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First published online October 21, 2005; 10.1104/pp.105.069468 Plant Physiology 139:1163-1174 (2005) © 2005 American Society of Plant Biologists Differential Expression of Sucrose-Phosphate Synthase Isoenzymes in Tobacco Reflects Their Functional Specialization during Dark-Governed Starch Mobilization in Source LeavesInstitut für Pflanzengenetik und Kulturpflanzenforschung, 06466 Gatersleben, Germany
Sucrose (Suc)-phosphate synthase (SPS) plays a crucial role in the synthesis of Suc in photosynthetic and nonphotosynthetic tissues. Several isoforms of SPS exist in dicotyledonous plants that can be grouped into the different families A, B, and C. To explore whether functional differences between the SPS gene families might exist, we characterized a representative for each family from tobacco (Nicotiana tabacum). RNA-blot analysis revealed a distinct expression pattern for each of the three SPS genes. While the A-family member (NtSPSA) was found to be expressed in all tissues examined, expression of the B isoform (NtSPSB) was mainly confined to the reproductive organs and NtSPSC mRNA was exclusively detected in mature source leaves. We used RNA interference to assess the in planta function of NtSPSA and C. While silencing of NtSPSA had no detectable influence on leaf carbohydrate metabolism, reduction of NtSPSC led to an increase in leaf starch content by a factor of 3 to 8. Further analysis revealed that starch accumulation in NtSPSC-silenced plants was not due to an increased partitioning of carbon into starch, but rather showed that starch mobilization was impaired. The transgenic plants were unable to efficiently mobilize their transitory leaf starch during a prolonged period of darkness and accumulated maltose as a major intermediate of starch breakdown. NtSPSC mRNA level increased appreciably during the dark period while transcript levels of the other isoforms showed no diurnal changes. Together, these results suggest that NtSPSC is specifically involved in the synthesis of Suc during starch mobilization in the dark. The roles of the other SPS isoforms are discussed.
1 Present address: Lehrstuhl für Biochemie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany. The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Frederik Börnke (fboernke{at}biologie.uni-erlangen.de). Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.069468. * Corresponding author; e-mail fboernke{at}biologie.uni-erlangen.de; fax 4991318528254. Received August 3, 2005; returned for revision September 20, 2005; accepted September 20, 2005. This article has been cited by other articles:
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