Differential activities of maize Plant Elicitor Peptides as mediators of immune signaling and herbivore resistance.
Identifieur interne : 000027 ( Main/Corpus ); précédent : 000026; suivant : 000028Differential activities of maize Plant Elicitor Peptides as mediators of immune signaling and herbivore resistance.
Auteurs : Elly Poretsky ; Keini Dressano ; Philipp Weckwerth ; Miguel Ruiz ; Si Nian Char ; Shi Da ; Ruben Abagyan ; Bing Yang ; Alisa HuffakerSource :
- The Plant journal : for cell and molecular biology [ 1365-313X ] ; 2020.
Abstract
Plant Elicitor Peptides (Peps) are conserved regulators of defense responses and models for the study of Damage-Associated Molecular Pattern (DAMP)-induced immunity. Although present as multigene families in most species, the functional relevance of these multigene families remains largely undefined. While Arabidopsis Peps appear largely redundant in function, previous work examining Pep-induced responses in maize implied specificity of function. To better define function of individual ZmPeps and their cognate ZmPEPR receptors, activities were examined by assessing changes in defense-associated phytohormones, specialized metabolites and global gene expression patterns, in combination with heterologous expression assays and analyses of CRISPR/Cas9-generated knockout plants. Beyond simply delineating individual ZmPep and ZmPEPR activities, these experiments led to a number of new insights into Pep signaling mechanisms. ZmPROPEP and other Poaceous precursors were found to contain multiple active Peps, a phenomenon not previously observed for this family. In all, seven new ZmPeps were identified and the peptides were found to have specific activities defined by relative magnitude of response output rather than by uniqueness. A striking correlation between individual ZmPep-elicited changes in levels of jasmonic acid and ethylene and the magnitude of induced defense responses was observed, indicating that collectively ZmPeps may regulate immune output through rheostat-like tuning of phytohormone levels. Peptide structure-function studies and ligand-receptor modeling revealed structural features critical to ZmPep function and led to identification of ZmPep5a as a potential antagonist peptide able to competitively inhibit activity of other ZmPeps, a regulatory mechanism not previously observed for this family.
DOI: 10.1111/tpj.15022
PubMed: 33058410
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USA.</nlm:affiliation></affiliation></author><author><name sortKey="Ruiz, Miguel" sort="Ruiz, Miguel" uniqKey="Ruiz M" first="Miguel" last="Ruiz">Miguel Ruiz</name><affiliation><nlm:affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Char, Si Nian" sort="Char, Si Nian" uniqKey="Char S" first="Si Nian" last="Char">Si Nian Char</name><affiliation><nlm:affiliation>Division of Plant Sciences, Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Da, Shi" sort="Da, Shi" uniqKey="Da S" first="Shi" last="Da">Shi Da</name><affiliation><nlm:affiliation>Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Abagyan, Ruben" sort="Abagyan, Ruben" uniqKey="Abagyan R" first="Ruben" last="Abagyan">Ruben 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first="Philipp" last="Weckwerth">Philipp Weckwerth</name><affiliation><nlm:affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Ruiz, Miguel" sort="Ruiz, Miguel" uniqKey="Ruiz M" first="Miguel" last="Ruiz">Miguel Ruiz</name><affiliation><nlm:affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Char, Si Nian" sort="Char, Si Nian" uniqKey="Char S" first="Si Nian" last="Char">Si Nian Char</name><affiliation><nlm:affiliation>Division of Plant Sciences, Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Da, Shi" sort="Da, Shi" uniqKey="Da S" first="Shi" last="Da">Shi Da</name><affiliation><nlm:affiliation>Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Abagyan, Ruben" sort="Abagyan, Ruben" uniqKey="Abagyan R" first="Ruben" last="Abagyan">Ruben Abagyan</name><affiliation><nlm:affiliation>Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Bing" sort="Yang, Bing" uniqKey="Yang B" first="Bing" last="Yang">Bing Yang</name><affiliation><nlm:affiliation>Division of Plant Sciences, Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Huffaker, Alisa" sort="Huffaker, Alisa" uniqKey="Huffaker A" first="Alisa" last="Huffaker">Alisa Huffaker</name><affiliation><nlm:affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The Plant journal : for cell and molecular biology</title><idno type="eISSN">1365-313X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant Elicitor Peptides (Peps) are conserved regulators of defense responses and models for the study of Damage-Associated Molecular Pattern (DAMP)-induced immunity. Although present as multigene families in most species, the functional relevance of these multigene families remains largely undefined. While Arabidopsis Peps appear largely redundant in function, previous work examining Pep-induced responses in maize implied specificity of function. To better define function of individual ZmPeps and their cognate ZmPEPR receptors, activities were examined by assessing changes in defense-associated phytohormones, specialized metabolites and global gene expression patterns, in combination with heterologous expression assays and analyses of CRISPR/Cas9-generated knockout plants. Beyond simply delineating individual ZmPep and ZmPEPR activities, these experiments led to a number of new