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Author Choudhury, Swarup Roy ♦ Pandey, Sona
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) 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 ♦ Enzymes and Coenzymes ♦ Amino Acids, Peptides, and Proteins ♦ Chemicals and Drugs ♦ Investigative Techniques ♦ Analytical, Diagnostic and Therapeutic Techniques and Equipment ♦ Chemical Phenomena ♦ Genetic Phenomena ♦ Plant Physiological Phenomena ♦ Biological Sciences
Subject Keyword Discipline Botany ♦ Gtp-binding Proteins ♦ Genetics ♦ Gene Expression Regulation, Plant ♦ Genes, Plant ♦ Plant Proteins ♦ Metabolism ♦ Root Nodules, Plant ♦ Growth & Development ♦ Soybeans ♦ Models, Biological ♦ Phosphorylation ♦ Plant Root Nodulation ♦ Plants, Genetically Modified ♦ Protein Binding ♦ Drug Effects ♦ Rgs Proteins ♦ Receptors, Cell Surface ♦ Journal Article ♦ Research Support, Non-u.s. Gov't
Abstract Signaling pathways mediated by heterotrimeric G-protein complexes comprising G , Gß, and Gγ subunits and their regulatory RGS (Regulator of G-protein Signaling) protein are conserved in all eukaryotes. We have shown that the specific Gß and Gγ proteins of a soybean (Glycine max) heterotrimeric G-protein complex are involved in regulation of nodulation. We now demonstrate the role of Nod factor receptor 1 (NFR1)-mediated phosphorylation in regulation of the G-protein cycle during nodulation in soybean. We also show that during nodulation, the G-protein cycle is regulated by the activity of RGS proteins. Lower or higher expression of RGS proteins results in fewer or more nodules, respectively. NFR1 interacts with RGS proteins and phosphorylates them. Analysis of phosphorylated RGS protein identifies specific amino acids that, when phosphorylated, result in significantly higher GTPase accelerating activity. These data point to phosphorylation-based regulation of G-protein signaling during nodule development. We propose that active NFR1 receptors phosphorylate and activate RGS proteins, which help maintain the G proteins in their inactive, trimeric conformation, resulting in successful nodule development. Alternatively, RGS proteins might also have a direct role in regulating nodulation because overexpression of their phospho-mimic version leads to partial restoration of nodule formation in nod49 mutants.
Description Author Affiliation: Choudhury SR ( Donald Danforth Plant Science Center, St. Louis, Missouri 63132.); Pandey S ( Donald Danforth Plant Science Center, St. Louis, Missouri 63132
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 2015-11-01
Publisher Place United States
e-ISSN 1531298X
Volume Number 27
Issue Number 11

Source: WHO-Global Index Medicus