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The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface‐exposed residue
Summary Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment....
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| Published in: | The New phytologist 2022-04, Vol.234 (2), p.592-606 |
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| creator | Ortiz, Diana Chen, Jian Outram, Megan A. Saur, Isabel M.L. Upadhyaya, Narayana M. Mago, Rohit Ericsson, Daniel J. Cesari, Stella Chen, Chunhong Williams, Simon J. Dodds, Peter N. |
| description | Summary
Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment.
Here we examined the role of genetic diversity of the stem rust (Puccinia graminis f. sp. tritici (Pgt)) AvrSr50 gene in determining recognition by the corresponding wheat Sr50 resistance gene. We solved the crystal structure of a natural variant of AvrSr50 and used site‐directed mutagenesis and transient expression assays to dissect the molecular mechanisms explaining gain of virulence.
We report that AvrSr50 can escape recognition by Sr50 through different mechanisms including DNA insertion, stop codon loss or by amino‐acid variation involving a single substitution of the AvrSr50 surface‐exposed residue Q121. We also report structural homology of AvrSr50 to cupin superfamily members and carbohydrate‐binding modules indicating a potential role in binding sugar moieties.
This study identifies key polymorphic sites present in AvrSr50 alleles from natural stem rust populations that play important roles to escape from Sr50 recognition. This constitutes an important step to better understand Pgt effector evolution and to monitor AvrSr50 variants in natural rust populations. |
| doi_str_mv | 10.1111/nph.18011 |
| format | article |
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Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment.
Here we examined the role of genetic diversity of the stem rust (Puccinia graminis f. sp. tritici (Pgt)) AvrSr50 gene in determining recognition by the corresponding wheat Sr50 resistance gene. We solved the crystal structure of a natural variant of AvrSr50 and used site‐directed mutagenesis and transient expression assays to dissect the molecular mechanisms explaining gain of virulence.
We report that AvrSr50 can escape recognition by Sr50 through different mechanisms including DNA insertion, stop codon loss or by amino‐acid variation involving a single substitution of the AvrSr50 surface‐exposed residue Q121. We also report structural homology of AvrSr50 to cupin superfamily members and carbohydrate‐binding modules indicating a potential role in binding sugar moieties.
This study identifies key polymorphic sites present in AvrSr50 alleles from natural stem rust populations that play important roles to escape from Sr50 recognition. This constitutes an important step to better understand Pgt effector evolution and to monitor AvrSr50 variants in natural rust populations.</description><identifier>ISSN: 0028-646X</identifier><identifier>EISSN: 1469-8137</identifier><identifier>DOI: 10.1111/nph.18011</identifier><identifier>PMID: 35107838</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Alleles ; AvrSr50 ; Basidiomycota - physiology ; Binding ; Breeding ; Carbohydrates ; Colonization ; Crystal structure ; Deoxyribonucleic acid ; Disease Resistance - genetics ; DNA ; effector evolution ; effector structure ; Evolution ; Genetic diversity ; Genetic variation ; Homology ; Insertion ; Life Sciences ; Molecular modelling ; Mutagenesis ; Pathogens ; Phytopathology and phytopharmacy ; Plant Breeding ; Plant Diseases - genetics ; Plant resistance ; Population genetics ; Populations ; Proteins ; Recognition ; Residues ; resistance breakdown ; Saccharides ; Site-directed mutagenesis ; Sr50 ; Stem rust ; Stems ; Stop codon ; Substitutes ; Triticum - genetics ; Vegetal Biology ; Virulence ; wheat resistance</subject><ispartof>The New phytologist, 2022-04, Vol.234 (2), p.592-606</ispartof><rights>2022 The Authors © 2022 New Phytologist Foundation</rights><rights>2022 The Authors New Phytologist © 2022 New Phytologist Foundation.</rights><rights>2022. