Identification of Arabidopsis VTC3 as a putative and unique dual function protein kinase::protein phosphatase involved in the regulation of the ascorbic acid pool in plants

Ascorbic acid (AsA) is present at high levels in plants and is a potent antioxidant and cellular reductant. The major plant AsA biosynthetic pathway is through the intermediates D-mannose and L-galactose. Although there is ample evidence that plants respond to fluctuating environmental conditions wi...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 64(2013), 10 vom: 15. Juli, Seite 2793-804
1. Verfasser: Conklin, Patricia L (VerfasserIn)
Weitere Verfasser: DePaolo, Dennis, Wintle, Brittie, Schatz, Carmit, Buckenmeyer, Gail
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Antioxidant Arabidopsis Smirnoff–Wheeler. ascorbic acid biosynthesis kinase phosphatase mehr... vtc3 Arabidopsis Proteins Protein Kinases EC 2.7.- Phosphoprotein Phosphatases EC 3.1.3.16 Protein Phosphatase 2C VTC3 protein, Arabidopsis Ascorbic Acid PQ6CK8PD0R
Beschreibung
Zusammenfassung:Ascorbic acid (AsA) is present at high levels in plants and is a potent antioxidant and cellular reductant. The major plant AsA biosynthetic pathway is through the intermediates D-mannose and L-galactose. Although there is ample evidence that plants respond to fluctuating environmental conditions with changes in the pool size of AsA, it is unclear how this regulation occurs. The AsA-deficient Arabidopsis thaliana mutants vtc3-1 and vtc3-2 define a locus that has been identified by positional cloning as At2g40860. Confirmation of this identification was through the study of AsA-deficient At2g40860 insertion mutants and by transgenic complementation of the AsA deficiency in vtc3-1 and vtc3-2 with wild-type At2g40860 cDNA. The very unusual VTC3 gene is predicted to encode a novel polypeptide with an N-terminal protein kinase domain tethered covalently to a C-terminal protein phosphatase type 2C domain. Homologues of this gene exist only within the Viridiplantae/Chloroplastida and the gene may therefore have arisen along with the D-mannose/L-galactose AsA biosynthetic pathway. The vtc3 mutant plants are defective in the ability to elevate the AsA pool in response to light and heat, suggestive of an important role for VTC3 in the regulation of the AsA pool size
Beschreibung:Date Completed 21.01.2014
Date Revised 25.11.2016
published: Print-Electronic
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/ert140