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Author Hamburger, Dirk ♦ Rezzonico, Enea ♦ MacDonald-Comber Petétot, Jean ♦ Somerville, Chris ♦ Poirier, Yves
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 anatomy, cytology, histology ♦ Human physiology ♦ Pharmacology and therapeutics ♦ Diseases ♦ Manufacture for specific uses ♦ Precision instruments & other devices
Subject Domain (in MeSH) Plant Structures ♦ Anatomy ♦ Eukaryota ♦ Organisms ♦ Inorganic Chemicals ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Metabolism ♦ Genetic Phenomena ♦ Biological Sciences ♦ Information Science ♦ Information Science
Subject Keyword Discipline Botany ♦ Arabidopsis Proteins ♦ Genetics ♦ Arabidopsis ♦ Phosphate Transport Proteins ♦ Phosphates ♦ Metabolism ♦ Plant Structures ♦ Alleles ♦ Amino Acid Sequence ♦ Physiology ♦ Biological Transport ♦ Chromosome Mapping ♦ Gene Expression Profiling ♦ Gene Expression Regulation, Plant ♦ Molecular Sequence Data ♦ Mutation ♦ Phosphorus ♦ Pharmacology ♦ Plants, Genetically Modified ♦ Sequence Homology, Amino Acid ♦ Signal Transduction ♦ Comparative Study ♦ Journal Article ♦ Research Support, Non-u.s. Gov't ♦ Research Support, U.s. Gov't, Non-p.h.s.
Abstract The Arabidopsis mutant pho1 is deficient in the transfer of Pi from root epidermal and cortical cells to the xylem. The PHO1 gene was identified by a map-based cloning strategy. The N-terminal half of PHO1 is mainly hydrophilic, whereas the C-terminal half has six potential membrane-spanning domains. PHO1 shows no homology with any characterized solute transporter, including the family of H(+)-Pi cotransporters identified in plants and fungi. PHO1 shows highest homology with the Rcm1 mammalian receptor for xenotropic murine leukemia retroviruses and with the Saccharomyces cerevisiae Syg1 protein involved in the mating pheromone signal transduction pathway. PHO1 is expressed predominantly in the roots and is upregulated weakly under Pi stress. Studies with PHO1 promoter-beta-glucuronidase constructs reveal predominant expression of the PHO1 promoter in the stelar cells of the root and the lower part of the hypocotyl. There also is beta-glucuronidase staining of endodermal cells that are adjacent to the protoxylem vessels. The Arabidopsis genome contains 10 additional genes showing homology with PHO1. Thus, PHO1 defines a novel class of proteins involved in ion transport in plants.
Description Country affiliation: Switzerland
Author Affiliation: Hamburger D ( Institut d'Ecologie-Biologie et Physiologie Végétales, Bâtiment de Biologie, Université de Lausanne, CH-1015 Lausanne, Switzerland.)
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 2002-04-01
Publisher Place United States
e-ISSN 1531298X
Journal THE PLANT CELL ONLINE
Volume Number 14
Issue Number 4


Source: WHO-Global Index Medicus