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Attribution - NonCommercial - NoDerivatives</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4771-f6857ca97453354a9d426802fb2dfe1b6c2d15b27b3f2aacf6d9667331de0e973</citedby><cites>FETCH-LOGICAL-c4771-f6857ca97453354a9d426802fb2dfe1b6c2d15b27b3f2aacf6d9667331de0e973</cites><orcidid>0000-0002-5610-1260 ; 0000-0003-0620-5923 ; 0000-0001-8670-6984 ; 0000-0001-5101-9244 ; 0000-0001-7813-2415 ; 0000-0003-4510-3575 ; 0000-0003-4781-6261 ; 0000-0001-8558-0371 ; 0000-0001-6120-5788 ; 0000-0001-5286-073X ; 0000-0002-3052-0416 ; 0000-0002-3088-4738</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fnph.18011$$EPDF$$P50$$Gwiley$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fnph.18011$$EHTML$$P50$$Gwiley$$Hfree_for_read</linktohtml><link.rule.ids>230,315,786,790,891,27957,27958,50923,51032</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35107838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.inrae.fr/hal-03610628$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Ortiz, Diana</creatorcontrib><creatorcontrib>Chen, Jian</creatorcontrib><creatorcontrib>Outram, Megan A.</creatorcontrib><creatorcontrib>Saur, Isabel M.L.</creatorcontrib><creatorcontrib>Upadhyaya, Narayana M.</creatorcontrib><creatorcontrib>Mago, Rohit</creatorcontrib><creatorcontrib>Ericsson, Daniel J.</creatorcontrib><creatorcontrib>Cesari, Stella</creatorcontrib><creatorcontrib>Chen, Chunhong</creatorcontrib><creatorcontrib>Williams, Simon J.</creatorcontrib><creatorcontrib>Dodds, Peter N.</creatorcontrib><title>The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface‐exposed residue</title><title>The New phytologist</title><addtitle>New Phytol</addtitle><description>Summary
Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment.
Here we examined the role of genetic diversity of the stem rust (Puccinia graminis f. sp. tritici (Pgt)) AvrSr50 gene in determining recognition by the corresponding wheat Sr50 resistance gene. We solved the crystal structure of a natural variant of AvrSr50 and used site‐directed mutagenesis and transient expression assays to dissect the molecular mechanisms explaining gain of virulence.
We report that AvrSr50 can escape recognition by Sr50 through different mechanisms including DNA insertion, stop codon loss or by amino‐acid variation involving a single substitution of the AvrSr50 surface‐exposed residue Q121. We also report structural homology of AvrSr50 to cupin superfamily members and carbohydrate‐binding modules indicating a potential role in binding sugar moieties.
This study identifies key polymorphic sites present in AvrSr50 alleles from natural stem rust populations that play important roles to escape from Sr50 recognition. This constitutes an important step to better understand Pgt effector evolution and to monitor AvrSr50 variants in natural rust populations.</description><subject>Alleles</subject><subject>AvrSr50</subject><subject>Basidiomycota - physiology</subject><subject>Binding</subject><subject>Breeding</subject><subject>Carbohydrates</subject><subject>Colonization</subject><subject>Crystal structure</subject><subject>Deoxyribonucleic acid</subject><subject>Disease Resistance - genetics</subject><subject>DNA</subject><subject>effector evolution</subject><subject>effector structure</subject><subject>Evolution</subject><subject>Genetic diversity</subject><subject>Genetic variation</subject><subject>Homology</subject><subject>Insertion</subject><subject>Life Sciences</subject><subject>Molecular modelling</subject><subject>Mutagenesis</subject><subject>Pathogens</subject><subject>Phytopathology and phytopharmacy</subject><subject>Plant Breeding</subject><subject>Plant Diseases - genetics</subject><subject>Plant resistance</subject><subject>Population genetics</subject><subject>Populations</subject><subject>Proteins</subject><subject>Recognition</subject><subject>Residues</subject><subject>resistance breakdown</subject><subject>Saccharides</subject><subject>Site-directed mutagenesis</subject><subject>Sr50</subject><subject>Stem rust</subject><subject>Stems</subject><subject>Stop codon</subject><subject>Substitutes</subject><subject>Triticum - genetics</subject><subject>Vegetal Biology</subject><subject>Virulence</subject><subject>wheat