Trehalose accumulation in rice plants confers high tolerance levels to different abiotic stresses.
Trehalose is a nonreducing disaccharide of glucose that functions as a compatible solute in the stabilization of biological structures under abiotic stress in bacteria, fungi, and invertebrates. With the notable exception of the desiccation-tolerant "resurrection plants," trehalose is not thought to accumulate to detectable levels in most plants. We report here the regulated overexpression of Escherichia coli trehalose biosynthetic genes (otsA and otsB) as a fusion gene for manipulating abiotic stress tolerance in rice. The fusion gene has the advantages of necessitating only a single transformation event and a higher net catalytic efficiency for trehalose formation. The expression of the transgene was under the control of either tissue-specific or stress-dependent promoters. Compared with nontransgenic rice, several independent transgenic lines exhibited sustained plant growth, less photo-oxidative damage, and more favorable mineral balance under salt, drought, and low-temperature stress conditions. Depending on growth conditions, the transgenic rice plants accumulate trehalose at levels 3-10 times that of the nontransgenic controls. The observation that peak trehalose levels remain well below 1 mgg fresh weight indicates that the primary effect of trehalose is not as a compatible solute. Rather, increased trehalose accumulation correlates with higher soluble carbohydrate levels and an elevated capacity for photosynthesis under both stress and nonstress conditions, consistent with a suggested role in modulating sugar sensing and carbohydrate metabolism. These findings demonstrate the feasibility of engineering rice for increased tolerance of abiotic stress and enhanced productivity through tissue-specific or stress-dependent overproduction of trehalose.
Garg
Ajay K
AK
Departments of Molecular Biology and Genetics, Plant Biology, and Horticulture, Cornell University, Ithaca, NY 14853, USA.
Kim
Ju-Kon
JK
Owens
Thomas G
TG
Ranwala
Anil P
AP
Choi
Yang Do
YD
Kochian
Leon V
LV
Wu
Ray J
RJ
D050260:Carbohydrate Metabolism; D003080:Cold Temperature; D029968:Escherichia coli Proteins / Q000502:physiology; D018506:Gene Expression Regulation, Plant; D005818:Genetic Engineering; D005964:Glucosyltransferases / Q000235:genetics / Q000502:physiology; D006813:Humidity; D018527:Hydroponics; D009928:Organ Specificity; D012275:Oryza / Q000201:enzymology* / Q000502:physiology; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000502:physiology; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism; D010935:Plant Diseases; D030821:Plants, Genetically Modified / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000502:physiology; D012462:Saline Solution, Hypertonic / Q000633:toxicity; D014199:Trehalose / Q000096:biosynthesis / Q000502:physiology*
D029968:Escherichia coli Proteins; D045322:Photosynthetic Reaction Center Complex Proteins; D011993:Recombinant Fusion Proteins; D012462:Saline Solution, Hypertonic; D014199:Trehalose; D005964:Glucosyltransferases; C023180:trehalose-6-phosphate synthase; C023178:trehalose-phosphatase; D010744:Phosphoric Monoester Hydrolases