{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,21]],"date-time":"2026-04-21T17:43:30Z","timestamp":1776793410224,"version":"3.51.2"},"reference-count":54,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2008,6,28]],"date-time":"2008-06-28T00:00:00Z","timestamp":1214611200000},"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":[[2008,10]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>Establishing the mechanisms regulating the autolysis of xylem tracheary elements (TEs) is important for understanding this programmed cell death process. These data demonstrate that two paralogous <jats:italic>Arabidopsis thaliana<\/jats:italic> proteases, XYLEM CYSTEINE PROTEASE1 (XCP1) and XCP2, participated in micro\u2010autolysis within the intact central vacuole before mega\u2010autolysis was initiated by tonoplast implosion. The data acquisition was aided by the predictable pattern of seedling root xylogenesis, the availability of single and double total knock\u2010out T\u2010DNA lines, anti\u2010sera that recognized XCP1 and XCP2, and the microwave\u2010assisted processing of whole seedlings prior to immunolabeling and observation in the transmission electron microscope. During secondary wall thickening, XCP1 and XCP2 (in wild type), XCP1 (in <jats:italic>xcp2<\/jats:italic> seedlings) or XCP2 (in <jats:italic>xcp1<\/jats:italic> seedlings) were imported into the TE central vacuole. Both XCP1 and XCP2 heavily labeled dense aggregates of material within the vacuole. However, because of XCP1 deficiency in <jats:italic>xcp1<\/jats:italic> and <jats:italic>xcp1\u2003xcp2<\/jats:italic> TEs, non\u2010degraded cellular remnants first accumulated in the vacuole and then persisted in the TE lumen (longer than in the wild type) after the final mega\u2010autolysis was otherwise complete. This delayed TE clearing phenotype in <jats:italic>xcp1<\/jats:italic> was rescued by complementation with wild\u2010type <jats:italic>XCP1<\/jats:italic>. Although TEs in the <jats:italic>xcp2<\/jats:italic> single knock\u2010out cleared comparably with wild type, the non\u2010degraded remnants in <jats:italic>xcp1\u2003xcp2<\/jats:italic> TEs were more densely packed than in <jats:italic>xcp1<\/jats:italic> TEs. Therefore, XCP2 has a minor but distinct role in micro\u2010autolysis. After tonoplast implosion, XCP1 and XCP2 remained associated with disintegrating cellular material as mega\u2010autolysis, aided by additional lytic enzymes, destroyed the bulk of the cellular contents.<\/jats:p>","DOI":"10.1111\/j.1365-313x.2008.03592.x","type":"journal-article","created":{"date-parts":[[2008,6,20]],"date-time":"2008-06-20T16:23:30Z","timestamp":1213979010000},"page":"303-315","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":164,"title":["Cysteine proteases XCP1 and XCP2 aid micro\u2010autolysis within the intact central vacuole during xylogenesis in Arabidopsis roots"],"prefix":"10.1111","volume":"56","author":[{"given":"Utku","family":"Avci","sequence":"first","affiliation":[]},{"given":"H.","family":"Earl Petzold","sequence":"additional","affiliation":[]},{"given":"Ihab O.","family":"Ismail","sequence":"additional","affiliation":[]},{"given":"Eric 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