Structural Requirements of the Phytoplasma Effector Protein SAP54 for Causing Homeotic Transformation of Floral Organs.
Identifieur interne : 000044 ( Main/Exploration ); précédent : 000043; suivant : 000045Structural Requirements of the Phytoplasma Effector Protein SAP54 for Causing Homeotic Transformation of Floral Organs.
Auteurs : Marc-Benjamin Aurin [Allemagne] ; Michael Haupt [Allemagne] ; Matthias Görlach [Allemagne] ; Florian Rümpler [Allemagne] ; Günter Thei En [Allemagne]Source :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
- composition chimique : Protéines bactériennes.
- génétique : Phytoplasma, Protéines bactériennes.
- microbiologie : Fleurs, Maladies des plantes.
- Plantes, Relation structure-activité, Structure secondaire des protéines.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Bacterial Proteins.
- chemical , genetics : Bacterial Proteins.
- genetics : Phytoplasma.
- microbiology : Flowers, Plant Diseases.
- Plants, Protein Structure, Secondary, Structure-Activity Relationship.
Abstract
Phytoplasmas are intracellular bacterial plant pathogens that cause devastating diseases in crops and ornamental plants by the secretion of effector proteins. One of these effector proteins, termed SECRETED ASTER YELLOWS WITCHES' BROOM PROTEIN 54 (SAP54), leads to the degradation of a specific subset of floral homeotic proteins of the MIKC-type MADS-domain family via the ubiquitin-proteasome pathway. In consequence, the developing flowers show the homeotic transformation of floral organs into vegetative leaf-like structures. The molecular mechanism of SAP54 action involves binding to the keratin-like domain of MIKC-type proteins and to some RAD23 proteins, which translocate ubiquitylated substrates to the proteasome. The structural requirements and specificity of SAP54 function are poorly understood, however. Here, we report, based on biophysical and molecular biological analyses, that SAP54 folds into an α-helical structure. Insertion of helix-breaking mutations disrupts correct folding of SAP54 and compromises SAP54 binding to its target proteins and, concomitantly, its ability to evoke disease phenotypes in vivo. Interestingly, dynamic light scattering data together with electrophoretic mobility shift assays suggest that SAP54 preferentially binds to multimeric complexes of MIKC-type proteins rather than to dimers or monomers of these proteins. Together with data from literature, this finding suggests that MIKC-type proteins and SAP54 constitute multimeric α-helical coiled coils. Our investigations clarify the structure-function relationship of an important phytoplasma effector protein and may thus ultimately help to develop treatments against some devastating plant diseases.
DOI: 10.1094/MPMI-02-20-0028-R
PubMed: 32689871
Affiliations:
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Fritz Lipmann Institute, Beutenbergstr. 11, 07745 Jena, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Leibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, 07745 Jena</wicri:regionArea><wicri:noRegion>07745 Jena</wicri:noRegion><wicri:noRegion>07745 Jena</wicri:noRegion><wicri:noRegion>07745 Jena</wicri:noRegion></affiliation></author><author><name sortKey="Rumpler, Florian" sort="Rumpler, Florian" uniqKey="Rumpler F" first="Florian" last="Rümpler">Florian Rümpler</name><affiliation wicri:level="1"><nlm:affiliation>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena</wicri:regionArea><wicri:noRegion>07743 Jena</wicri:noRegion><wicri:noRegion>07743 Jena</wicri:noRegion><wicri:noRegion>07743 Jena</wicri:noRegion></affiliation></author><author><name sortKey="Thei En, Gunter" sort="Thei En, Gunter" uniqKey="Thei En G" first="Günter" last="Thei En">Günter Thei En</name><affiliation wicri:level="1"><nlm:affiliation>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena</wicri:regionArea><wicri:noRegion>07743 Jena</wicri:noRegion><wicri:noRegion>07743 Jena</wicri:noRegion><wicri:noRegion>07743 Jena</wicri:noRegion></affiliation></author></analytic><series><title level="j">Molecular plant-microbe interactions : MPMI</title><idno type="ISSN">0894-0282</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (genetics)</term><term>Flowers (microbiology)</term><term>Phytoplasma (genetics)</term><term>Plant Diseases (microbiology)</term><term>Plants (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Structure-Activity Relationship (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Fleurs (microbiologie)</term><term>Maladies des plantes (microbiologie)</term><term>Phytoplasma (génétique)</term><term>Plantes (MeSH)</term><term>Protéines bactériennes (composition chimique)</term><term>Protéines bactériennes (génétique)</term><term>Relation structure-activité (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phytoplasma</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Phytoplasma</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Fleurs</term><term>Maladies des plantes</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Flowers</term><term>Plant Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Plants</term><term>Protein Structure, Secondary</term><term>Structure-Activity Relationship</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Plantes</term><term>Relation structure-activité</term><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Phytoplasmas are intracellular bacterial plant pathogens that cause devastating diseases in crops and ornamental plants by the secretion of effector proteins. One of these effector proteins, termed SECRETED ASTER YELLOWS WITCHES' BROOM PROTEIN 54 (SAP54), leads to the degradation of a specific subset of floral homeotic proteins of the MIKC-type MADS-domain family via the ubiquitin-proteasome pathway. In consequence, the developing flowers show the homeotic transformation of floral organs into vegetative leaf-like structures. The molecular mechanism of SAP54 action involves binding to the keratin-like domain of MIKC-type proteins and to some RAD23 proteins, which translocate ubiquitylated substrates to the proteasome. The structural requirements