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A 1-phytase type III effector interferes with plant hormone signaling.
Blüher, Doreen; Laha, Debabrata; Thieme, Sabine; Hofer, Alexandre; Eschen-Lippold, Lennart; Masch, Antonia; Balcke, Gerd; Pavlovic, Igor; Nagel, Oliver; Schonsky, Antje; Hinkelmann, Rahel; Wörner, Jakob; Parvin, Nargis; Greiner, Ralf; Weber, Stefan; Tissier, Alain; Schutkowski, Mike; Lee, Justin; Jessen, Henning; Schaaf, Gabriel; Bonas, Ulla.
Afiliação
  • Blüher D; Institute for Biology, Department of Genetics, Martin-Luther University Halle-Wittenberg, Weinbergweg 10, 06120, Halle (Saale), Germany.
  • Laha D; Institute of Crop Science and Resource Conservation, Department of Plant Nutrition, University of Bonn, Karlrobert-Kreiten-Strasse 13, 53115, Bonn, Germany.
  • Thieme S; Center for Plant Molecular Biology, Department of Plant Physiology, Eberhard Karls University Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany.
  • Hofer A; Institute for Biology, Department of Genetics, Martin-Luther University Halle-Wittenberg, Weinbergweg 10, 06120, Halle (Saale), Germany.
  • Eschen-Lippold L; Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland.
  • Masch A; Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120, Halle (Saale), Germany.
  • Balcke G; Institute for Biochemistry and Biotechnology, Department of Enzymology, Martin-Luther University Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120, Halle (Saale), Germany.
  • Pavlovic I; Department of Cell and Metabolic Biology, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120, Halle (Saale), Germany.
  • Nagel O; Institute of Organic Chemistry, Albert-Ludwigs University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany.
  • Schonsky A; Institute for Biology, Department of Genetics, Martin-Luther University Halle-Wittenberg, Weinbergweg 10, 06120, Halle (Saale), Germany.
  • Hinkelmann R; Institute for Biology, Department of Genetics, Martin-Luther University Halle-Wittenberg, Weinbergweg 10, 06120, Halle (Saale), Germany.
  • Wörner J; Institute of Organic Chemistry, Albert-Ludwigs University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany.
  • Parvin N; Institute of Physical Chemistry, Albert-Ludwigs University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany.
  • Greiner R; Center for Plant Molecular Biology, Department of Plant Physiology, Eberhard Karls University Tübingen, Auf der Morgenstelle 32, 72076, Tübingen, Germany.
  • Weber S; Department of Food Technology and Bioprocess Engineering, Max-Rubner-Institut, Federal Research Institute of Nutrition and Food, Haid-und-Neu-Straße 9, 76131, Karlsruhe, Germany.
  • Tissier A; Institute of Physical Chemistry, Albert-Ludwigs University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany.
  • Schutkowski M; Department of Cell and Metabolic Biology, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120, Halle (Saale), Germany.
  • Lee J; Institute for Biochemistry and Biotechnology, Department of Enzymology, Martin-Luther University Halle-Wittenberg, Kurt-Mothes-Strasse 3, 06120, Halle (Saale), Germany.
  • Jessen H; Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, Weinberg 3, 06120, Halle (Saale), Germany.
  • Schaaf G; Department of Chemistry, University of Zurich, Winterthurerstrasse 190, 8057, Zurich, Switzerland. henning.jessen@oc.uni-freiburg.de.
  • Bonas U; Institute of Organic Chemistry, Albert-Ludwigs University Freiburg, Albertstrasse 21, 79104, Freiburg, Germany. henning.jessen@oc.uni-freiburg.de.
Nat Commun ; 8(1): 2159, 2017 12 18.
Article em En | MEDLINE | ID: mdl-29255246
ABSTRACT
Most Gram-negative phytopathogenic bacteria inject type III effector (T3E) proteins into plant cells to manipulate signaling pathways to the pathogen's benefit. In resistant plants, specialized immune receptors recognize single T3Es or their biochemical activities, thus halting pathogen ingress. However, molecular function and mode of recognition for most T3Es remains elusive. Here, we show that the Xanthomonas T3E XopH possesses phytase activity, i.e., dephosphorylates phytate (myo-inositol-hexakisphosphate, InsP6), the major phosphate storage compound in plants, which is also involved in pathogen defense. A combination of biochemical approaches, including a new NMR-based method to discriminate inositol polyphosphate enantiomers, identifies XopH as a naturally occurring 1-phytase that dephosphorylates InsP6 at C1. Infection of Nicotiana benthamiana and pepper by Xanthomonas results in a XopH-dependent conversion of InsP6 to InsP5. 1-phytase activity is required for XopH-mediated immunity of plants carrying the Bs7 resistance gene, and for induction of jasmonate- and ethylene-responsive genes in N. benthamiana.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ácido Fítico / Proteínas de Bactérias / Xanthomonas campestris / 6-Fitase Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ácido Fítico / Proteínas de Bactérias / Xanthomonas campestris / 6-Fitase Idioma: En Ano de publicação: 2017 Tipo de documento: Article