Enhanced Resistance to Blast Fungus and Bacterial Blight in Transgenic Rice Constitutively Expressing<i>OsSBP</i>, a Rice Homologue of Mammalian Selenium-binding Proteins

Sawada, Kazutoshi; Hasegawa, Morifumi; Tokuda, Lena; Kameyama, Junko; Kodama, Osamu; Kohchi, Takayuki; Yoshida, Kazuya; Shinmyo, Atsuhiko

doi:10.1271/bbb.68.873

Cited by 60 publications

(37 citation statements)

References 42 publications

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“…In addition to cadmium, AtSBP1 over-expressing A. thaliana plants showed increased tolerance to stress such as selenium and H 2 O 2 that also require GSH for detoxification (38). Overexpression of OsSBP1 in rice enhanced tolerance to various pathogens (17) and the importance of GSH in plant defense to biotic stress has been recently reviewed (39). These results suggest that SBP1 may share similar functions with GSH in response to stress.…”

mentioning

confidence: 96%

Biochemical and Biophysical Characterization of the Selenium-binding and Reducing Site in Arabidopsis thaliana Homologue to Mammals Selenium-binding Protein 1

Schild

Kieffer‐Jaquinod

Palencia

et al. 2014

Journal of Biological Chemistry

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Background:The selenium-binding site in selenium-binding protein (SBP) homologues was not identified. Results:The Arabidopsis thaliana SBP1 selenium-binding site was characterized as a R-S-Se(II)-S-R-type complex involving Cys 21 and Cys 22 . Conclusion: This is the first identification of the selenium-binding site in any SBP. Significance: It is an important step toward a better understanding of the link between selenium binding and function of SBP.

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mentioning

confidence: 96%

Biochemical and Biophysical Characterization of the Selenium-binding and Reducing Site in Arabidopsis thaliana Homologue to Mammals Selenium-binding Protein 1

Schild

Kieffer‐Jaquinod

Palencia

et al. 2014

Journal of Biological Chemistry

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“…For example, in Lotus japonicus, SBP1 was reported to be involved in nodule formation and function (Flemetakis et al, 2002). In rice (Oryza sativa), overexpression of SBP1 led to enhanced tolerance against different pathogens (Sawada et al, 2004).…”

mentioning

confidence: 99%

Arabidopsis Putative Selenium-Binding Protein1 Expression Is Tightly Linked to Cellular Sulfur Demand and Can Reduce Sensitivity to Stresses Requiring Glutathione for Tolerance

et al. 2009

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Selenium-Binding Protein1 (SBP1) gene expression was studied in Arabidopsis (Arabidopsis thaliana) seedlings challenged with several stresses, including cadmium (Cd), selenium {selenate [Se(VI)] and selenite [Se(IV)]}, copper (Cu), zinc (Zn), and hydrogen peroxide (H 2 O 2 ) using transgenic lines expressing the luciferase (LUC) reporter gene under the control of the SBP1 promoter. In roots and shoots of SBP1::LUC lines, LUC activity increased in response to Cd, Se(VI), Cu, and H 2 O 2 but not in response to Se(IV) or Zn. The pattern of expression of SBP1 was similar to that of PRH43, which encodes the 5#-Adenylylphosphosulfate Reductase2, a marker for the induction of the sulfur assimilation pathway, suggesting that an enhanced sulfur demand triggers SBP1 up-regulation. Correlated to these results, SBP1 promoter showed enhanced activity in response to sulfur starvation. The sulfur starvation induction of SBP1 was abolished by feeding the plants with glutathione (GSH) and was enhanced when seedlings were treated simultaneously with buthionine sulfoxide, which inhibits GSH synthesis, indicating that GSH level participates in the regulation of SBP1 expression. Changes in total GSH level were observed in seedlings challenged with Cd, Se(VI), and H 2 O 2 . Accordingly, cad2-1 seedlings, affected in GSH synthesis, were more sensitive than wild-type plants to these three stresses. Moreover, wild-type and cad2-1 seedlings overexpressing SBP1 showed a significant enhanced tolerance to Se(VI) and H 2 O 2 in addition to the previously described resistance to Cd, highlighting that SBP1 expression decreases sensitivity to stress requiring GSH for tolerance. These results are discussed with regard to the potential regulation and function of SBP1 in plants.

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“…Interestingly, in transgenic lines overexpressing a bacterial effector gene, phytoalexin accumulation was shown to increase in parallel with decreased H2O2 and increased anti-oxidant enzymes which are known ROS scavengers [75]. This phenomenon was also demonstrated in transgenic rice lines overexpressing a fungal PRR gene [56]. This may reflect a novel role for phytoalexins at later stages of infection when they have accumulated to sufficient levels so that pathogen ingress has been limited, and therefore they participate in a negative feedback "ROS-quenching" mechanism to prevent an over-reaction by the plant cell to the pathogen.…”

Section: Chemical Triggers After Pathogen Recognitionmentioning

confidence: 78%

“…Likewise, momilactone accumulation was shown to be accelerated by the overexpression of selenium-binding protein homologue gene (OsSBP), a receptor for the fungal elicitor, cerebroside from M. grisea, which triggered resistance to M. grisea and Xanthomonas oryzae pv. oryzae (Xoo) (the causal organism of bacterial blight disease) [56]. Thus, PAMPs -and PRR recognition of PAMPs -set in motion PTI-specific signalling pathways that lead to accumulation of antimicrobial secondary metabolites.…”

Section: Pathogen Recognition Events That Lead To Secondary Metabolitmentioning

confidence: 99%

Signals that stop the rot: Regulation of secondary metabolite defences in cereals

Meyer

Murray

Berger

2016

Physiological and Molecular Plant Pathology

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Plants accumulate a vast arsenal of chemically diverse secondary metabolites for defence against pathogens. This review will focus on the signal transduction and regulation of defence secondary metabolite production in five food security cereal crops: maize, rice, wheat, sorghum and oats. Recent research advances in this field have revealed novel processes and chemistry in these monocots that make this a rich field for future research.

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Enhanced Resistance to Blast Fungus and Bacterial Blight in Transgenic Rice Constitutively ExpressingOsSBP, a Rice Homologue of Mammalian Selenium-binding Proteins

Cited by 60 publications

References 42 publications

Biochemical and Biophysical Characterization of the Selenium-binding and Reducing Site in Arabidopsis thaliana Homologue to Mammals Selenium-binding Protein 1

Biochemical and Biophysical Characterization of the Selenium-binding and Reducing Site in Arabidopsis thaliana Homologue to Mammals Selenium-binding Protein 1

Arabidopsis Putative Selenium-Binding Protein1 Expression Is Tightly Linked to Cellular Sulfur Demand and Can Reduce Sensitivity to Stresses Requiring Glutathione for Tolerance

Signals that stop the rot: Regulation of secondary metabolite defences in cereals

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