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Dioscorin is one of the major soluble proteins in yam tubers. Unlike other well-known plant storage proteins, such as patatin and sporamin, dioscorin is argued for its function as storage proteins, and the molecular mechanisms underlying its expressional complexity are little understood. In this study, we isolated five dioscorin genes from L., comprising three class A (, - and -) and two class B ( and -) isoforms. Expressions of all dioscorin genes gradually decreased in mother tubers during yam sprouting and regrowth. On the other hand, all dioscorin genes accumulated transcripts progressively with tuber development in new tubers, with being the most prominent isoform. In yam leaves, the expressions of 5 were up-regulated by the treatments of five phytohormones (gibberellic acid, salicylic acid, indole-3-acetic acid, abscisic acid, and ethylene), and three abiotic stresses (high-temperature, low-temperature and drought). To further elucidate the regulatory mechanisms of expressions, transgenic plants harboring the promoter-β-glucuronidase (GUS) fusion were generated. GUS staining showed that expressions of the promoter were detected mainly in the shoot apical meristem (SAM) and hypocotyls, and enhanced by the treatments of the five hormones, and the three abiotic stresses mentioned above. These results suggest diverse roles of in yam sprouting, regrowth, and tuberization, as well as in response to enviromental cues.
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http://dx.doi.org/10.3390/ijms18071579 | DOI Listing |
J Genet Eng Biotechnol
July 2020
Department of Biochemistry and Molecular Biology, Obafemi Awolowo University, Ile-Ife, Nigeria.
Background: The storage protein of the aerial tuber of Dioscorea bulbifera was purified and its physicochemical, enzymatic and molecular properties determined with a view to comparing its functionality and genetic relatedness with other storage proteins.
Results: The purified protein had molecular weight of 21 kDa. The protein showed carbonic anhydrase, trypsin inhibitory, dehydroascorbate reductase and monodehydroascorbate reductase activities.
Int J Mol Sci
July 2017
Institute of Tropical Agriculture and Forestry, Hainan University, Haikou 570228, China.
Dioscorin is one of the major soluble proteins in yam tubers. Unlike other well-known plant storage proteins, such as patatin and sporamin, dioscorin is argued for its function as storage proteins, and the molecular mechanisms underlying its expressional complexity are little understood. In this study, we isolated five dioscorin genes from L.
View Article and Find Full Text PDFJ Sci Food Agric
March 2013
Department of Life Science and Institute of Biotechnology, National Dong Hwa University, Hualien County 974, Taiwan.
Background: Dioscorins are the major storage proteins of yam tubers. However, the molecular nature of their heterogeneity in tubers has not been fully elucidated. In this study the authors isolated the dioscorin gene families of Dioscorea japonica and Dioscorea pseudojaponica, performed matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF-MS) and elucidated which dioscorin isoforms are the major constituents in tubers.
View Article and Find Full Text PDFProtein Expr Purif
September 2012
Department of Life Science, National Dong Hwa University, Hualien County 974, Taiwan, ROC.
Plant Sci
February 2012
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Dioscorin, the major tuber storage protein of yam, has been shown to possess carbonic anhydrase, trypsin inhibitor, dehydroascorbate reductase, and monodehydroascorbate reductase activities. In the present study, dioscorin from Dioscorea japonica was confirmed as a glycoprotein using the enhanced concanavalin A-peroxidase staining method, and the protein was shown to have both N- and O-glycans. Following the gene cloning, four full-length isoforms of dioscorin were expressed in Escherichia coli and purified by affinity purification and anion-exchange chromatography for structural and biochemical experiments.
View Article and Find Full Text PDF