A Copper Cofactor for the Ethylene Receptor ETR1 from Arabidopsis
| Autor: | G. Eric Schaller, Jeffrey J. Esch, Fernando I. Rodríguez, Anne E. Hall, Anthony B. Bleecker, Brad M. Binder |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular Copper Sulfate Silver Ethylene Recombinant Fusion Proteins Arabidopsis Receptors Cell Surface Saccharomyces cerevisiae Cyanobacteria Cofactor Conserved sequence Open Reading Frames chemistry.chemical_compound Bacterial Proteins Amino Acid Sequence Peptide sequence Conserved Sequence Plant Proteins Binding Sites Multidisciplinary biology Mutagenesis Synechocystis Ethylenes biology.organism_classification Ethylene binding Amino Acid Substitution chemistry Biochemistry biology.protein Dimerization Copper |
| Zdroj: | Science. 283:996-998 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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