and specificity of SAP54 function are poorly understood, however. Here, we report, based on biophysical and molecular biological analyses, that SAP54 folds into an α-helical structure. Insertion of helix-breaking mutations disrupts correct folding of SAP54 and compromises SAP54 binding to its target proteins and, concomitantly, its ability to evoke disease phenotypes in vivo. Interestingly, dynamic light scattering data together with electrophoretic mobility shift assays suggest that SAP54 preferentially binds to multimeric complexes of MIKC-type proteins rather than to dimers or monomers of these proteins. Together with data from literature, this finding suggests that MIKC-type proteins and SAP54 constitute multimeric α-helical coiled coils. Our investigations clarify the structure-function relationship of an important phytoplasma effector protein and may thus ultimately help to develop treatments against some devastating plant diseases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">32689871</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0894-0282</ISSN><JournalIssue CitedMedium="Print"><Volume>33</Volume><Issue>9</Issue><PubDate><Year>2020</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Molecular plant-microbe interactions : MPMI</Title><ISOAbbreviation>Mol Plant Microbe Interact</ISOAbbreviation></Journal><ArticleTitle>Structural Requirements of the Phytoplasma Effector Protein SAP54 for Causing Homeotic Transformation of Floral Organs.</ArticleTitle><Pagination><MedlinePgn>1129-1141</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1094/MPMI-02-20-0028-R</ELocationID><Abstract><AbstractText>Phytoplasmas are intracellular bacterial plant pathogens that cause devastating diseases in crops and ornamental plants by the secretion of effector proteins. One of these effector proteins, termed SECRETED ASTER YELLOWS WITCHES' BROOM PROTEIN 54 (SAP54), leads to the degradation of a specific subset of floral homeotic proteins of the MIKC-type MADS-domain family via the ubiquitin-proteasome pathway. In consequence, the developing flowers show the homeotic transformation of floral organs into vegetative leaf-like structures. The molecular mechanism of SAP54 action involves binding to the keratin-like domain of MIKC-type proteins and to some RAD23 proteins, which translocate ubiquitylated substrates to the proteasome. The structural requirements and specificity of SAP54 function are poorly understood, however. Here, we report, based on biophysical and molecular biological analyses, that SAP54 folds into an α-helical structure. Insertion of helix-breaking mutations disrupts correct folding of SAP54 and compromises SAP54 binding to its target proteins and, concomitantly, its ability to evoke disease phenotypes in vivo. Interestingly, dynamic light scattering data together with electrophoretic mobility shift assays suggest that SAP54 preferentially binds to multimeric complexes of MIKC-type proteins rather than to dimers or monomers of these proteins. Together with data from literature, this finding suggests that MIKC-type proteins and SAP54 constitute multimeric α-helical coiled coils. Our investigations clarify the structure-function relationship of an important phytoplasma effector protein and may thus ultimately help to develop treatments against some devastating plant diseases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aurin</LastName><ForeName>Marc-Benjamin</ForeName><Initials>MB</Initials><AffiliationInfo><Affiliation>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Haupt</LastName><ForeName>Michael</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Görlach</LastName><ForeName>Matthias</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Leibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, 07745 Jena, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rümpler</LastName><ForeName>Florian</ForeName><Initials>F</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-4986-2595</Identifier><AffiliationInfo><Affiliation>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Theißen</LastName><ForeName>Günter</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Matthias Schleiden Institute / Genetics, Friedrich Schiller University Jena, Philosophenweg 12, 07743 Jena, Germany.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>07</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Plant Microbe Interact</MedlineTA><NlmUniqueID>9107902</NlmUniqueID><ISSNLinking>0894-0282</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D035264" MajorTopicYN="N">Flowers</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045582" MajorTopicYN="N">Phytoplasma</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010944" MajorTopicYN="N">Plants</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013329" MajorTopicYN="N">Structure-Activity Relationship</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">MADS-box gene</Keyword><Keyword MajorTopicYN="N">keratin-like domain</Keyword><Keyword MajorTopicYN="N">phyllody</Keyword><Keyword MajorTopicYN="N">phyllogen</Keyword><Keyword MajorTopicYN="N">α-helical coiled coils</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>11</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32689871</ArticleId><ArticleId IdType="doi">10.1094/MPMI-02-20-0028-R</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Aurin, Marc Benjamin" sort="Aurin, Marc Benjamin" uniqKey="Aurin M" first="Marc-Benjamin" last="Aurin">Marc-Benjamin Aurin</name></noRegion><name sortKey="Gorlach, Matthias" sort="Gorlach, Matthias" uniqKey="Gorlach M" first="Matthias" last="Görlach">Matthias Görlach</name><name sortKey="Haupt, Michael" sort="Haupt, Michael" uniqKey="Haupt M" first="Michael" last="Haupt">Michael Haupt</name><name sortKey="Rumpler, Florian" sort="Rumpler, Florian" uniqKey="Rumpler F" first="Florian" last="Rümpler">Florian Rümpler</name><name sortKey="Thei En, Gunter" sort="Thei En, Gunter" uniqKey="Thei En G" first="Günter" last="Thei En">Günter Thei En</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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