EGY3 mediates chloroplastic ROS homeostasis and promotes retrograde signaling in response to salt stress in Arabidopsis

Zhuang, Yong; Wei, Ming; Ling, Chengcheng; Liu, Yangxuan; Amin, Abdul Karim; Li, Penghui; Li, Pengwei; Hu, Xufan; Bao, Huaxu; Huo, Heqiang; Smalle, Jan; Wang, Songhu

doi:10.1016/j.celrep.2021.109384

Cited by 38 publications

(33 citation statements)

References 105 publications

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“…This result correlates with hydrogen peroxide concentrations, which are lower in egy3 mutant exposed to analyzed stress conditions. These findings agree with the previous findings concerning the EGY3 role in the salt-stress response (Zhuang et al, 2021). The exposition to high-temperature stress, however, did not cause any statistically significant differences in the abundance of CSD2 protein in egy3 mutants; however, the lower, than in WT plants, the concentration of hydrogen peroxide was observed.…”

Section: Locussupporting

confidence: 92%

“…It was shown that the EGY3 pseudoprotease participates in the stabilization of a chloroplastic copper/zinc superoxide dismutase (CSD2) in response to salt stress (Zhuang et al, 2021). Our results indicate that in response to high light stress, the presence of EGY3 pseudoprotease reassures a higher abundance of CSD2.…”

Section: Locusmentioning

confidence: 61%

“…In plants, grown in standard laboratory conditions, the lack of the protease does not lead to any visible phenotype changes; however, in egy3 mutants, the increased value of the non-photochemical quenching and slower recovery rate after photoinhibitory treatment were observed (Adamiec et al, 2019). It has been also suggested that EGY3 may participate in response to salt stress by promoting the copper/zinc superoxide dismutase 2 (CSD2) stability and H 2 O 2mediated chloroplastic retrograde signaling (Zhuang et al, 2021). The transcriptional data indicate also that expression of the gene encoding EGY3 is significantly increased under the hightemperature treatment.…”

Section: Introductionmentioning

confidence: 99%

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Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition

et al. 2022

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The EGY3 is a pseudoprotease, located in the thylakoid membrane, that shares homology with the family of site-2-proteases (S2P). Although S2P proteases are present in the cells of all living organisms, the EGY3 was found only in plant cells. The sequence of the pseudoprotease is highly conserved in the plant kingdom; however, little is known about its physiological importance. Results obtained with real-time PCR indicated that the expression of the EGY3 gene is dramatically induced during the first few hours of exposure to high light and high-temperature stress. The observed increase in transcript abundance correlates with protein accumulation level, which indicates that EGY3 participates in response to both high-temperature and high light stresses. The lack of the pseudoprotease leads, in both stresses, to lower concentrations of hydrogen peroxide. However, the decrease of chloroplast copper/zinc superoxide dismutase 2 level was observed only during the high light stress. In both analyzed stressful conditions, proteins related to RubisCO folding, glycine metabolism, and photosystem I were identified as differently accumulating in egy3 mutant lines and WT plants; however, the functional status of PSII during analyzed stressful conditions remains very similar. Our results lead to a conclusion that EGY3 pseudoprotease participates in response to high light and high-temperature stress; however, its role is associated rather with photosystem I and light-independent reactions of photosynthesis.

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Section: Locussupporting

confidence: 92%

Section: Locusmentioning

confidence: 61%

Section: Introductionmentioning

confidence: 99%

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Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition

et al. 2022

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“…According to our data, Os03g0729000 was significantly up-regulated after drought stress. Furthermore, we inferred by NR annotation that Os03g0729000 was likely to be zinc metalloprotease EGY3, which can promote the stability of chloroplast copper/zinc superoxide dismutase and improve stress resistance when plants are stressed [ 33 ]. In addition, we predicted that 28 lncRNAs could target Os03g0729000 (EGY3), and all of them were up-regulated.…”

Section: Discussionmentioning

confidence: 99%

Research on lncRNA related to drought resistance of Shanlan upland rice

et al. 2022

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Background Drought has become the major abiotic stress that causes losses in rice yields and consequently is one of the main environmental factors threatening food security. Long non-coding RNA (lncRNA) is known to play an important role in plant response to drought stress, while the mechanisms of competing endogenous RNA (ceRNA) in drought resistance in upland rice have been rarely reported. Results In our study, a total of 191 lncRNAs, 2115 mRNAs and 32 miRNAs (microRNAs) were found by strand-specific sequencing and small RNA sequencing to be differentially expressed in drought-stressed rice. Functional analysis of results indicate that they play important roles in hormone signal transduction, chlorophyll synthesis, protein synthesis and other pathways. Construction of a ceRNA network revealed that MSTRG.28732.3 may interact with miR171 in the chlorophyll biosynthesis pathway and affect the ability of plants to withstand drought stress by regulating Os02g0662700, Os02g0663100 and Os06g0105350. The accuracy of the regulatory network was verified by qRT-PCR. Conclusion Our results provide a theoretical basis for future studies on the potential function of lncRNA in plant drought resistance, and they provide new genetic resources for drought-resistant rice breeding.

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“…Several abiotic stresses enhance ROS accumulation in the chloroplast, a major site of ROS production 22 , 41 , 42 . Recently, ROS was proposed to act as a retrograde signal to influence plant responses to abiotic stresses, particularly for plant tolerance to salt stress 43 . This raises an exciting question of whether chloroplastic ROS could act as a retrograde signal under Fe deficiency to regulate the expression of nuclear PRGs.…”

Section: Discussionmentioning

confidence: 99%

Interdependent iron and phosphorus availability controls photosynthesis through retrograde signaling

et al. 2021

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Iron deficiency hampers photosynthesis and is associated with chlorosis. We recently showed that iron deficiency-induced chlorosis depends on phosphorus availability. How plants integrate these cues to control chlorophyll accumulation is unknown. Here, we show that iron limitation downregulates photosynthesis genes in a phosphorus-dependent manner. Using transcriptomics and genome-wide association analysis, we identify two genes, PHT4;4 encoding a chloroplastic ascorbate transporter and bZIP58, encoding a nuclear transcription factor, which prevent the downregulation of photosynthesis genes leading to the stay-green phenotype under iron-phosphorus deficiency. Joint limitation of these nutrients induces ascorbate accumulation by activating expression of an ascorbate biosynthesis gene, VTC4, which requires bZIP58. Furthermore, we demonstrate that chloroplastic ascorbate transport prevents the downregulation of photosynthesis genes under iron-phosphorus combined deficiency through modulation of ROS homeostasis. Our study uncovers a ROS-mediated chloroplastic retrograde signaling pathway to adapt photosynthesis to nutrient availability.

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EGY3 mediates chloroplastic ROS homeostasis and promotes retrograde signaling in response to salt stress in Arabidopsis

Cited by 38 publications

References 105 publications

Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition

Stress-related expression of the chloroplast EGY3 pseudoprotease and its possible impact on chloroplasts’ proteome composition

Research on lncRNA related to drought resistance of Shanlan upland rice

Interdependent iron and phosphorus availability controls photosynthesis through retrograde signaling

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