Abstract: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 Á À ), nitric oxide and peroxynitrite (ONOO -). These organelles have an active nitrooxidative 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 f… Show more
“…These observations are also supported by in vitro biochemical assays in Arabidopsis using H 2 S donors. Thus, it has been shown that H 2 S positively regulates ascorbate peroxidase activity (Aroca et al ) but exerts an inhibitory effect on catalase activity (Corpas et al ). A recent proteomic study of A. thaliana leaves reported that both NADP‐ICDH and NADP‐ME are targets of persulfidation (Aroca et al ) [which is a posttranslational protein modification, similar to protein S ‐nitrosation (Cys‐SNO), mediated by H 2 S that affects thiol groups (Cys‐SSH)].…”
NADPH is an essential cofactor in many physiological processes. Fruit ripening is caused by multiple biochemical pathways in which, reactive oxygen and nitrogen species (ROS/RNS) metabolism is involved. Previous studies have demonstrated the differential modulation of nitric oxide (NO) and hydrogen sulfide (H2S) content during sweet pepper (Capsicum annuum L.) fruit ripening, both of which regulate NADP‐isocitrate dehydrogenase activity. To gain a deeper understanding of the potential functions of other NADPH‐generating components, we analyzed glucose‐6‐phosphate dehydrogenase (G6PDH) and 6‐phosphogluconate dehydrogenase (6PGDH), which are involved in the oxidative phase of the pentose phosphate pathway (OxPPP) and NADP‐malic enzyme (NADP‐ME). During fruit ripening, G6PDH activity diminished by 38%, while 6PGDH and NADP‐ME activity increased 1.5‐ and 2.6‐fold, respectively. To better understand the potential regulation of these NADP‐dehydrogenases by H2S, we obtained a 50–75% ammonium‐sulfate‐enriched protein fraction containing these proteins. With the aid of in vitro assays, in the presence of H2S, we observed that, while NADP‐ME activity was inhibited by up to 29–32% using 2 and 5 mM Na2S as H2S donor, G6PDH and 6PGDH activities were unaffected. On the other hand, NO donors, S‐nitrosocyteine (CysNO) and DETA NONOate also inhibited NADP‐ME activity by 35%. These findings suggest that both NADP‐ME and 6PGDH play an important role in maintaining the supply of NADPH during pepper fruit ripening and that H2S and NO partially modulate the NADPH‐generating system.
“…These observations are also supported by in vitro biochemical assays in Arabidopsis using H 2 S donors. Thus, it has been shown that H 2 S positively regulates ascorbate peroxidase activity (Aroca et al ) but exerts an inhibitory effect on catalase activity (Corpas et al ). A recent proteomic study of A. thaliana leaves reported that both NADP‐ICDH and NADP‐ME are targets of persulfidation (Aroca et al ) [which is a posttranslational protein modification, similar to protein S ‐nitrosation (Cys‐SNO), mediated by H 2 S that affects thiol groups (Cys‐SSH)].…”
NADPH is an essential cofactor in many physiological processes. Fruit ripening is caused by multiple biochemical pathways in which, reactive oxygen and nitrogen species (ROS/RNS) metabolism is involved. Previous studies have demonstrated the differential modulation of nitric oxide (NO) and hydrogen sulfide (H2S) content during sweet pepper (Capsicum annuum L.) fruit ripening, both of which regulate NADP‐isocitrate dehydrogenase activity. To gain a deeper understanding of the potential functions of other NADPH‐generating components, we analyzed glucose‐6‐phosphate dehydrogenase (G6PDH) and 6‐phosphogluconate dehydrogenase (6PGDH), which are involved in the oxidative phase of the pentose phosphate pathway (OxPPP) and NADP‐malic enzyme (NADP‐ME). During fruit ripening, G6PDH activity diminished by 38%, while 6PGDH and NADP‐ME activity increased 1.5‐ and 2.6‐fold, respectively. To better understand the potential regulation of these NADP‐dehydrogenases by H2S, we obtained a 50–75% ammonium‐sulfate‐enriched protein fraction containing these proteins. With the aid of in vitro assays, in the presence of H2S, we observed that, while NADP‐ME activity was inhibited by up to 29–32% using 2 and 5 mM Na2S as H2S donor, G6PDH and 6PGDH activities were unaffected. On the other hand, NO donors, S‐nitrosocyteine (CysNO) and DETA NONOate also inhibited NADP‐ME activity by 35%. These findings suggest that both NADP‐ME and 6PGDH play an important role in maintaining the supply of NADPH during pepper fruit ripening and that H2S and NO partially modulate the NADPH‐generating system.
“…The presence of superoxide dismutase (SOD) activity was confirmed biochemically in various species (reviewed in Corpas et al, 2017), and a Cu-Zn superoxide dismutase (CSD3) was identified in multiple Arabidopsis peroxisome proteomic studies (reviewed in . Peroxisomes also generate RNS under stress conditions such as excess Cd, and probably reactive sulfur species (RSS) as well (Corpas & Barroso, 2014;Corpas et al, 2019a). Proteome analysis showed that numerous peroxisomal proteins are S-nitrosylated or nitrated, implying that RNS has a role in peroxisomal function (Sandalio & Romero-Puertas, 2015).…”
Summary
Peroxisomes are small, ubiquitous organelles that are delimited by a single membrane and lack genetic material. However, these simple‐structured organelles are highly versatile in morphology, abundance and protein content in response to various developmental and environmental cues. In plants, peroxisomes are essential for growth and development and perform diverse metabolic functions, many of which are carried out coordinately by peroxisomes and other organelles physically interacting with peroxisomes. Recent studies have added greatly to our knowledge of peroxisomes, addressing areas such as the diverse proteome, regulation of division and protein import, pexophagy, matrix protein degradation, solute transport, signaling, redox homeostasis and various metabolic and physiological functions. This review summarizes our current understanding of plant peroxisomes, focusing on recent discoveries. Current problems and future efforts required to better understand these organelles are also discussed. An improved understanding of peroxisomes will be important not only to the understanding of eukaryotic cell biology and metabolism, but also to agricultural efforts aimed at improving crop performance and defense.
“…All these data point out the complexity of plant peroxisomal metabolism which seems to be much more intricate than expected, as well as new functions for peroxisomes in the connection with different subcellular compartments. In this sense, very recent data obtained in our laboratory indicated that plant peroxisomes also contain the gasotransmitter hydrogen sulfide (H 2 S) which is a catalase inhibitor (Corpas et al ), and raised new questions on the potential physiological function of H 2 S in the metabolism of plant peroxisomes.…”
Plant peroxisomes are subcellular compartments involved in many biochemical pathways during the life cycle of a plant but also in the mechanism of response against adverse environmental conditions. These organelles have an active nitro-oxidative metabolism under physiological conditions but this could be exacerbated under stress situations. Furthermore, peroxisomes have the capacity to proliferateand also undergo biochemical adaptations depending on the surrounding cellular status. An important characteristic of peroxisomes is that they have a dynamic metabolism of reactive nitrogen and oxygen species (RNS and ROS) which generates two key molecules, nitric oxide (NO) and hydrogen peroxide (H 2 O 2 ). These molecules can exert signaling functions by means of post-translational modifications that affect the functionality of target molecules like proteins, peptides or fatty acids. This review provides an overview of the endogenous metabolism of ROS and RNS in peroxisomes with special emphasis on polyamine and uric acid metabolism as well as the possibility that these organelles could be a source of signal molecules involved in the functional interconnection with other subcellular compartments.
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