SiHSFA2e regulated expression of SisHSP21.9 maintains chloroplast proteome integrity under high temperature stress

Singh, Roshan Kumar; Muthamilarasan, Mehanathan; Prasad, Manoj

doi:10.1007/s00018-022-04611-9

Cited by 7 publications

(4 citation statements)

References 43 publications

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“…Certain protective chaperone proteins in the chloroplasts promote the stability and protein turnover of MdEF‐Tu, as indicated by the enhanced thermotolerance in MdEF‐Tu ‐overexpressing lines in apples (Figure 1). In light of the induction of the expression of chloroplast‐localized heat shock proteins under high‐temperature stress (Hu et al., 2015; Kim et al., 2012; Singh et al., 2022), as well as the interaction between MdEF‐Tu and MdHsp70 (Figure 5), it could be argued that the enhanced thermotolerance of MdEF‐Tu ‐overexpressing lines might be associated with the increased expression of MdHsp70 , which promoted the protein turnover of MdEF‐Tu. This was consistent with the observation that the transcript level and protein abundance of MdHsp70 were higher in MdEF‐Tu ‐overexpressing lines than in WT plants (Figure 6f; Figure S5b).…”

Section: Discussionmentioning

confidence: 99%

Elongation factor MdEF‐Tu coordinates with heat shock protein MdHsp70 to enhance apple thermotolerance

Che,

Liu,

Yan

et al. 2023

The Plant Journal

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SUMMARYHigh‐temperature stress results in protein misfolding/unfolding and subsequently promotes the accumulation of cytotoxic protein aggregates that can compromise cell survival. Heat shock proteins (HSPs) function as molecular chaperones that coordinate the refolding and degradation of aggregated proteins to mitigate the detrimental effects of high temperatures. However, the relationship between HSPs and protein aggregates in apples under high temperatures remains unclear. Here, we show that an apple (Malus domestica) chloroplast‐localized, heat‐sensitive elongation factor Tu (MdEF‐Tu), positively regulates apple thermotolerance when it is overexpressed. Transgenic apple plants exhibited higher photosynthetic capacity and better integrity of chloroplasts during heat stress. Under high temperatures, MdEF‐Tu formed insoluble aggregates accompanied by ubiquitination modifications. Furthermore, we identified a chaperone heat shock protein (MdHsp70), as an interacting protein of MdEF‐Tu. Moreover, we observed obviously elevated MdHsp70 levels in 35S: MdEF‐Tu apple plants that prevented the accumulation of ubiquitinated MdEF‐Tu aggregates, which positively contributes to the thermotolerance of the transgenic plants. Overall, our results provide new insights into the molecular chaperone function of MdHsp70, which mediates the homeostasis of thermosensitive proteins under high temperatures.

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Section: Discussionmentioning

confidence: 99%

Elongation factor MdEF‐Tu coordinates with heat shock protein MdHsp70 to enhance apple thermotolerance

Che,

Liu,

Yan

et al. 2023

The Plant Journal

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“…Foxtail millet (Setaria italica) is one of the C4 panicoid crops known for its climate-resilient traits, including drought stress tolerance 26,[27][28][29][30][31] . This has made foxtail millet an attractive model to study the genetic determinants underlying drought stress tolerance 30,[32][33][34] ; however, a few studies have attempted to dissect the epigenetic regulation of drought tolerance 35,36 . Besides, no systematic and detailed investigations have been made to decipher the role of epigenetics in regulating the genes involved in drought stress responses.…”

Section: Mainmentioning

confidence: 99%

SiHDA9 interacts with SiHAT3.1 and SiHDA19 to repress dehydration responses through H3K9 deacetylation in foxtail millet

Kumar

Singh

Sharma

et al. 2023

Preprint

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Drought stress affects the growth and productivity of plants, where C4 plants can advantageously perceive and respond to the stress for their survival and reproduction. Epigenetic modifications play a prominent role in conferring drought tolerance in C4 plants; however, the molecular links between histone modifiers and their regulation are unclear. In the present study, we performed a genome-wide H3K9ac enrichment in foxtail millet (Setaria italica) and analyzed their role in regulating the expression of drought-responsive genes. The presence of H3K9ac on these genes were identified through the comparative analysis of dehydration tolerant (cv. IC4) and sensitive (IC41) cultivars of foxtail millet. A histone deacetylase, SiHDA9, showed significant upregulation in the sensitive cultivar during dehydration stress. SiHDA9 overexpression in Arabidopsis thaliana conferred higher sensitivity to dehydration/drought stress than WT plants. We found that SiHDA9 physically interacts with SiHAT3.1 and SiHDA19. This complex is recruited through the SiHAT3.1 recognition sequence on the upstream of drought-responsive genes (SiRAB18, SiRAP2.4, SiP5CS2, SiRD22, SiPIP1;4, and SiLHCB2.3) to decrease H3K9 acetylation levels. The modulations in H3K9ac levels cause repression of gene expression and induce drought-sensitivity in the sensitive cultivar. Overall, the study provides mechanistic insights into SiHDA9-mediated regulation of drought stress response in foxtail millet.

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Section: Mainmentioning

confidence: 99%

Histone deacetylase 9 interacts with SiHAT3.1 and SiHDA19 to repress dehydration responses through H3K9 deacetylation in foxtail millet

Kumar,

Singh,

Kumar Singh

et al. 2023

Journal of Experimental Botany

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Climate change inflicts several stresses on plants, of which dehydration stress severely affects growth and productivity. C4 plants possess better adaptability to dehydration stress; however, the role of epigenetic modifications underlying this trait is unclear. Particularly, the molecular links between histone modifiers and their regulation remain elusive. In this study, genome-wide H3K9 acetylation (H3K9ac) enrichment using ChIP-seq was performed in two foxtail millet cultivars contrastingly differing in dehydration tolerance (IC403579; cv. IC4 – tolerant, and IC480117; cv. IC41 – sensitive). It revealed that a histone deacetylase, SiHDA9, was significantly up-regulated in the sensitive cultivar. Further characterization indicated that SiHDA9 interacts with SiHAT3.1 and SiHDA19 to form a repressor complex. SiHDA9 might be recruited through the SiHAT3.1 recognition sequence onto the upstream of dehydration-responsive genes to decrease H3K9 acetylation levels. The silencing of SiHDA9 resulted in the up-regulation of crucial genes, namely, SiRAB18, SiRAP2.4, SiP5CS2, SiRD22, SiPIP1;4 and SiLHCB2.3, which imparted dehydration tolerance in the sensitive cultivar (IC41). Overall, the study provides mechanistic insights into SiHDA9-mediated regulation of dehydration stress response in foxtail millet.

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SiHSFA2e regulated expression of SisHSP21.9 maintains chloroplast proteome integrity under high temperature stress

Cited by 7 publications

References 43 publications

Elongation factor MdEF‐Tu coordinates with heat shock protein MdHsp70 to enhance apple thermotolerance

Elongation factor MdEF‐Tu coordinates with heat shock protein MdHsp70 to enhance apple thermotolerance

SiHDA9 interacts with SiHAT3.1 and SiHDA19 to repress dehydration responses through H3K9 deacetylation in foxtail millet

Histone deacetylase 9 interacts with SiHAT3.1 and SiHDA19 to repress dehydration responses through H3K9 deacetylation in foxtail millet

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