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Author Wang, Wuyi ♦ Esch, Jeff J. ♦ Shiu, Shin-Han ♦ Agula, Hasi ♦ Binder, Brad M. ♦ Chang, Caren ♦ Patterson, Sara E. ♦ Bleecker, Anthony B.
Source World Health Organization (WHO)-Global Index Medicus
Content type Text
Publisher American Society of Plant Biologists
File Format HTM / HTML
Language English
Difficulty Level Medium
Subject Domain (in DDC) Computer science, information & general works ♦ Library & information sciences ♦ Natural sciences & mathematics ♦ Chemistry & allied sciences ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Genetics and evolution ♦ Natural history of organisms ♦ Microorganisms, fungi & algae ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Eukaryota ♦ Bacteria ♦ Organisms ♦ Organic Chemicals ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Genetic Phenomena ♦ Biological Sciences ♦ Information Science ♦ Information Science
Subject Keyword Discipline Botany ♦ Arabidopsis Proteins ♦ Chemistry ♦ Metabolism ♦ Arabidopsis ♦ Ethylenes ♦ Receptors, Cell Surface ♦ Signal Transduction ♦ Amino Acid Sequence ♦ Amino Acids ♦ Genetics ♦ Growth & Development ♦ Bacteria ♦ Genes, Plant ♦ Genetic Complementation Test ♦ Genome ♦ Models, Biological ♦ Molecular Sequence Data ♦ Mutation ♦ Phylogeny ♦ Protein Structure, Tertiary ♦ Seedling ♦ Sequence Alignment ♦ Structure-activity Relationship ♦ Transgenes ♦ Yeasts ♦ Journal Article ♦ Research Support, N.i.h., Extramural ♦ Research Support, Non-u.s. Gov't ♦ Research Support, U.s. Gov't, Non-p.h.s.
Abstract The ethylene binding domain (EBD) of the Arabidopsis thaliana ETR1 receptor is modeled as three membrane-spanning helices. We surveyed ethylene binding activity in different kingdoms and performed a bioinformatic analysis of the EBD. Ethylene binding is confined to land plants, Chara, and a group of cyanobacteria but is largely absent in other organisms, consistent with our finding that EBD-like sequences are overrepresented among plant and cyanobacterial species. We made amino acid substitutions in 37 partially or completely conserved residues of the EBD and assayed their effects on ethylene binding and signaling. Mutations primarily in residues in Helices I and II midregions eliminated ethylene binding and conferred constitutive signaling, consistent with the inverse-agonist model of ethylene receptor signaling and indicating that these residues define the ethylene binding pocket. The largest class of mutations, clustered near the cytoplasmic ends of Helices I and III, gave normal ethylene binding activity yet still conferred constitutive signaling. Therefore, these residues may play a role in turning off the signal transmitter domain of the receptor. By contrast, only two mutations were loss of function with respect to signaling. These findings yield insight into the structure and function of the EBD and suggest a conserved role of the EBD as a negative regulator of the signal transmitter domain.
Description Country affiliation: United States
Author Affiliation: Wang W ( Department of Botany, University of Wisconsin, Madison, Wisconsin 53706, USA.)
ISSN 10404651
Educational Role Student ♦ Teacher
Age Range above 22 year
Educational Use Reading ♦ Research ♦ Self Learning
Interactivity Type Expositive
Education Level UG and PG
Learning Resource Type Article
Publisher Date 2006-12-01
Publisher Place United States
e-ISSN 1531298X
Journal THE PLANT CELL ONLINE
Volume Number 18
Issue Number 12


Source: WHO-Global Index Medicus