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Author Lasswell, J. ♦ Rogg, L. E. ♦ Nelson, D. C. ♦ Rongey, C. ♦ Bartel, 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 ♦ Technology ♦ Medicine & health ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Eukaryota ♦ Organisms ♦ Inorganic Chemicals ♦ Heterocyclic Compounds ♦ Amino Acids, Peptides, and Proteins ♦ Nucleic Acids, Nucleotides, and Nucleosides ♦ 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 ♦ Arabidopsis ♦ Genetics ♦ Metabolism ♦ Indoleacetic Acids ♦ Membrane Proteins ♦ Amino Acid Sequence ♦ Animals ♦ Cloning, Molecular ♦ Dna, Complementary ♦ Manganese ♦ Pharmacology ♦ Chemistry ♦ Mice ♦ Molecular Sequence Data ♦ Nerve Tissue Proteins ♦ Phenotype ♦ Sequence Homology, Amino Acid ♦ Journal Article ♦ Research Support, Non-u.s. Gov't ♦ Research Support, U.s. Gov't, Non-p.h.s. ♦ Research Support, U.s. Gov't, P.h.s.
Abstract Most indole-3-acetic acid (IAA) in higher plants is conjugated to amino acids, sugars, or peptides, and these conjugates are implicated in regulating the concentration of the free hormone. We identified iar1 as an Arabidopsis mutant that is resistant to the inhibitory effects of several IAA-amino acid conjugates but remains sensitive to free IAA. iar1 partially suppresses phenotypes of a mutant that overproduces IAA, suggesting that IAR1 participates in auxin metabolism or response. We used positional information to clone IAR1, which encodes a novel protein with seven predicted transmembrane domains and several His-rich regions. IAR1 has homologs in other multicellular organisms, including Drosophila, nematodes, and mammals; in addition, the mouse homolog KE4 can functionally substitute for IAR1 in vivo. IAR1 also structurally resembles and has detectable sequence similarity to a family of metal transporters. We discuss several possible roles for IAR1 in auxin homeostasis.
Description Country affiliation: United States
Author Affiliation: Lasswell J ( Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005-1892, 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 2000-12-01
Publisher Place United States
e-ISSN 1531298X
Volume Number 12
Issue Number 12

Source: WHO-Global Index Medicus