resistance</subject><issn>0028-646X</issn><issn>1469-8137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><recordid>eNp1kc9uEzEQxi1ERdPAgRdAlrjQw7b-s-vdvSBFFRCkqK1EkbhZXu84cbVZL_Y6JTcegWfkSXCSUpVK-GBrxr_5xuMPodeUnNG0zvthdUYrQukzNKG5qLOK8vI5mhDCqkzk4tsxOgnhlhBSF4K9QMe8oKSseDVBdzcrwGGENfYxjBiMAT06jwfvRrA9nm38F18QDEGrAQLeBx60W_Z2tK7HzRYrHGITRjvGfSZVpYztl11Sjt4oDb9__oIfgwvQptpg2wgv0ZFRXYBX9-cUff344eZini2uPn2-mC0ynZclzYyoilKruswLzotc1W3OREWYaVhrgDZCs5YWDSsbbphS2oi2FqLknLZAoC75FL0_6A6xWUOroR-96uTg7Vr5rXTKyn9veruSS7eRNSepN0kCpweB1ZOy-WwhdznCBSWCVRua2Hf3zbz7HiGMcm2Dhq5TPbgYJBMsrwu2m2WK3j5Bb130ffqKROWEpe1xc-1dCB7MwwsokTvrZbJe7q1P7JvHkz6Qf71OwPkBuLMdbP-vJC-v5wfJPzM9ub8</recordid><startdate>202204</startdate><enddate>202204</enddate><creator>Ortiz, Diana</creator><creator>Chen, Jian</creator><creator>Outram, Megan A.</creator><creator>Saur, Isabel M.L.</creator><creator>Upadhyaya, Narayana M.</creator><creator>Mago, Rohit</creator><creator>Ericsson, Daniel J.</creator><creator>Cesari, Stella</creator><creator>Chen, Chunhong</creator><creator>Williams, Simon J.</creator><creator>Dodds, Peter N.</creator><general>Wiley Subscription Services, Inc</general><general>Wiley</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7SN</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>1XC</scope><scope>VOOES</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-5610-1260</orcidid><orcidid>https://orcid.org/0000-0003-0620-5923</orcidid><orcidid>https://orcid.org/0000-0001-8670-6984</orcidid><orcidid>https://orcid.org/0000-0001-5101-9244</orcidid><orcidid>https://orcid.org/0000-0001-7813-2415</orcidid><orcidid>https://orcid.org/0000-0003-4510-3575</orcidid><orcidid>https://orcid.org/0000-0003-4781-6261</orcidid><orcidid>https://orcid.org/0000-0001-8558-0371</orcidid><orcidid>https://orcid.org/0000-0001-6120-5788</orcidid><orcidid>https://orcid.org/0000-0001-5286-073X</orcidid><orcidid>https://orcid.org/0000-0002-3052-0416</orcidid><orcidid>https://orcid.org/0000-0002-3088-4738</orcidid></search><sort><creationdate>202204</creationdate><title>The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface‐exposed residue</title><author>Ortiz, Diana ; Chen, Jian ; Outram, Megan A. ; Saur, Isabel M.L. ; Upadhyaya, Narayana M. ; Mago, Rohit ; Ericsson, Daniel J. ; Cesari, Stella ; Chen, Chunhong ; Williams, Simon J. ; Dodds, Peter N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4771-f6857ca97453354a9d426802fb2dfe1b6c2d15b27b3f2aacf6d9667331de0e973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Alleles</topic><topic>AvrSr50</topic><topic>Basidiomycota - physiology</topic><topic>Binding</topic><topic>Breeding</topic><topic>Carbohydrates</topic><topic>Colonization</topic><topic>Crystal structure</topic><topic>Deoxyribonucleic acid</topic><topic>Disease Resistance - genetics</topic><topic>DNA</topic><topic>effector evolution</topic><topic>effector structure</topic><topic>Evolution</topic><topic>Genetic diversity</topic><topic>Genetic variation</topic><topic>Homology</topic><topic>Insertion</topic><topic>Life Sciences</topic><topic>Molecular modelling</topic><topic>Mutagenesis</topic><topic>Pathogens</topic><topic>Phytopathology and phytopharmacy</topic><topic>Plant Breeding</topic><topic>Plant Diseases - genetics</topic><topic>Plant resistance</topic><topic>Population genetics</topic><topic>Populations</topic><topic>Proteins</topic><topic>Recognition</topic><topic>Residues</topic><topic>resistance breakdown</topic><topic>Saccharides</topic><topic>Site-directed mutagenesis</topic><topic>Sr50</topic><topic>Stem rust</topic><topic>Stems</topic><topic>Stop codon</topic><topic>Substitutes</topic><topic>Triticum - genetics</topic><topic>Vegetal Biology</topic><topic>Virulence</topic><topic>wheat resistance</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ortiz, Diana</creatorcontrib><creatorcontrib>Chen, Jian</creatorcontrib><creatorcontrib>Outram, Megan A.</creatorcontrib><creatorcontrib>Saur, Isabel M.L.</creatorcontrib><creatorcontrib>Upadhyaya, Narayana M.</creatorcontrib><creatorcontrib>Mago, Rohit</creatorcontrib><creatorcontrib>Ericsson, Daniel J.</creatorcontrib><creatorcontrib>Cesari, Stella</creatorcontrib><creatorcontrib>Chen, Chunhong</creatorcontrib><creatorcontrib>Williams, Simon J.