Transformed plants with elevated levels of chloroplastic SOD are not more resistant to superoxide toxicity
- 1 April 1990
- journal article
- research article
- Published by Springer Nature in Plant Molecular Biology
- Vol. 14 (4), 501-511
- https://doi.org/10.1007/bf00027496
Abstract
The petunia nuclear gene which encodes the chloroplast isozyme of superoxide dismutase, SOD-1, has been fused with an efficient rbcS promoter fragment and 3′ flanking region and introduced into tobacco and tomato cells. Transformed plants carrying this chimeric gene have up to 50-fold the levels of SOD-1 which occur in wild-type plants. However, tobacco plants with 30-to 50-fold the normal SOD-1 activity do not exhibit resistance to the light-activated herbicide paraquat. Similarly, tomato plants with 2-to 4-fold increases in SOD-1 do not exhibit tolerance to photoinhibitory conditions known to increase superoxide levels (high light, low temperatures and low CO2 concentrations). Our data indicate that increasing the chloroplastic SOD level in a plant cell is not sufficient to reduce the toxicity of superoxide.This publication has 37 references indexed in Scilit:
- Chilling-Enhanced PhotooxidationPlant Physiology, 1987
- Flash-induced fluorescence estimation of photosystem II electron-transport rates in light-adapted leavesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1987
- A Simple and General Method for Transferring Genes into PlantsScience, 1985
- SUPEROXIDE RADICALS, SUPEROXIDE DISMUTASES and OXYGEN TOXICITY IN PLANTSPhotochemistry and Photobiology, 1983
- Interaction between light and chilling temperature on the inhibition of photosynthesis in chilling‐sensitive plants*Plant, Cell & Environment, 1983
- Oxygen Activation and Oxygen ToxicityAnnual Review of Plant Physiology, 1982
- Superoxide DismutasePlant Physiology, 1982
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARISPlant Physiology, 1949