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Unlike most other <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">RLP<\/jats:styled-content> genes involved in plant defence, the <jats:italic>I<\/jats:italic> gene is not a member of a gene cluster and contains introns in its coding sequence. The <jats:italic>I<\/jats:italic> gene encodes a loopout domain larger than those in most other <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">RLP<\/jats:styled-content>s, with a distinct composition rich in serine and threonine residues. The I protein also lacks a basic cytosolic domain. Instead, this domain is rich in aromatic residues that could form a second transmembrane domain. The I protein recognises the <jats:italic>Fol<\/jats:italic> Avr1 effector protein, but, unlike many other <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">RLP<\/jats:styled-content>s, recognition specificity is determined in the C\u2010terminal half of the protein by polymorphic amino acid residues in the <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content>s just preceding the loopout domain and in the loopout domain itself. Despite these differences, we show that I\/Avr1\u2010dependent necrosis in <jats:italic>Nicotiana benthamiana<\/jats:italic> depends on the <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content> receptor\u2010like kinases (<jats:styled-content style=\"fixed-case\">RLK<\/jats:styled-content>s) <jats:styled-content style=\"fixed-case\">SERK<\/jats:styled-content>3\/<jats:styled-content style=\"fixed-case\">BAK<\/jats:styled-content>1 and <jats:styled-content style=\"fixed-case\">SOBIR<\/jats:styled-content>1. Sequence comparisons revealed that the I protein and other <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">RLP<\/jats:styled-content>s involved in plant defence all carry residues in their last <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content> and C\u2010terminal <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content> capping domain that are conserved with <jats:styled-content style=\"fixed-case\">SERK<\/jats:styled-content>3\/<jats:styled-content style=\"fixed-case\">BAK<\/jats:styled-content>1\u2010interacting residues in the same relative positions in the <jats:styled-content style=\"fixed-case\">LRR<\/jats:styled-content>\u2010<jats:styled-content style=\"fixed-case\">RLK<\/jats:styled-content>s <jats:styled-content style=\"fixed-case\">BRI<\/jats:styled-content>1 and <jats:styled-content style=\"fixed-case\">PSKR<\/jats:styled-content>1. Tyrosine mutations of two of these conserved residues, Q922 and T925, abolished I\/Avr1\u2010dependent necrosis in <jats:italic>N. benthamiana<\/jats:italic>, consistent with similar mutations in <jats:styled-content style=\"fixed-case\">BRI<\/jats:styled-content>1 and <jats:styled-content style=\"fixed-case\">PSKR<\/jats:styled-content>1 preventing their interaction with <jats:styled-content style=\"fixed-case\">SERK<\/jats:styled-content>3\/<jats:styled-content style=\"fixed-case\">BAK<\/jats:styled-content>1.<\/jats:p>","DOI":"10.1111\/tpj.13458","type":"journal-article","created":{"date-parts":[[2016,12,20]],"date-time":"2016-12-20T07:22:57Z","timestamp":1482218577000},"page":"1195-1209","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":116,"title":["The tomato <i>I<\/i> gene for Fusarium wilt resistance encodes an atypical leucine\u2010rich repeat receptor\u2010like protein whose function is nevertheless dependent on <scp>SOBIR<\/scp>1 and <scp>SERK<\/scp>3\/<scp>BAK<\/scp>1"],"prefix":"10.1111","volume":"89","author":[{"given":"Ann\u2010Maree","family":"Catanzariti","sequence":"first","affiliation":[{"name":"Division of Plant Sciences Research School of Biology The Australian National University Acton ACT Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huong T. T.","family":"Do","sequence":"additional","affiliation":[{"name":"Division of Plant Sciences Research School of Biology The Australian National University Acton ACT Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierrick","family":"Bru","sequence":"additional","affiliation":[{"name":"Division of Plant Sciences Research School of Biology The Australian National University Acton ACT Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mara","family":"de Sain","sequence":"additional","affiliation":[{"name":"Swammerdam Institute for Life Sciences University of Amsterdam Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Louise F.","family":"Thatcher","sequence":"additional","affiliation":[{"name":"CSIRO Agriculture and Food Centre for Environment and Life Sciences Wembley WA Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Martijn","family":"Rep","sequence":"additional","affiliation":[{"name":"Swammerdam Institute for Life Sciences University of Amsterdam Amsterdam The Netherlands"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8809-5822","authenticated-orcid":false,"given":"David A.","family":"Jones","sequence":"additional","affiliation":[{"name":"Division of Plant Sciences Research School of Biology The Australian National University Acton ACT Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2017,2,11]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.17.10306"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1038\/nplants.2015.140"},{"key":"e_1_2_6_4_1","first-page":"303","article-title":"Physiological specialization in the Tomato wilt fungus Fusarium oxysporum f. sp. lycopersici","volume":"70","author":"Alexander L.J.","year":"1945","journal-title":"J. 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