| Literature DB >> 9974395 |
F I Rodríguez1, J J Esch, A E Hall, B M Binder, G E Schaller, A B Bleecker.
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.Entities:
Mesh:
Substances:
Year: 1999 PMID: 9974395 DOI: 10.1126/science.283.5404.996
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728