insights into Pep signaling mechanisms. ZmPROPEP and other Poaceous precursors were found to contain multiple active Peps, a phenomenon not previously observed for this family. In all, seven new ZmPeps were identified and the peptides were found to have specific activities defined by relative magnitude of response output rather than by uniqueness. A striking correlation between individual ZmPep-elicited changes in levels of jasmonic acid and ethylene and the magnitude of induced defense responses was observed, indicating that collectively ZmPeps may regulate immune output through rheostat-like tuning of phytohormone levels. Peptide structure-function studies and ligand-receptor modeling revealed structural features critical to ZmPep function and led to identification of ZmPep5a as a potential antagonist peptide able to competitively inhibit activity of other ZmPeps, a regulatory mechanism not previously observed for this family.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33058410</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-313X</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>15</Day></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>Differential activities of maize Plant Elicitor Peptides as mediators of immune signaling and herbivore resistance.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/tpj.15022</ELocationID><Abstract><AbstractText>Plant Elicitor Peptides (Peps) are conserved regulators of defense responses and models for the study of Damage-Associated Molecular Pattern (DAMP)-induced immunity. Although present as multigene families in most species, the functional relevance of these multigene families remains largely undefined. While Arabidopsis Peps appear largely redundant in function, previous work examining Pep-induced responses in maize implied specificity of function. To better define function of individual ZmPeps and their cognate ZmPEPR receptors, activities were examined by assessing changes in defense-associated phytohormones, specialized metabolites and global gene expression patterns, in combination with heterologous expression assays and analyses of CRISPR/Cas9-generated knockout plants. Beyond simply delineating individual ZmPep and ZmPEPR activities, these experiments led to a number of new insights into Pep signaling mechanisms. ZmPROPEP and other Poaceous precursors were found to contain multiple active Peps, a phenomenon not previously observed for this family. In all, seven new ZmPeps were identified and the peptides were found to have specific activities defined by relative magnitude of response output rather than by uniqueness. A striking correlation between individual ZmPep-elicited changes in levels of jasmonic acid and ethylene and the magnitude of induced defense responses was observed, indicating that collectively ZmPeps may regulate immune output through rheostat-like tuning of phytohormone levels. Peptide structure-function studies and ligand-receptor modeling revealed structural features critical to ZmPep function and led to identification of ZmPep5a as a potential antagonist peptide able to competitively inhibit activity of other ZmPeps, a regulatory mechanism not previously observed for this family.</AbstractText><CopyrightInformation>This article is protected by copyright. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Poretsky</LastName><ForeName>Elly</ForeName><Initials>E</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-6116-6827</Identifier><AffiliationInfo><Affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dressano</LastName><ForeName>Keini</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Weckwerth</LastName><ForeName>Philipp</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruiz</LastName><ForeName>Miguel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Char</LastName><ForeName>Si Nian</ForeName><Initials>SN</Initials><AffiliationInfo><Affiliation>Division of Plant Sciences, Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Da</LastName><ForeName>Shi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Abagyan</LastName><ForeName>Ruben</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Bing</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Division of Plant Sciences, Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Huffaker</LastName><ForeName>Alisa</ForeName><Initials>A</Initials><Identifier Source="ORCID">https://orcid.org/0000-0002-3886-8433</Identifier><AffiliationInfo><Affiliation>Division of Biology, University of California San Diego, La Jolla, CA, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>10</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant J</MedlineTA><NlmUniqueID>9207397</NlmUniqueID><ISSNLinking>0960-7412</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Zea mays
</Keyword><Keyword MajorTopicYN="N">Peptide signalling</Keyword><Keyword MajorTopicYN="N">Plant-herbivore interactions</Keyword><Keyword MajorTopicYN="N">Protein-protein interactions</Keyword><Keyword MajorTopicYN="N">Signalling and hormones</Keyword><Keyword MajorTopicYN="N">Transcriptional response</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>10</Month><Day>15</Day><Hour>17</Hour><Minute>45</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>10</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33058410</ArticleId><ArticleId IdType="doi">10.1111/tpj.15022</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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