RustEffectorV1, Main, Exploration, bibRecord, 000028

Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.

Identifieur interne : 000028 ( Main/Exploration ); précédent : 000027; suivant : 000029

Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.

Auteurs : Li Wan [Australie, États-Unis] ; Markus Koeck [Australie] ; Simon J. Williams [Australie] ; Anthony R. Ashton [Australie] ; Gregory J. Lawrence [Australie] ; Hitoshi Sakakibara [Japon] ; Mikiko Kojima [Japon] ; Christine Böttcher [Australie] ; Daniel J. Ericsson [Australie] ; Adrienne R. Hardham [Australie] ; David A. Jones [Australie] ; Jeffrey G. Ellis [Australie] ; Bostjan Kobe [Australie] ; Peter N. Dodds [Australie]

Source :

Molecular plant pathology [ 1364-3703 ] ; 2019.

RBID : pubmed:30242946

Descripteurs français

KwdFr :
- Basidiomycota (génétique), Basidiomycota (métabolisme), Basidiomycota (pathogénicité), Liaison aux protéines (MeSH), Lin (microbiologie), Lin (métabolisme), Maladies des plantes (microbiologie), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Techniques de double hybride (MeSH).
MESH :
- génétique : Basidiomycota, Oxidoreductases, Protéines fongiques, Protéines végétales.
- microbiologie : Lin, Maladies des plantes.
- métabolisme : Basidiomycota, Lin, Oxidoreductases, Protéines fongiques, Protéines végétales.
- pathogénicité : Basidiomycota.
- Liaison aux protéines, Techniques de double hybride.

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

Affiliations:

Australie, Japon, États-Unis

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000043
to stream Main, to step Curation: 000043