</creatorcontrib><creatorcontrib>Dodds, Peter N.</creatorcontrib><collection>Wiley Open Access</collection><collection>Wiley Online Library</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The New phytologist</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ortiz, Diana</au><au>Chen, Jian</au><au>Outram, Megan A.</au><au>Saur, Isabel M.L.</au><au>Upadhyaya, Narayana M.</au><au>Mago, Rohit</au><au>Ericsson, Daniel J.</au><au>Cesari, Stella</au><au>Chen, Chunhong</au><au>Williams, Simon J.</au><au>Dodds, Peter N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface‐exposed residue</atitle><jtitle>The New phytologist</jtitle><addtitle>New Phytol</addtitle><date>2022-04</date><risdate>2022</risdate><volume>234</volume><issue>2</issue><spage>592</spage><epage>606</epage><pages>592-606</pages><issn>0028-646X</issn><eissn>1469-8137</eissn><notes>These authors contributed equally to this work.</notes><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Summary
Pathogen effectors are crucial players during plant colonisation and infection. Plant resistance mostly relies on effector recognition to activate defence responses. Understanding how effector proteins escape from plant surveillance is important for plant breeding and resistance deployment.
Here we examined the role of genetic diversity of the stem rust (Puccinia graminis f. sp. tritici (Pgt)) AvrSr50 gene in determining recognition by the corresponding wheat Sr50 resistance gene. We solved the crystal structure of a natural variant of AvrSr50 and used site‐directed mutagenesis and transient expression assays to dissect the molecular mechanisms explaining gain of virulence.
We report that AvrSr50 can escape recognition by Sr50 through different mechanisms including DNA insertion, stop codon loss or by amino‐acid variation involving a single substitution of the AvrSr50 surface‐exposed residue Q121. We also report structural homology of AvrSr50 to cupin superfamily members and carbohydrate‐binding modules indicating a potential role in binding sugar moieties.
This study identifies key polymorphic sites present in AvrSr50 alleles from natural stem rust populations that play important roles to escape from Sr50 recognition. This constitutes an important step to better understand Pgt effector evolution and to monitor AvrSr50 variants in natural rust populations.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>35107838</pmid><doi>10.1111/nph.18011</doi><tpages>606</tpages><orcidid>https://orcid.org/0000-0002-5610-1260</orcidid><orcidid>https://orcid.org/0000-0003-0620-5923</orcidid><orcidid>https://orcid.org/0000-0001-8670-6984</orcidid><orcidid>https://orcid.org/0000-0001-5101-9244</orcidid><orcidid>https://orcid.org/0000-0001-7813-2415</orcidid><orcidid>https://orcid.org/0000-0003-4510-3575</orcidid><orcidid>https://orcid.org/0000-0003-4781-6261</orcidid><orcidid>https://orcid.org/0000-0001-8558-0371</orcidid><orcidid>https://orcid.org/0000-0001-6120-5788</orcidid><orcidid>https://orcid.org/0000-0001-5286-073X</orcidid><orcidid>https://orcid.org/0000-0002-3052-0416</orcidid><orcidid>https://orcid.org/0000-0002-3088-4738</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | The New phytologist, 2022-04, Vol.234 (2), p.592-606 |
| issn | 0028-646X 1469-8137 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_9306850 |
| source | Wiley-Blackwell Journals |
| subjects | Alleles AvrSr50 Basidiomycota - physiology Binding Breeding Carbohydrates Colonization Crystal structure Deoxyribonucleic acid Disease Resistance - genetics DNA effector evolution effector structure Evolution Genetic diversity Genetic variation Homology Insertion Life Sciences Molecular modelling Mutagenesis Pathogens Phytopathology and phytopharmacy Plant Breeding Plant Diseases - genetics Plant resistance Population genetics Populations Proteins Recognition Residues resistance breakdown Saccharides Site-directed mutagenesis Sr50 Stem rust Stems Stop codon Substitutes Triticum - genetics Vegetal Biology Virulence wheat resistance |
| title | The stem rust effector protein AvrSr50 escapes Sr50 recognition by a substitution in a single surface‐exposed residue |
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