 (1995) 247-281
6. Poland A., and Knutson J.C. 2,3,7,8-tetrachlorodibenzo-p-dioxin and related halogenated aromatic hydrocarbons: examination of the mechanism of toxicity. Annu. Rev. Pharmacol. Toxicol. 22 (1982) 517-554
7. Birnbaum L.S. The mechanism of dioxin toxicity: relationship to risk assessment. Environ. Health Perspect. 102 Suppl. 9 (1994) 157-167
8. Okey A.B., Franc M.A., Moffat I.D., Tijet N., Boutros P.C., Korkalainen M., Tuomisto J., and Pohjanvirta R. Toxicological implications of polymorphisms in receptors for xenobiotic chemicals: the case of the aryl hydrocarbon receptor. Toxicol. Appl. Pharmacol. 207 (2005) 43-51
9. Moriguchi T., Motohashi H., Hosoya T., Nakajima O., Takahashi S., Ohsako S., Aoki Y., Nishimura N., Tohyama C., Fujii Kuriyama Y., and Yamamoto M. Distinct response to dioxin in an arylhydrocarbon receptor (AHR)-humanized mouse. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5652-5657
10. Hahn M.E. Aryl hydrocarbon receptors: diversity and evolution. Chem. Biol. Interact. 141 (2002) 131-160
11. Taylor B.L., and Zhulin I.B. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63 (1999) 479-506
12. Kewley R.J., Whitelaw M.L., and Chapman Smith A. The mammalian basic helix-loop-helix/PAS family of transcriptional regulators. Int. J. Biochem. Cell. Biol. 36 (2004) 189-204
13. Lees M.J., and Whitelaw M.L. Multiple roles of ligand in transforming the dioxin receptor to an active basic helix-loop-helix/PAS transcription factor coplex with the nuclear protein Arnt. Mol. Cell. Biol. 19 (1999) 5811-5822
14. Denison M.S., Pandini A., Nagy S.R., Baldwin E.P., and Bonati L. Ligand binding and activation of the Ah receptor. Chem. Biol. Interact. 141 (2002) 3-24
15. Crews S.T., and Fan C.M. Remembrance of things PAS: regulation of development by bHLH-PAS protein. Curr. Opin. Genet. Dev. 9 (1999) 580-587
16. Gong W., Hao B., Mansy S.S., Gonzalez G., Gilles Gonzalez M.A., and Chan M.K. Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 15177-15182
17. Pellequer J.L., Wager Smith K.A., Kay S.A., and Getzoff E.D. Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5884-5890
18. Ashok M., Turner C., and Wilson T.G. Insect juvenile hormone resistance gene homology with the bHLH-PAS family of transcriptional regulators. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2761-2766
19. Miura K., Oda M., Makita S., and Chinzei Y. Characterization of the Drosophila Methoprene-tolerant gene product. Juvenile hormone binding and ligand-dependent gene regulation. FEBS J. 272 (2005) 1169-1178
20. Butler R.A., Kelley M.L., Powell W.H., Hahn M.E., and Van Beneden R.J. An aryl hydrocarbon receptor (AHR) homologue from the soft-shell clam, Mya arenaria: evidence that invertebrate AHR homologues lack 2,3,7,8-tetrachlorodibenzo-p-dioxin and beta-naphthoflavone binding. Gene 278 (2001) 223-234
21. Powell Coffman J.A., Bradfield C.A., and Wood W.B. Caenorhabditis elegans orthologs of the aryl hydrocarbon receptor and its heterodimerization partner the aryl hydrocarbon receptor nuclear translocator. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 2844-2849
22. Sonnenfeld M., Ward M., Nystrom G., Mosher J., Stahl S., and Crews S. The Drosophila tango gene encodes a bHLH-PAS protein that is orthologous to mammalian Arnt and controls CNS midline and tracheal development. Development 124 (1997) 4571-4582