Le document en format XML

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<author><name sortKey="Bottcher, Christine" sort="Bottcher, Christine" uniqKey="Bottcher C" first="Christine" last="Böttcher">Christine Böttcher</name>
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<country xml:lang="fr">Australie</country>
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<author><name sortKey="Ericsson, Daniel J" sort="Ericsson, Daniel J" uniqKey="Ericsson D" first="Daniel J" last="Ericsson">Daniel J. Ericsson</name>
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<author><name sortKey="Dodds, Peter N" sort="Dodds, Peter N" uniqKey="Dodds P" first="Peter N" last="Dodds">Peter N. Dodds</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (genetics)</term>
<term>Basidiomycota (metabolism)</term>
<term>Basidiomycota (pathogenicity)</term>
<term>Flax (metabolism)</term>
<term>Flax (microbiology)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Oxidoreductases (genetics)</term>
<term>Oxidoreductases (metabolism)</term>
<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>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (génétique)</term>
<term>Basidiomycota (métabolisme)</term>
<term>Basidiomycota (pathogénicité)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Lin (microbiologie)</term>
<term>Lin (métabolisme)</term>
<term>Maladies des plantes (microbiologie)</term>
<term>Oxidoreductases (génétique)</term>
<term>Oxidoreductases (métabolisme)</term>
<term>Protéines fongiques (génétique)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Techniques de double hybride (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Fungal Proteins</term>
<term>Oxidoreductases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Basidiomycota</term>
<term>Oxidoreductases</term>
<term>Protéines fongiques</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Basidiomycota</term>
<term>Flax</term>
<term>Fungal Proteins</term>
<term>Oxidoreductases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Lin</term>
<term>Maladies des plantes</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Flax</term>
<term>Plant Diseases</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Basidiomycota</term>
<term>Lin</term>
<term>Oxidoreductases</term>
<term>Protéines fongiques</term>
<term>Protéines végétales</term>
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<term>Two-Hybrid System Techniques</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>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30242946</PMID>
<DateCompleted><Year>2019</Year>
<Month>08</Month>
<Day>08</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>02</Month>
<Day>25</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1364-3703</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>20</Volume>
<Issue>2</Issue>
<PubDate><Year>2019</Year>
<Month>02</Month>
</PubDate>
</JournalIssue>
<Title>Molecular plant pathology</Title>
<ISOAbbreviation>Mol Plant Pathol</ISOAbbreviation>
</Journal>
<ArticleTitle>Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.</ArticleTitle>
<Pagination><MedlinePgn>211-222</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1111/mpp.12749</ELocationID>
<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>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wan</LastName>
<ForeName>Li</ForeName>
<Initials>L</Initials>
<Identifier Source="ORCID">0000-0002-0839-3748</Identifier>
<AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD, 4072, Australia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Biology, University of North Carolina, Chapel Hill, North Carolina, 27599-3280, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Koeck</LastName>
<ForeName>Markus</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Williams</LastName>
<ForeName>Simon J</ForeName>
<Initials>SJ</Initials>
<AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD, 4072, Australia.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Division of Plant Sciences, Research School of Biology, Australian National University, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ashton</LastName>
<ForeName>Anthony R</ForeName>
<Initials>AR</Initials>
<AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lawrence</LastName>
<ForeName>Gregory J</ForeName>
<Initials>GJ</Initials>
<AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sakakibara</LastName>
<ForeName>Hitoshi</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa, 230-0045, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kojima</LastName>
<ForeName>Mikiko</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>RIKEN Center for Sustainable Resource Science, Yokohama, Kanagawa, 230-0045, Japan.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Böttcher</LastName>
<ForeName>Christine</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organisation Agriculture and Food, Adelaide, SA, 5064, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ericsson</LastName>
<ForeName>Daniel J</ForeName>
<Initials>DJ</Initials>
<AffiliationInfo><Affiliation>Australian Synchrotron, Macromolecular Crystallography, Clayton, Victoria, 3168, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hardham</LastName>
<ForeName>Adrienne R</ForeName>
<Initials>AR</Initials>
<AffiliationInfo><Affiliation>Division of Plant Sciences, Research School of Biology, Australian National University, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jones</LastName>
<ForeName>David A</ForeName>
<Initials>DA</Initials>
<AffiliationInfo><Affiliation>Division of Plant Sciences, Research School of Biology, Australian National University, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ellis</LastName>
<ForeName>Jeffrey G</ForeName>
<Initials>JG</Initials>
<AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kobe</LastName>
<ForeName>Bostjan</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>School of Chemistry and Molecular Biosciences, Australian Infectious Diseases Research Centre and Institute for Molecular Bioscience, University of Queensland, Brisbane, QLD, 4072, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Dodds</LastName>
<ForeName>Peter N</ForeName>
<Initials>PN</Initials>
<AffiliationInfo><Affiliation>Commonwealth Scientific and Industrial Research Organisation Agriculture and Food, Canberra, ACT, 2601, Australia.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>11</Month>
<Day>15</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>Mol Plant Pathol</MedlineTA>
<NlmUniqueID>100954969</NlmUniqueID>
<ISSNLinking>1364-3703</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.-</RegistryNumber>
<NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance>
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<Chemical><RegistryNumber>EC 1.5.99.12</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019597" MajorTopicYN="N">Flax</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">crystal structure</Keyword>
<Keyword MajorTopicYN="Y">cytokinin</Keyword>
<Keyword MajorTopicYN="Y">cytokinin oxidase</Keyword>
<Keyword MajorTopicYN="Y">flax rust (Melampsora lini) effector</Keyword>
<Keyword MajorTopicYN="Y">pathogen virulence</Keyword>
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<country name="Japon"><noRegion><name sortKey="Sakakibara, Hitoshi" sort="Sakakibara, Hitoshi" uniqKey="Sakakibara H" first="Hitoshi" last="Sakakibara">Hitoshi Sakakibara</name>
</noRegion>
<name sortKey="Kojima, Mikiko" sort="Kojima, Mikiko" uniqKey="Kojima M" first="Mikiko" last="Kojima">Mikiko Kojima</name>
</country>
</tree>
</affiliations>
</record>

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HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000028 | SxmlIndent | more

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{{Explor lien
   |wiki=    Bois
   |area=    RustEffectorV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:30242946
   |texte=   Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.
}}

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	Serveur d'exploration sur les effecteurs de la rouille
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur les effecteurs de la rouille

Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.

Structural and functional insights into the modulation of the activity of a flax cytokinin oxidase by flax rust effector AvrL567-A.

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