{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,24]],"date-time":"2026-01-24T08:03:23Z","timestamp":1769241803210,"version":"3.49.0"},"reference-count":35,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2005,2,23]],"date-time":"2005-02-23T00:00:00Z","timestamp":1109116800000},"content-version":"vor","delay-in-days":4986,"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":[[1991,7]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p>In higher plants sucrose plays a central role with respect to both short\u2010term storage and distribution of photoassimilates formed in the leaf. Sucrose is synthesized in the cytosol, transiently stored in the vacuole and exported via the apoplast. In order to elucidate the role of the different compartments with respect to sucrose metabolism, a yeast\u2010derived invertase was directed into the cytosol and vacuole of transgenic tobacco plants. This was in addition to the targeting of yeast\u2010derived invertase into the apoplast described previously. Vacuolar targeting was achieved by fusing an N\u2010terminal portion (146 amino acids long) of the vacuolar protein patatin to the coding region of the mature invertase protein.<\/jats:p><jats:p>Transgenic tobacco plants expressing the yeast\u2010derived invertase in different subcellular compartments displayed dramatic phenotypic differences when compared to wild\u2010type plants. All transgenic plants showed stunted growth accompanied by reduced root formation. Starch and soluble sugars accumulated in leaves indicating that the distribution of sucrose was impaired in all cases. Expression of cytosolic yeast invertase resulted in the accumulation of starch and soluble sugars in both very young (sink) and older (source) leaves. The leaves were curved, indicating a more rapid cell expansion or cell division at the upper side of the leaf. Light\u2010green sectors with reduced photosynthetic activity were evenly distributed over the leaf surface. With the apoplastic and vacuolar invertase, the phenotypical changes induced only appear in older (source) leaves. The development of bleached and\/or necrotic sectors was linked to the source state of a leaf. Bleaching followed the sink to source transition, starting at the rim of the leaf and moving to the base. The bleaching was paralleled by the inhibition of photosynthesis.<\/jats:p>","DOI":"10.1111\/j.1365-313x.1991.00095.x","type":"journal-article","created":{"date-parts":[[2005,2,23]],"date-time":"2005-02-23T10:48:42Z","timestamp":1109155722000},"page":"95-106","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":155,"title":["Transgenic tobacco plants expressing yeast\u2010derived invertase in either the cytosol, vacuole or apoplast: a powerful tool for studying sucrose metabolism and sink\/source interactions"],"prefix":"10.1111","volume":"1","author":[{"given":"Uwe","family":"Sonnewald","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Monika","family":"Brauer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Antje","family":"von Schaewen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark","family":"Stitt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lothar","family":"Willmitzer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2005,2,23]]},"reference":[{"key":"e_1_2_1_2_1","doi-asserted-by":"publisher","DOI":"10.1105\/tpc.2.12.1145"},{"key":"e_1_2_1_3_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/12.22.8711"},{"key":"e_1_2_1_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.77.3.1496"},{"key":"e_1_2_1_5_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.63.6.1123"},{"key":"e_1_2_1_6_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-3040.1988.tb01792.x"},{"key":"e_1_2_1_7_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.81.3.461"},{"key":"e_1_2_1_8_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.79.1.114"},{"key":"e_1_2_1_9_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00330935"},{"key":"e_1_2_1_10_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/13.13.4777"},{"key":"e_1_2_1_11_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.89.4.1042"},{"key":"e_1_2_1_12_1","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.108.2.327"},{"key":"e_1_2_1_13_1","doi-asserted-by":"crossref","first-page":"4387","DOI":"10.1016\/S0021-9258(18)61360-2","article-title":"Structure, assembly and secretion of octameric invertase","volume":"262","author":"Esmon P.C.","year":"1987","journal-title":"J. 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