23. Emmons R.B., Duncan D., Estes P.A., Kiefel P., Mosher J.T., Sonnenfeld M., Ward M.P., Duncan I., and Crews S.T. The spineless-aristapedia and tango bHLH-PAS proteins interact to control antennal and tarsal development in Drosophila. Development 126 (1999) 3937-3945
24. Duncan D.M., Burgess E.A., and Duncan I. Control of distal antennal identity and tarsal development in Drosophila by spineless-aristapedia, a homolog of the mammalian dioxin receptor. Genes Dev. 12 (1998) 1290-1303
25. Shen J.C., Rideout W.M., and Jones P.A. High frequency mutagenesis by a DNA methyltransferase. Cell 71 (1992) 1073-1080
26. Backlund M., and Ingelman Sundberg M. Different structural requirements of the ligand binding domain of the aryl hydrocarbon receptor for high- and low-affinity ligand binding and receptor activation. Mol. Pharmacol. 65 (2004) 416-425
27. Jiang L., and Crews S.T. Transcriptional specificity of Drosophila dysfusion and the control of tracheal fusion cell gene expression. J. Biol. Chem. 282 (2007) 28659-28668
28. Burbach K.M., Poland A., and Bradfield C.A. Cloning of the Ah-receptor cDNA reveals a distinctive ligand-activated transcription factor. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 8185-8189
29. Ema M., Sogawa K., Watanabe N., Chujoh Y., Matsushita N., Gotoh O., Funae Y., and Fujii Kuriyama Y. cDNA cloning and structure of mouse putative Ah receptor. Biochem. Biophys. Res. Commun. 184 (1992) 246-253
30. Ema M., Ohe N., Suzuki M., Mimura J., Sogawa K., Ikawa S., and Fujii Kuriyama Y. Dioxin binding activities of polymorphic forms of mouse and human arylhydrocarbon receptors. J. Biol. Chem. 269 (1994) 27337-27343
31. Karchner S.I., Franks D.G., Kennedy S.W., and Hahn M.E. The molecular basis for differential dioxin sensitivity in birds: role of the aryl hydrocarbon receptor. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 6252-6257
32. Murray I.A., Reen R.K., Leathery N., Ramadoss P., Bonati L., Gonzalez F.J., Peters J.M., and Perdew G.H. Evidence that ligand binding is a key determinant of Ah receptor-mediated transcriptional activity. Arch. Biochem. Biophys. 442 (2005) 59-71
33. Goryo K., Suzuki A., Del Carpio C.A., Siizaki K., Kuriyama E., Mikami Y., Kinoshita K., Yasumoto K., Rannug A., Miyamoto A., Fujii Kuriyama Y., and Sogawa K. Identification of amino acid residues in the Ah receptor involved in ligand binding. Biochem. Biophys. Res. Commun. 354 (2007) 396-402
34. Jacobs M.N., Dickins M., and Lewis D.F. Homology modelling of the nuclear receptors: human oestrogen receptorbeta (hERbeta), the human pregnane-X-receptor (PXR), the Ah receptor (AhR) and the constitutive androstane receptor (CAR) ligand binding domains from the human oestrogen receptor alpha (hERalpha) crystal structure, and the human peroxisome proliferator activated receptor alpha (PPARalpha) ligand binding domain from the human PPARgamma crystal structure. J. Steroid. Biochem. Mol. Biol. 84 (2003) 117-132
35. Procopio M., Lahm A., Tramontano A., Bonati L., and Pitea D. A model for recognition of polychlorinated dibenzo-p-dioxins by the aryl hydrocarbon receptor. Eur. J. Biochem. 269 (2002) 13-18
36. McGuire J., Okamoto K., Whitelaw M.L., Tanaka H., and Poellinger L. Definition of a dioxin receptor mutant that is a constitutive activator of transcription: delineation of overlapping repression and ligand binding functions within the PAS domain. J. Biol. Chem. 276 (2001) 41841-41849