SmLEA2, a gene for late embryogenesis abundant protein isolated from Salvia miltiorrhiza, confers tolerance to drought and salt stress in Escherichia coli and S. miltiorrhiza

Wang, Huaiqin; Wu, Yucui; Yang, Xin; Guo, Xinfeng; Cao, Xiaoyan

doi:10.1007/s00709-016-0981-z

Cited by 33 publications

(23 citation statements)

References 48 publications

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“…Extensive studies focusing on an organism's adaptation against harsh environments have highlighted the importance of late embryogenesis abundant (LEA) proteins found in many species ranging from plants and animals to microbes as they were highly induced in dry environments (Tompa, ; Gal et al ., ; Tolleter et al ., ; Chakrabortee et al ., ; Hand et al ., ). The accumulated LEA proteins act in a chaperone‐like manner to protect the organisms from various stresses, for example, salt, desiccation and oxidation (Hoekstra et al ., ; Shimizu et al ., ; Cuevas‐Velazquez et al ., ; Wang et al ., ). Further bioinformatic and structural analyses revealed that 11‐mer motifs specific to group 3 LEA (G3LEA) proteins (HD) might be the crucial regions determining their whole‐length functions (Dure, ; Xue et al ., ).…”

Section: Discussionmentioning

confidence: 97%

“…Escherichia coli recombinant strain cultures were induced with IPTG at a final optimal concentration of 0.1 mM for 4 h, and the cells were desiccated and treated with H 2 O 2 as previously described (Rajpurohit and Misra, ; Jiang et al ., ; Wang et al ., ). Different serial dilutions of these cells were plated onto LB agar plates and incubated at 37°C for 1 day before colonies were observed and counted.…”

Section: Methodsmentioning

confidence: 97%

“…Long‐term investigations into the molecular mechanism of desiccation resistance emphasized late embryogenesis abundant (LEA) proteins, which account for more than 4% of cellular proteins in cotton orthodox seeds (Hughes and Galau, ; Roberts et al ., ; Shimizu et al ., ). Furthermore, many reports have revealed that the heterologous expression of LEA proteins can significantly improve recipient oxidation resistance (Liu and Zheng, ; Kovacs et al ., ; Shih et al ., ; Sasaki et al ., ; Wang et al ., ).…”

Section: Introductionmentioning

confidence: 97%

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Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms

Liu

Zhang

Han

et al. 2019

Microbial Biotechnology

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Summary Late embryogenesis abundant (LEA) proteins play a protective role during desiccation and oxidation stresses. LEA3 proteins are a major group characterized by a hydrophilic domain (HD) with a highly conserved repeating 11‐amino acid motif. We compared four different HD orthologs from distant organisms: (i) DrHD from the extremophilic bacterium Deinococcus radiodurans; (ii) CeHD from the nematode Caenorhabditis elegans; (iii) YlHD from the yeast Yarrowia lipolytica; and (iv) BnHD from the plant Brassica napus. Circular dichroism spectroscopy showed that all four HDs were intrinsically disordered in phosphate buffer and then folded into α‐helical structures with the addition of glycerol or trifluoroethanol. Heterologous HD expression conferred enhanced desiccation and oxidation tolerance to Escherichia coli. These four HDs protected the enzymatic activities of lactate dehydrogenase (LDH) by preventing its aggregation under desiccation stress. The HDs also interacted with LDH, which was intensified by the addition of hydrogen peroxide (H2O2), suggesting a protective role in a chaperone‐like manner. Based on these results, the HDs of LEA3 proteins show promise as protectants for desiccation and oxidation stresses, especially DrHD, which is a potential ideal stress‐response element that can be applied in synthetic biology due to its extraordinary protection and stress resistance ability.

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Section: Discussionmentioning

confidence: 97%

Section: Methodsmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 97%

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Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms

Liu

Zhang

Han

et al. 2019

Microbial Biotechnology

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“…Besides, E. coli cells show better growth under stress treatments by introduction of many plant genes related to stresses [21,28,[38][39][40], suggesting that some protective mechanisms might be common for both prokaryote and eukaryote cells under stress conditions. To explore the growth of BL/CsCAT3 and BL/ pET32a under different stresses, we first investigated the cell viability of E. coli recombinants under NaCl and sorbitol treatments.…”

Section: Overexpression Of Cscat3 In E Coli Enhanced Growth Under Abmentioning

confidence: 99%

CsCAT3, a catalase gene from Cucumis sativus, confers resistance to a variety of stresses to Escherichia coli

