Bacterial wilt is a serious problem affecting many important food crops. Recent studies have indicated that treatment with biotic or abiotic stress factors may increase the resistance of plants to bacterial infection. This study investigated the effects of magnesium oxide nanoparticles (MgO NP) on disease resistance in tomato plants against Ralstonia solanacearum, as well as its antibacterial activity. The roots of tomato seedlings were inoculated with R. solanacearum and then immediately treated with MgO NP; the treated plants showed very little inhibition of bacterial wilt. In contrast, when roots were drenched with a MgO NP suspension prior to inoculation with the pathogen, the incidence of disease was significantly reduced. Rapid generation of reactive oxygen species such as O 2À˙r adicals was observed in tomato roots treated with MgO NP. Further O 2 À˙w as rapidly generated when tomato plant extracts or polyphenols were added to the MgO NP suspension, suggesting that the generation of O 2 À˙i n tomato roots might be due to a reaction between MgO NP and polyphenols present in the roots. Salicylic acid-inducible PR1, jasmonic acid-inducible LoxA, ethylene-inducible Osm, and systemic resistance-related GluA were up-regulated in both the roots and hypocotyls of tomato plants after treatment of the plant roots with MgO NP. Histochemical analyses showed that b-1,3-glucanase and tyloses accumulated in the xylem and apoplast of pith tissues of the hypocotyls after MgO NP treatment. These results indicate that MgO NP induces systemic resistance in tomato plants against R. solanacearum.
Ferroportin 1 (FPN1) is an iron export protein found in mammals. FPN1 is important for the export of iron across the basolateral membrane of absorptive enterocytes and across the plasma membrane of macrophages. The expression of FPN1 is regulated by hepcidin, which binds to FPN1 and then induces its degradation. Previously, we demonstrated that divalent metal transporter 1 (DMT1) interacts with the intracellular iron chaperone protein poly(rC)-binding protein 2 (PCBP2). Subsequently, PCBP2 receives iron from DMT1 and then disengages from the transporter. In this study, we investigated the function of PCBP2 in iron export. Mammalian genomes encode four PCBPs (i.e. PCBP1-4). Here, for the first time, we demonstrated using both yeast and mammalian cells that PCBP2, but not PCBP1, PCBP3, or PCBP4, binds with FPN1. Importantly, ironloaded, but not iron-depleted, PCBP2 interacts with FPN1. The PCBP2-binding domain of FPN1 was identified in its C-terminal cytoplasmic region. The silencing of PCBP2 expression suppressed FPN1-dependent iron export from cells. These results suggest that FPN1 exports iron received from the iron chaperone PCBP2. Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process.Iron is an essential but potentially hazardous bio-metal (1). Because of its ability to readily accept or donate electrons, iron is a valuable cofactor that is used in oxygen transport, electron transfer, and DNA synthesis (2, 3). However, iron is potentially toxic because it catalyzes the generation of reactive oxygen species. The ensuing oxidative stress is associated with damage to cellular molecules, injury to tissues, and disease via processes including hydroxyl radical formation, glutathione depletion, protein aggregation, lipid peroxidation, and nucleic acid modification (4, 5).Despite its high abundance in nature, ferric iron is poorly bioavailable due to its exceedingly low solubility at physiological pH. Thus, the acquisition and usage of iron presents a considerable challenge to cells and organisms, which have evolved sophisticated mechanisms to satisfy their metabolic needs and concomitantly minimize the risk of toxicity.It has long been known that there is very little, yet potentially toxic, low-molecular-weight iron in rapidly metabolizing cells (6). However, the molecular mechanisms involved in intracellular iron transport have remained elusive (7). Recently, it was revealed that one of the mechanisms of iron transport and metabolism involves intracellular chaperone proteins (8). It was reported that poly(rC)-binding protein 1 (PCBP1), 3 also referred to as ␣-CP1 or hnRNP E1, is a cytosolic iron chaperone protein that delivers iron to ferritin (9). PCBP1 binds to iron with micromolar affinity at a molar ratio of 3:1 Fe:PCBP1. Notably, PCBP1 has been shown previously to function as an RNAand DNA-binding protein and has been identified as a member of a family of four homologous proteins containing three heterogeneous nuclear ribonucleoprotein K-homology (KH) do...
Grey mould (Botrytis cinerea) is a very successful necrotroph, causing serious losses in more than 200 crop hosts. This study investigated the antifungal effect of 405-nm light on this pathogen. Our results suggest that the excitation of endogenous porphyrins and subsequent accumulation of singlet oxygen contribute to the 405-nm light-mediated photoinactivation of grey mould. The development of symptoms in detached tomato leaves inoculated with B. cinerea spores was significantly inhibited by irradiation with 405-nm light, indicating that this wavelength of light has a potential use in controlling plant diseases caused by B. cinerea.
The n-butanol extract of shallot basal plates and roots showed antifungal activity against plant pathogenic fungi. The purified compounds from the extract were examined for antifungal activity to determine the predominant antifungal compounds in the extract. Two major antifungal compounds purified were determined to be alliospiroside A (ALA) and alliospiroside B. ALA had prominent antifungal activity against a wide range of fungi. The products of acid hydrolysis of ALA showed a reduced antifungal activity, suggesting that the compound's sugar chain is essential for its antifungal activity. Fungal cells treated with ALA showed rapid production of reactive oxygen species. The fungicidal action of ALA was partially inhibited by a superoxide scavenger, Tiron, suggesting that superoxide anion generation in the fungal cells may be related to the compound's action. Inoculation experiments showed that ALA protected strawberry plants against Colletotrichum gloeosporioides , indicating that ALA has the potential to control anthracnose of the plant.
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