Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Nat Commun ; 8(1): 2159, 2017 12 18.
Article in English | 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.


Subject(s)
6-Phytase/metabolism , Bacterial Proteins/metabolism , Phytic Acid/metabolism , Xanthomonas campestris/metabolism , 6-Phytase/genetics , Amino Acid Sequence , Bacterial Proteins/genetics , Bacterial Secretion Systems/genetics , Bacterial Secretion Systems/metabolism , Biocatalysis , Disease Resistance/genetics , Inositol Phosphates/metabolism , Kinetics , Phosphorylation , Plant Cells/metabolism , Plant Cells/microbiology , Plant Diseases/genetics , Plant Diseases/microbiology , Sequence Homology, Amino Acid , Substrate Specificity , Xanthomonas campestris/genetics , Xanthomonas campestris/physiology
SELECTION OF CITATIONS
SEARCH DETAIL
...