Zhou

Liu

Yang

et al. 2017

Biotechnology & Biotechnological Equipment

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Catalase (CAT) is a key scavenging enzyme for the degradation of hydrogen peroxide (H 2 O 2 ) and plays an important role in the tolerance to diverse abiotic stresses in many different organisms. In this study, we characterized the function of a catalase gene (CsCAT3) previously isolated from Cucumis sativus in the defence against a variety of stresses. Protein alignment and phylogenetic analysis revealed that CsCAT3 was clustered in the dicot group and shared 41%-95% identity with other plant CATs. Expression analyses revealed that the expression of CsCAT3 was induced by diverse abiotic stresses such as heat, polyethylene glycol, cold and NaCl treatment, as well as by signalling molecules such as abscisic acid (ABA) and H 2 O 2 . An Escherichia coli heterologous expression system was constructed to characterize the function of CsCAT3 in vitro. Its overexpression in E. coli could increase the tolerance to heat, cold, salinity and osmotic conditions. These results indicate that CsCAT3 plays important roles in abiotic stress tolerance and that CsCAT3 confers tolerance in E. coli recombinants against abiotic stresses, which may be due to the increased activities of antioxidant enzymes that reduce the oxidative damage caused by stress conditions.

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“…Because their quality and quantity strongly depends on environmental stresses, such as drought, cold, and salinity, this results in a lower yield of S. miltiorrhiza ( Akula, 2011 ; Liu et al, 2011 ; Zhao et al, 2014 ). Several studies have reported that by overexpressing SmLEA2 , AtDREB1A , AtDREB1B , and AtDREB1C , the salt and drought tolerance of transgenic S. miltiorrhiza was improved ( Wei et al, 2016a , b , 2017 ; Wang et al, 2017 ). More of such genes should be investigated via genetic engineering methods, as it could assist in breeding new varieties of S. miltiorrhiza that have a higher content of active ingredients and a stronger tolerance to stresses.…”

Section: Introductionmentioning

confidence: 99%

The Protein Kinase SmSnRK2.6 Positively Regulates Phenolic Acid Biosynthesis in Salvia miltiorrhiza by Interacting with SmAREB1

et al. 2017

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Subclass III members of the sucrose non-fermenting-1-related protein kinase 2 (SnRK2) play essential roles in both the abscisic acid signaling and abiotic stress responses of plants by phosphorylating the downstream ABA-responsive element (ABRE)-binding proteins (AREB/ABFs). This comprehensive study investigated the function of new candidate genes, namely SmSnRK2.3, SmSnRK2.6, and SmAREB1, with a view to breeding novel varieties of Salvia miltiorrhiza with improved stress tolerance stresses and more content of bioactive ingredients. Exogenous ABA strongly induced the expression of these genes. PlantCARE predicted several hormones and stress response cis-elements in their promoters. SmSnRK2.6 and SmAREB1 showed the highest expression levels in the leaves of S. miltiorrhiza seedlings, while SmSnRK2.3 exhibited a steady expression in their roots, stems, and leaves. A subcellular localization assay revealed that both SmSnRK2.3 and SmSnRK2.6 were located in the cell membrane, cytoplasm, and nucleus, whereas SmAREB1 was exclusive to the nucleus. Overexpressing SmSnRK2.3 did not significantly promote the accumulation of rosmarinic acid (RA) and salvianolic acid B (Sal B) in the transgenic S. miltiorrhiza hairy roots. However, overexpressing SmSnRK2.6 and SmAREB1 increased the contents of RA and Sal B, and regulated the expression levels of structural genes participating in the phenolic acid-branched and side-branched pathways, including SmPAL1, SmC4H, Sm4CL1, SmTAT, SmHPPR, SmRAS, SmCHS, SmCCR, SmCOMT, and SmHPPD. Furthermore, SmSnRK2.3 and SmSnRK2.6 interacted physically with SmAREB1. In summary, our results indicate that SmSnRK2.6 is involved in stress responses and can regulate structural gene transcripts to promote greater metabolic flux to the phenolic acid-branched pathway, via its interaction with SmAREB1, a transcription factor. In this way, SmSnRK2.6 contributes to the positive regulation of phenolic acids in S. miltiorrhiza hairy roots.

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SmLEA2, a gene for late embryogenesis abundant protein isolated from Salvia miltiorrhiza, confers tolerance to drought and salt stress in Escherichia coli and S. miltiorrhiza

Cited by 33 publications

References 48 publications

Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms

Functional assessment of hydrophilic domains of late embryogenesis abundant proteins from distant organisms

CsCAT3, a catalase gene from Cucumis sativus, confers resistance to a variety of stresses to Escherichia coli

The Protein Kinase SmSnRK2.6 Positively Regulates Phenolic Acid Biosynthesis in Salvia miltiorrhiza by Interacting with SmAREB1

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