The induction of manganese superoxide dismutase in response to stress in Nicotiana plumbaginifolia

Superoxide dismutases (SODs) are metalloproteins that catalyse the dismutation of superoxide radicals to oxygen and hydrogen peroxide. The enzyme has been found in all aerobic organisms examined, where it plays a major role in the defence against toxic reduced oxygen species which are generated in m...

Full description

Saved in:
Bibliographic Details
Published in:The EMBO journal 1989-01, Vol.8 (1), p.31-38
Main Authors: Bowler, C., Alliotte, T., De Loose, M., Van Montagu, M., Inzé, D.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Base Sequence
Biological and medical sciences
DNA - genetics
Electron Transport Complex IV - analysis
Enzyme Induction - drug effects
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Isoenzymes - biosynthesis
Mitochondria - enzymology
Molecular Sequence Data
Nicotiana - enzymology
Nicotiana - genetics
Oxidoreductases
Plant Diseases
Plant Proteins - biosynthesis
Plant Proteins - genetics
Plants, Toxic
Salts - pharmacology
Sucrose - pharmacology
Superoxide Dismutase - biosynthesis
Superoxide Dismutase - genetics
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Superoxide dismutases (SODs) are metalloproteins that catalyse the dismutation of superoxide radicals to oxygen and hydrogen peroxide. The enzyme has been found in all aerobic organisms examined, where it plays a major role in the defence against toxic reduced oxygen species which are generated in many biological oxidations. Here we report the complete primary structure of a plant manganese superoxide dismutase (MnSOD), deduced from a cDNA clone of Nicotiana plumbaginifolia. The plant protein is highly homologous to MnSODs from other organisms and also contains an N‐terminal leader sequence resembling a transit peptide for mitochondrial targeting. The location of the mature protein within the mitochondria has been demonstrated by subcellular fractionation experiments. We have analysed the expression profile of this MnSOD and found that it is dramatically induced during stress conditions, most notably in tissue culture as a result of sugar metabolism and also as part of the pathogenesis response of the plant, being induced by ethylene, salicylic acid, and Pseudomonas syringae infection. This induction is always accompanied by an increase in cytochrome oxidase activity, which suggests a specific protective role for MnSOD during conditions of increased mitochondrial respiration.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1989.tb03345.x