Increased cysteine biosynthesis capacity of transgenic tobacco overexpressing an O-acetylserine(thiol) lyase modifies plant responses to oxidative stress.
O-Acetylserine(thiol) lyase (OASTL), a key enzyme of plant sulfur metabolism, catalyzes the formation of Cys from sulfide and O-acetylserine. The biosynthesis of Cys is regarded as the exclusive function of sulfur reduction in plants, and a key limiting step in the production of glutathione (GSH), a thiol implicated in various cellular functions, including sulfur transport, gene expression, scavenging of reactive oxygen species (ROS), and resistance to biotic and abiotic stresses. To examine whether an increased capacity for cysteine (Cys) biosynthesis alters cellular responses to such stresses, we studied the differential changes in thiol levels and ROS scavenging of transgenic tobacco (Nicotiana tabacum) plants expressing the wheat (Triticum aestivum) OASTL gene, cys1, to SO(2) and to the ROS generator, methyl viologen. Intracellular Cys and GSH contents were generally higher in cys1 transgenics than in controls under normal growth conditions, but became especially elevated in transgenic plants after SO(2) exposure. An examination of differences in the ROS scavenging system of the transgenic plants also demonstrated the specific accumulation of Cu/Zn superoxide dismutase transcripts, known to be induced by Cys or GSH, and elevated cellular superoxide dismutase activities. The transgenic plants accordingly showed dramatic reductions in the extent of both foliar and photooxidative damage in response to acute SO(2), as well as reduced levels of chlorosis and membrane damage following methyl viologen treatment. Overall, our results imply that OASTL plays a pivotal role in the synthesis of Cys and GSH that are required for regulation of plant responses to oxidative stress.
Youssefian
S
S
Laboratory of Molecular Genetics, Biotechnology Institute, Faculty of Bioresource Sciences, Akita Prefectural University, Ohgata-mura 010-0444, Akita, Japan. shohab@agri.akita-pu.ac.jp
Nakamura
M
M
Orudgev
E
E
Kondo
N
N
D000222:Adaptation, Physiological; D019757:Carbon-Oxygen Lyases / Q000378:metabolism*; D003545:Cysteine / Q000096:biosynthesis*; D003547:Cysteine Synthase; D004351:Drug Resistance; D017343:Genes, Plant; D005978:Glutathione / Q000096:biosynthesis; D006540:Herbicides / Q000494:pharmacology; D009097:Multienzyme Complexes; D018384:Oxidative Stress; D010269:Paraquat / Q000494:pharmacology; D018515:Plant Leaves / Q000378:metabolism; D030821:Plants, Genetically Modified; D010947:Plants, Toxic; D012333:RNA, Messenger / Q000378:metabolism; D018749:RNA, Plant / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013440:Sulfides / Q000378:metabolism; D013458:Sulfur Dioxide / Q000378:metabolism; D013482:Superoxide Dismutase / Q000096:biosynthesis / Q000235:genetics; D014026:Nicotiana / Q000201:enzymology / Q000378:metabolism*; D014908:Triticum / Q000201:enzymology / Q000235:genetics
D006540:Herbicides; D009097:Multienzyme Complexes; D012333:RNA, Messenger; D018749:RNA, Plant; D017382:Reactive Oxygen Species; D029701:Saccharomyces cerevisiae Proteins; D013438:Sulfhydryl Compounds; D013440:Sulfides; D013458:Sulfur Dioxide; D013482:Superoxide Dismutase; D003547:Cysteine Synthase; C103381:MET17 protein, S cerevisiae; C018725:O-acetylhomoserine (thiol)-lyase; D019757:Carbon-Oxygen Lyases; D005978:Glutathione; D003545:Cysteine; D010269:Paraquat