A copper cofactor for the ethylene receptor ETR1 from Arabidopsis.
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.
Rodríguez
F I
FI
Department of Botany, 430 Lincoln Drive, University of Wisconsin, Madison, WI 53706, USA.
Esch
J J
JJ
Hall
A E
AE
Binder
B M
BM
Schaller
G E
GE
Bleecker
A B
AB
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D001665:Binding Sites; D017124:Conserved Sequence; D003300:Copper / Q000032:analysis / Q000378:metabolism*; D019327:Copper Sulfate / Q000494:pharmacology; D000458:Cyanobacteria / Q000235:genetics / Q000378:metabolism; D019281:Dimerization; D005030:Ethylenes / Q000378:metabolism*; D008958:Models, Molecular; D016296:Mutagenesis; D016366:Open Reading Frames; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae; D012834:Silver / Q000378:metabolism / Q000494:pharmacology