copper cofactor for the ethylene receptor ETR1 from Arabidopsis

• Published in: Science (American Association for the Advancement of Science) Vol. 283; no. 5404; pp. 996 - 998
• Main Authors: Rodriguez, F.I, Esch, J.J, Hall, A.E, Binder, B.M, Schaller, G.E, Bleecker, A.B
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 12.02.1999; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: Amino Acid Sequence; Amino Acid Substitution; Amino acids; Arabidopsis; Arabidopsis - genetics; Arabidopsis - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; binding; Binding Sites; Biological and medical sciences; Biology; Cell membranes; Cells; Centrifugation; Chemistry; Classical genetics, quantitative genetics, hybrids; Coding; cofactors; Conserved Sequence; Copper; Copper - analysis; Copper - metabolism; Copper Sulfate - pharmacology; Cyanobacteria; Cyanobacteria - genetics; Cyanobacteria - metabolism; Cytology; Dimerization; Dimers; Ethylene; Ethylenes - metabolism; Fundamental and applied biological sciences. Psychology; Genetics of eukaryotes. Biological and molecular evolution; Grants; Hormones; ion activity; mechanism of action; Models, Molecular; Mutagenesis; Open Reading Frames; Organic Chemistry; plant physiology; Plant Proteins - chemistry; Plant Proteins - genetics; Plant Proteins - isolation & purification; Plant Proteins - metabolism; Pteridophyta, spermatophyta; Receptors; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - genetics; Receptors, Cell Surface - isolation & purification; Receptors, Cell Surface - metabolism; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Saccharomyces cerevisiae; Silver - metabolism; Silver - pharmacology; structural models; Synechocystis; Vegetals; Yeasts; Ligand binding; Arabidopsis; Ethylene; Molecular interaction; Synechocystis; Cofactor; Gene; Cruciferae; Dicotyledones; Angiospermae; Cyanobacteria; Bacteria; Plant growth substance; Spermatophyta; Mutation; Copper; Hormonal receptor
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.283.5404.996

The ETR1 receptor from Arabidopsis binds the gaseous hormone ethylene. A copper ion associated with the ethylene-binding domain is required for high-affinity ethylene-binding activity. A missense mutation in the domain that renders the plant insensitive to ethylene eliminates both ethylene binding and the interaction of copper with the receptor. A sequence from the genome of the cyanobacterium Synechocystis sp. strain 6803 that shows homology to the ethylene-binding domain of ETR1 encodes a functional ethylene-binding protein. On the basis of sequence conservation between the Arabidopsis and the cyanobacterial ethylene-binding domains and on in vitro mutagenesis of ETR1, a structural model for this copper-based ethylene sensor domain is presented.