{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T00:30:51Z","timestamp":1774485051119,"version":"3.50.1"},"reference-count":64,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2012,7,9]],"date-time":"2012-07-09T00:00:00Z","timestamp":1341792000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Plant Journal"],"published-print":{"date-parts":[[2012,9]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Accumulating evidence shows that proper degradation of proteins that affect defense responses in a positive or negative manner is critical in plant immunity. However, the role of plant degradation systems such as the 26S proteasome in plant immunity is not well understood. Loss\u2010of\u2010function mutations in <jats:italic>EDR2<\/jats:italic> (<jats:italic>ENHANCED DISEASE RESISTANCE 2<\/jats:italic>) lead to increased resistance to the adapted biotrophic powdery mildew pathogen <jats:italic>Golovinomyces cichoracearum<\/jats:italic>. To study the molecular interactions between powdery mildew pathogen and Arabidopsis, we performed a screen for suppressors of <jats:italic>edr2<\/jats:italic> and found that mutation in the gene that encodes RPN1a, a subunit of the 26S proteasome, suppressed <jats:italic>edr2\u2010<\/jats:italic>associated disease resistance phenotypes. In addition, RPN1a is required for <jats:italic>edr1\u2010<\/jats:italic> and <jats:italic>pmr4<\/jats:italic>\u2010mediated powdery mildew resistance and mildew\u2010induced cell death. Furthermore, we show that <jats:italic>rpn1a<\/jats:italic> displayed enhanced susceptibility to the fungal pathogen <jats:italic>G.\u00a0cichoracearum<\/jats:italic> and to virulent and avirulent bacterial <jats:italic>Pto<\/jats:italic> DC3000 strains, which indicated that <jats:italic>rpn1a<\/jats:italic> has defects in basal defense and resistance (R) protein\u2010mediated defense. RPN1a\u2013GFP localizes to both the nucleus and cytoplasm. Accumulation of RPN1a is affected by salicylic acid (SA) and the <jats:italic>rpn1a<\/jats:italic> mutant has defects in SA accumulation upon <jats:italic>Pto<\/jats:italic> DC3000 infection. Further analysis revealed that two other subunits of the 26S proteasome, RPT2a and RPN8a are also involved in <jats:italic>edr2<\/jats:italic>\u2010mediated disease resistance. Based on these results, we conclude that RPN1a is required for basal defense and R protein\u2010mediated defense. Our data provide evidence that some subunits of the 26S proteasome are involved in innate immunity in Arabidopsis.<\/jats:p>","DOI":"10.1111\/j.1365-313x.2012.05048.x","type":"journal-article","created":{"date-parts":[[2012,5,11]],"date-time":"2012-05-11T17:50:26Z","timestamp":1336758626000},"page":"1015-1028","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":48,"title":["RPN1a, a 26S proteasome subunit, is required for innate immunity in 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