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Kolbert, Z.* ; Molnar, A.* ; Oláh, D.* ; Feigl, G.* ; Horváth, E.* ; Erdei, L.* ; Ördög, A.* ; Rudolf, E.E. ; Barth, T.K. ; Lindermayr, C.

S-nitrosothiol signaling is involved in regulating hydrogen peroxide metabolism of zinc-stressed Arabidopsis.

Plant Cell Physiol. 60, 2449-2463 (2019)
Verlagsversion Postprint DOI
Open Access Green
Accumulation of heavy metals such as zinc (Zn) disturbs the metabolism of reactive oxygen (e.g. hydrogen peroxide, H2O2) and nitrogen species (e.g. nitric oxide, NO; S-nitrosoglutathione, GSNO) in plant cells; however, their signal interactions are not well understood. Therefore, this study examines the interplay between H2O2 metabolism and GSNO signaling in Arabidopsis. Comparing the Zn tolerance of the wild type (WT), GSNO reductase (GSNOR) overexpressor 35S::FLAG-GSNOR1 and GSNOR-deficient gsnor1-3, we observed relative Zn tolerance of gsnor1-3, which was not accompanied by altered Zn accumulation capacity. Moreover, in gsnor1-3 plants Zn did not induce NO/S-nitrosothiol (SNO) signaling, possibly due to the enhanced activity of NADPH-dependent thioredoxin reductase. In WT and 35S::FLAG-GSNOR1, GSNOR was inactivated by Zn, and Zn-induced H2O2 is directly involved in the GSNOR activity loss. In WT seedlings, Zn resulted in a slight intensification of protein nitration detected by Western blot and protein S-nitrosation observed by resin-assisted capture of SNO proteins (RSNO-RAC). LC-MS/MS analyses indicate that Zn induces the S-nitrosation of ascorbate peroxidase 1. Our data collectively show that Zn-induced H2O2 may influence its own level, which involves GSNOR inactivation-triggered SNO signaling. These data provide new evidence for the interplay between H2O2 and SNO signaling in Arabidopsis plants affected by metal stress.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 35s::flag-gsnor1 ; S-nitrosoglutathione Reductase ; S-nitrosothiol ; Excess Zinc ; Gsnor1-3 ; Nitric Oxide; Induced Oxidative Stress; Tyrosine Nitration; Nitric-oxide; Nitrosoglutathione Reductase; Superoxide-dismutase; Reactive Oxygen; Primary Leaves; Plants; Nitrosylation; Glutathione
ISSN (print) / ISBN 0032-0781
e-ISSN 1471-9053
Quellenangaben Band: 60, Heft: 11, Seiten: 2449-2463 Artikelnummer: , Supplement: ,
Verlag Oxford University Press
Verlagsort Oxford
Begutachtungsstatus Peer reviewed