Heat shock protein hsp90 regulates dioxin receptor function in vivo

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 92; no. 10; pp. 4437 - 4441
• Main Authors: Whitelaw, M.L. (Karolinska Institutet, Huddinge, Sweden.), McGuire, J, Picard, D, Gustafsson, J.A, Poellinger, L
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 09.05.1995; National Acad Sciences; National Academy of Sciences
• Subjects: ADN; ADN RECOMBINADO; ADN RECOMBINE; Animals; Aryl Hydrocarbon Receptor Nuclear Translocator; Aryl hydrocarbon receptors; Benzoflavones - pharmacology; beta-Galactosidase - analysis; beta-Galactosidase - biosynthesis; beta-Naphthoflavone; Biochemistry; Cellular biology; Chimeras; CHIMIORECEPTEUR; COMPOSE ORGANOCHLORE; COMPUESTO ORGANICO DEL CLORO; Dioxins; Dioxins - pharmacology; DNA-Binding Proteins; ESTRES TERMICO; Gene expression regulation; GENETICA; GENETIQUE; Glucocorticoid receptors; Helix-Loop-Helix Motifs; HSP90 Heat-Shock Proteins - metabolism; Humans; Kinetics; Ligands; Medicin och hälsovetenskap; Mice; Promoter Regions, Genetic; PROTEINAS; PROTEINAS AGLUTINANTES; PROTEINE; PROTEINE DE LIAISON; Proteins; QUIMIORECEPTORES; Receptors; Receptors, Aryl Hydrocarbon - drug effects; Receptors, Aryl Hydrocarbon - metabolism; Receptors, Glucocorticoid - metabolism; Recombinant Fusion Proteins - metabolism; SACCHAROMYCES CEREVISIAE; Saccharomyces cerevisiae - metabolism; STRESS THERMIQUE; Transactivation; Transcription Factors - metabolism; Transcription, Genetic; Yeast; Yeasts

The dioxin (aryl hydrocarbon) receptor is a ligand-dependent basic helix-loop-helix (bHLH) factor that binds to xenobiotic response elements of target promoters upon heterodimerization with the bHLH partner factor Arnt. Here we have replaced the bHLH motif of the dioxin receptor with a heterologous...