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Home > Mathematics and Science Textbooks > Biology, life sciences > Botany and plant sciences > Characterization of the Promoter of Smcp, the Gene Encoding Solanum Melongena Cysteine Proteinase
Characterization of the Promoter of Smcp, the Gene Encoding Solanum Melongena Cysteine Proteinase

Characterization of the Promoter of Smcp, the Gene Encoding Solanum Melongena Cysteine Proteinase


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This dissertation, "Characterization of the Promoter of SmCP, the Gene Encoding Solanum Melongena Cysteine Proteinase" by Reetika, Rawat, was obtained from The University of Hong Kong (Pokfulam, Hong Kong) and is being sold pursuant to Creative Commons: Attribution 3.0 Hong Kong License. The content of this dissertation has not been altered in any way. We have altered the formatting in order to facilitate the ease of printing and reading of the dissertation. All rights not granted by the above license are retained by the author. Abstract: Abstract of thesis entitled CHARACTERIZATION OF THE PROMOTER OF SmCP, THE GENE ENCODING SOLANUM MELONGENA CYSTEINE PROTEINASE submitted by Reetika Rawat for the Degree of Doctor of Philosophy at The University of Hong Kong in September 2004 The gene encoding Solanum melongena cysteine proteinase, SmCP, is expressed at developmental events associated with programmed cell death, suggesting its involvement in protein degradation. Its expression is ethylene-inducible and is under circadian regulation with peak expression in late light. To better understand the regulation of SmCP, a 1.34-kb SmCP 5'-flanking region and its deletion derivatives were analyzed for cis-elements using reporter GUS or luc gene fusions and in vitro binding assays. These constructs were used in Agrobacterium-mediated transformation to generate transgenic tobacco for analysis. Histochemical GUS assays on transgenic tobacco revealed that with a -127/+54 promoter region, minimal basal expression occurred in all organs, while use of a larger -827/+54 fragment resulted in enhanced expression. The 5'-flanking region of SmCP contains three putative ethylene-responsive elements (EREs at -141/-134, -355/-348 and -683/-676) and two putative evening elements (EEs at -785/-777 and -795/-787). Analysis of tobacco transgenic for SmCP promoter-GUS constructs confirmed that the first putative ERE lacked activity, consistent with previous results from in vitro binding studies. Deletion -415/+54 containing ERE(- 355/-348) conferred three-fold ethylene-induction of GUS expression, while -827/+54 also containing ERE(-683/-676), produced five-fold induction. Using gel mobility shift assays, each ERE was shown to bind nuclear proteins from both ethephon-treated and untreated five-week-old seedlings, suggesting that different transcriptions factors bind each ERE under varying physiological conditions. Binding was also observed in extracts from senescent, but not young, fruits. The variation in binding at the EREs in fruits and seedlings implies that organ-specific factors may participate in binding. Analysis of transgenic tobacco expressing the various SmCP promoter-luc constructs containing wild-type or mutant EEs confirmed that both conserved EEs at - 795/-787 and -785/-777 function in circadian control. This study shows for the first time, the binding of total plant nuclear proteins to EEs in gel mobility shift assays. It suggests that multiple proteins bind these EEs, which are conserved in plants other than Arabidopsis. The presence of functional EEs and EREs in the promoter of a gene encoding cysteine proteinase suggests roles for ethylene and the circadian clock in regulating plant proteinase expression. DOI: 10.5353/th_b3474015 Subjects: Eggplant - GeneticsCysteine proteinases


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Product Details
  • ISBN-13: 9781361137277
  • Publisher: Open Dissertation Press
  • Publisher Imprint: Open Dissertation Press
  • Height: 279 mm
  • Weight: 549 gr
  • ISBN-10: 1361137274
  • Publisher Date: 26 Jan 2017
  • Binding: Paperback
  • Spine Width: 12 mm
  • Width: 216 mm


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Characterization of the Promoter of Smcp, the Gene Encoding Solanum Melongena Cysteine Proteinase
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