Abstract
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.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Arabidopsis / genetics
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Arabidopsis / metabolism*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Binding Sites
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Conserved Sequence
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Copper / analysis
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Copper / metabolism*
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Copper Sulfate / pharmacology
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Cyanobacteria / genetics
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Cyanobacteria / metabolism
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Dimerization
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Ethylenes / metabolism*
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Models, Molecular
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Mutagenesis
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Open Reading Frames
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Plant Proteins / chemistry
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Plant Proteins / genetics
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Plant Proteins / isolation & purification
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Plant Proteins / metabolism*
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / isolation & purification
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Receptors, Cell Surface / metabolism*
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae
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Silver / metabolism
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Silver / pharmacology
Substances
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Bacterial Proteins
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Ethylenes
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Plant Proteins
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Receptors, Cell Surface
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Recombinant Fusion Proteins
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ethylene receptors, plant
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Silver
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Copper
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ethylene
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Copper Sulfate