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. 2016 Dec:109:248-261.
doi: 10.1016/j.plaphy.2016.10.005. Epub 2016 Oct 11.

Senescence-specific change in ROS scavenging enzyme activities and regulation of various SOD isozymes to ROS levels in psf mutant rice leaves

Affiliations

Senescence-specific change in ROS scavenging enzyme activities and regulation of various SOD isozymes to ROS levels in psf mutant rice leaves

Fubiao Wang et al. Plant Physiol Biochem. 2016 Dec.

Abstract

To clarify the interaction between different antioxidant enzymes for monitoring oxidative stress and ROS burst in rice senescent leaves, we investigated the genotype-dependent alteration in temporal patterns of the O2•- production rate, H2O2 content, and ROS-scavenging enzyme activities during leaf senescence in two rice genotypes, namely, the premature senescence of flag leaf (psf) mutant and its wild type. Results showed that the psf mutant differed obviously from its wild type in leaf O2•- generation rate and H2O2 content accumulation, and the decreased activities of SOD, CAT, and APX in the psf leaves were strongly responsible for the increased ROS level and the accelerated leaf senescence. By contrast, the increase in POD activity was positively correlated with the senescence-related enhancement in O2•- generation in rice leaves. Among various SOD isoforms, Mn-SOD responded sensitively to the increasing O2•- generation rate, whereas Cu/Zn-SOD remained stable with the progression of leaf senescence. These findings suggest that the senescence-related decline in total SOD activity was mostly attributable to the downregulation of both the translation and transcription of Mn-SOD isoform. This occurrence finally resulted in the collapse of SOD defense system and accelerated leaf senescence for the psf mutant. Furthermore, we presented the possible contribution of several Cu/Zn-SOD expression patterns to the senescence-related O2•- detoxification in different cell compartments.

Keywords: Antioxidant enzymes; Leaf senescence; Methyl viologen (MV); Reactive oxygen species (ROS); SOD isoforms.

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