Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.
Identifieur interne : 000024 ( PubMed/Corpus ); précédent : 000023; suivant : 000025Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.
Auteurs : Li Wan ; Markus Koeck ; Simon J. Williams ; Anthony R. Ashton ; Gregory J. Lawrence ; Hitoshi Sakakibara ; Mikiko Kojima ; Christine Böttcher ; Daniel J. Ericsson ; Adrienne R. Hardham ; David A. Jones ; Jeffrey G. Ellis ; Bostjan Kobe ; Peter N. DoddsSource :
- Molecular plant pathology [ 1364-3703 ] ; 2019.
English descriptors
- KwdEn :
- Basidiomycota (genetics), Basidiomycota (metabolism), Basidiomycota (pathogenicity), Flax (metabolism), Flax (microbiology), Fungal Proteins (genetics), Fungal Proteins (metabolism), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plant Diseases (microbiology), Plant Proteins (genetics), Plant Proteins (metabolism), Protein Binding (MeSH), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , genetics : Fungal Proteins, Oxidoreductases, Plant Proteins.
- genetics : Basidiomycota.
- metabolism : Basidiomycota, Flax, Fungal Proteins, Oxidoreductases, Plant Proteins.
- microbiology : Flax, Plant Diseases.
- pathogenicity : Basidiomycota.
- Protein Binding, Two-Hybrid System Techniques.
Abstract
During infection, plant pathogens secrete effector proteins to facilitate colonization. In comparison with our knowledge of bacterial effectors, the current understanding of how fungal effectors function is limited. In this study, we show that the effector AvrL567-A from the flax rust fungus Melampsora lini interacts with a flax cytosolic cytokinin oxidase, LuCKX1.1, using both yeast two-hybrid and in planta bimolecular fluorescence assays. Purified LuCKX1.1 protein shows catalytic activity against both N6-(Δ2-isopentenyl)-adenine (2iP) and trans-zeatin (tZ) substrates. Incubation of LuCKX1.1 with AvrL567-A results in increased catalytic activity against both substrates. The crystal structure of LuCKX1.1 and docking studies with AvrL567-A indicate that the AvrL567 binding site involves a flexible surface-exposed region that surrounds the cytokinin substrate access site, which may explain its effect in modulating LuCKX1.1 activity. Expression of AvrL567-A in transgenic flax plants gave rise to an epinastic leaf phenotype consistent with hormonal effects, although no difference in overall cytokinin levels was observed. We propose that, during infection, plant pathogens may differentially modify the levels of extracellular and intracellular cytokinins.
DOI: 10.1111/mpp.12749
PubMed: 30242946
PubMed Central: PMC6637871
Links to Exploration step
pubmed:30242946Le document en format XML
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<term>Flax (microbiology)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
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<term>Plant Diseases (microbiology)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Two-Hybrid System Techniques (MeSH)</term>
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<term>Oxidoreductases</term>
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<front><div type="abstract" xml:lang="en">During infection, plant pathogens secrete effector proteins to facilitate colonization. In comparison with our knowledge of bacterial effectors, the current understanding of how fungal effectors function is limited. In this study, we show that the effector AvrL567-A from the flax rust fungus Melampsora lini interacts with a flax cytosolic cytokinin oxidase, LuCKX1.1, using both yeast two-hybrid and in planta bimolecular fluorescence assays. Purified LuCKX1.1 protein shows catalytic activity against both N6-(Δ2-isopentenyl)-adenine (2iP) and trans-zeatin (tZ) substrates. Incubation of LuCKX1.1 with AvrL567-A results in increased catalytic activity against both substrates. The crystal structure of LuCKX1.1 and docking studies with AvrL567-A indicate that the AvrL567 binding site involves a flexible surface-exposed region that surrounds the cytokinin substrate access site, which may explain its effect in modulating LuCKX1.1 activity. Expression of AvrL567-A in transgenic flax plants gave rise to an epinastic leaf phenotype consistent with hormonal effects, although no difference in overall cytokinin levels was observed. We propose that, during infection, plant pathogens may differentially modify the levels of extracellular and intracellular cytokinins.</div>
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<Abstract><AbstractText>During infection, plant pathogens secrete effector proteins to facilitate colonization. In comparison with our knowledge of bacterial effectors, the current understanding of how fungal effectors function is limited. In this study, we show that the effector AvrL567-A from the flax rust fungus Melampsora lini interacts with a flax cytosolic cytokinin oxidase, LuCKX1.1, using both yeast two-hybrid and in planta bimolecular fluorescence assays. Purified LuCKX1.1 protein shows catalytic activity against both N6-(Δ2-isopentenyl)-adenine (2iP) and trans-zeatin (tZ) substrates. Incubation of LuCKX1.1 with AvrL567-A results in increased catalytic activity against both substrates. The crystal structure of LuCKX1.1 and docking studies with AvrL567-A indicate that the AvrL567 binding site involves a flexible surface-exposed region that surrounds the cytokinin substrate access site, which may explain its effect in modulating LuCKX1.1 activity. Expression of AvrL567-A in transgenic flax plants gave rise to an epinastic leaf phenotype consistent with hormonal effects, although no difference in overall cytokinin levels was observed. We propose that, during infection, plant pathogens may differentially modify the levels of extracellular and intracellular cytokinins.</AbstractText>
<CopyrightInformation>© 2018 The Authors. Molecular Plant Pathology published by BSPP and John Wiley & Sons Ltd.</CopyrightInformation>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Biology, University of North Carolina, Chapel Hill, North Carolina, 27599-3280, USA.</Affiliation>
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