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Hydrogen sulfide: A novel component in Arabidopsis peroxisomes which triggers catalase inhibition
Author(s) -
Corpas Francisco J.,
Barroso Juan B.,
GonzálezGordo Salvador,
MuñozVargas María A.,
Palma José M.
Publication year - 2019
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.12779
Subject(s) - peroxisome , catalase , biochemistry , chemistry , reactive oxygen species , arabidopsis , arabidopsis thaliana , superoxide dismutase , enzyme , mutant , gene
Plant peroxisomes have the capacity to generate different reactive oxygen and nitrogen species (ROS and RNS), such as H 2 O 2 , superoxide radical (O 2 · − ), nitric oxide and peroxynitrite (ONOO ‐ ). These organelles have an active nitro‐oxidative metabolism which can be exacerbated by adverse stress conditions. Hydrogen sulfide (H 2 S) is a new signaling gasotransmitter which can mediate the posttranslational modification (PTM) persulfidation. We used Arabidopsis thaliana transgenic seedlings expressing cyan fluorescent protein (CFP) fused to a canonical peroxisome targeting signal 1 (PTS1) to visualize peroxisomes in living cells, as well as a specific fluorescent probe which showed that peroxisomes contain H 2 S. H 2 S was also detected in chloroplasts under glyphosate‐induced oxidative stress conditions. Peroxisomal enzyme activities, including catalase, photorespiratory H 2 O 2 ‐generating glycolate oxidase (GOX) and hydroxypyruvate reductase (HPR), were assayed in vitro with a H 2 S donor. In line with the persulfidation of this enzyme, catalase activity declined significantly in the presence of the H 2 S donor. To corroborate the inhibitory effect of H 2 S on catalase activity, we also assayed pure catalase from bovine liver and pepper fruit‐enriched samples, in which catalase activity was inhibited. Taken together, these data provide evidence of the presence of H 2 S in plant peroxisomes which appears to regulate catalase activity and, consequently, the peroxisomal H 2 O 2 metabolism.