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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5404
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pubmed:dateCreated |
1999-3-9
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Copper Sulfate,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylenes,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Silver,
http://linkedlifedata.com/resource/pubmed/chemical/ethylene,
http://linkedlifedata.com/resource/pubmed/chemical/ethylene receptors, plant
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
283
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
996-8
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pubmed:dateRevised |
2007-3-19
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pubmed:meshHeading |
pubmed-meshheading:9974395-Amino Acid Sequence,
pubmed-meshheading:9974395-Amino Acid Substitution,
pubmed-meshheading:9974395-Arabidopsis,
pubmed-meshheading:9974395-Bacterial Proteins,
pubmed-meshheading:9974395-Binding Sites,
pubmed-meshheading:9974395-Conserved Sequence,
pubmed-meshheading:9974395-Copper,
pubmed-meshheading:9974395-Copper Sulfate,
pubmed-meshheading:9974395-Cyanobacteria,
pubmed-meshheading:9974395-Dimerization,
pubmed-meshheading:9974395-Ethylenes,
pubmed-meshheading:9974395-Models, Molecular,
pubmed-meshheading:9974395-Mutagenesis,
pubmed-meshheading:9974395-Open Reading Frames,
pubmed-meshheading:9974395-Plant Proteins,
pubmed-meshheading:9974395-Receptors, Cell Surface,
pubmed-meshheading:9974395-Recombinant Fusion Proteins,
pubmed-meshheading:9974395-Saccharomyces cerevisiae,
pubmed-meshheading:9974395-Silver
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pubmed:year |
1999
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pubmed:articleTitle |
A copper cofactor for the ethylene receptor ETR1 from Arabidopsis.
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pubmed:affiliation |
Department of Botany, 430 Lincoln Drive, University of Wisconsin, Madison, WI 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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