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An anionic class III peroxidase from zucchini may regulate hypocotyl elongation through its auxin oxidase activity
Authors:Claudia Cosio  Loic Vuillemin  Mireille De Meyer  Claire Kevers  Claude Penel  Christophe Dunand
Affiliation:1.Laboratoire of Plant Biochemistry and Physiology,University of Geneva,Geneva 4,Switzerland;2.Unité de Biologie Moléculaire et Biotechnologie Végétales,Université de Liège,Liège,Belgium;3.Institut Forel,Université de Genève,Versoix,Switzerland;4.Plant Cell Surfaces and Signaling Laboratory,University of Toulouse, UPS, CNRS,Castanet-Tolosan,France
Abstract:The high number of peroxidase genes explains the description of numerous physiological functions and the fact that the in planta function of a single isoform has never been characterized yet. We analyzed in transgenic Arabidopsis thaliana the localization of a zucchini isoperoxidase (APRX), previously purified thanks to its pectin binding ability. We confirmed that the protein is localized near the cell wall, mainly produced in the elongation area of the hypocotyls and respond to exogenous auxin. In addition, the ectopic overexpression of APRX induced changes in growth pattern and a significant reduction of endogenous indole-3-acetic acid (IAA) level. In agreement with these observations APRX showed an elevated in vitro auxin oxidase activity. We propose that APRX participates in the negative feedback regulation of auxin level and consequently terminates the hypocotyl elongation process. Electronic supplementary material  The online version of this article (doi:) contains supplementary material, which is available to authorized users. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors () is: C. Dunand (dunand@scsv.ups-tlse.fr). The genomic and promoter nucleotide sequence of APRX has been submitted to GenBank under the accession number DQ518906.
Keywords:Auxin oxidase activity  Cell elongation  Cell wall  Pectin  Peroxidase
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