Cyst Nematode Infection Elicits Alteration in the Level of Reactive Nitrogen Species, Protein S-Nitrosylation and Nitration, and Nitrosoglutathione Reductase in Arabidopsis thaliana Roots

Abstract

Reactive nitrogen species (RNS) are redox molecules important for plant defense against pathogens. The aim of the study was to determine whether the infection by the beet cyst nematode Heterodera schachtii disrupts RNS balance in Arabidopsis thaliana roots. For this purpose, measurements of nitric oxide (NO), peroxynitrite (ONOO−), protein S-nitrosylation and nitration, and nitrosoglutathione reductase (GSNOR) in A. thaliana roots from 1 day to 15 days post-inoculation (dpi) were performed. The cyst nematode infection caused generation of NO and ONOO− in the infected roots. These changes were accompanied by an expansion of S-nitrosylated and nitrated proteins. The enzyme activity of GSNOR was decreased at 3 and 15 dpi and increased at 7 dpi in infected roots, whereas the GSNOR1 transcript level was enhanced over the entire examination period. The protein content of GSNOR was increased in infected roots at 3 dpi and 7 dpi, but at 15 dpi, did not differ between uninfected and infected roots. The protein of GSNOR was detected in plastids, mitochondria, cytoplasm, as well as endoplasmic reticulum and cytoplasmic membranes. We postulate that RNS metabolism plays an important role in plant defense against the beet cyst nematode and helps the fine-tuning of the infected plants to stress sparked by phytoparasitic nematodes.

FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions

“…In this study, we identified several ER chaperones and key enzymes in protein glycosylation, folding, transport, and lipid biosynthesis which undergo S-nitrosylation (Table 1). Consistently, GSNOR1 is known to locate in ER 60 , and dysfunction of GSNOR1 in the gsnor1/hot5 mutants leads to the increased expression of ER-stress responsive genes, like BiPs, ERDJ3A, and SHD, resulting in an insensitive response to Tm-induced ER stress. The mutants that lack S-nitrosylation target proteins, such as crt1a or ebs1, also showed altered sensitivity to Tm 61,62 .…”

Identification of the Complex Interplay Between Nematode-Related lncRNAs and Their Target Genes in Glycine max L.

“…The potential association between DE-lncRNAs and a RING/U-box superfamily gene, an Aldolase-type TIM barrel family gene, laccase7, ARF8, a MYB domain-containing gene, and several HSPs, which are involved in resistance to SCN (Zhao et al, 2017;Ul Haq et al, 2019;Cheng et al, 2020;Hishinuma-Silva et al, 2020), brings new insights into the SCN-soybean interaction. Moreover, the association between lncRNAs and nitrite reductase as a major gene in reactive nitrogen species (RNS) metabolism and plant defense against the beet cyst nematode (Labudda et al, 2020), ACC oxidase which is involved in ethylene-based signal transduction and regulates the attractiveness of soybean roots to SCN (Tucker et al, 2010;Hu et al, 2017), galactinol synthase and drought-induced gene as neighboring nematode defenserelated protein-coding genes (Kandoth et al, 2011), and NAC and MADS-box as key TFs involved in soybean defense response under RKN invasion (de Sá et al, 2012) provides important notes for further characterization of SCN resistance genes in soybean. The possible association between DE-lncRNAs and the pectin lyase-like superfamily protein as a pectin-degrading enzyme suggests pectin lyase-like superfamily gene/DE-lncRNA interaction-mediated defense signals via modification of cell wall integrity and lignin content, which is consistent with the obtained results in previous studies (Gallego-Giraldo et al, 2020).…”

Nitric Oxide in Plant Functioning: Metabolism, Signaling, and Responses to Infestation with Ecdysozoa Parasites

“…The GSNOR level was enhanced in infected roots at 3 dpi and 7 dpi, but at 15 dpi, did not differ between uninfected and infected roots. The GSNOR was observed in plastids, mitochondria, the cytoplasm, as well as in the endoplasmic reticulum and cytoplasmic membranes [236].…”