Molecular cloning, characterization, heterologous expression and in-silico analysis of disordered boiling soluble stress-responsive wBsSRP protein from drought tolerant wheat cv.PBW 175

Rakhra, Gurmeen; Kaur, Tarandeep; Vyas, Dhiraj; Sharma, Arun Dev; Singh, Jatinder; Ram, Gobind

doi:10.1016/j.plaphy.2016.12.017

Cited by 12 publications

(6 citation statements)

References 31 publications

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“…As IDPs may show extreme variations in amino acid composition and physical properties, the use of more accurate quantification methods, such as ninhydrin and Qubit in combination with an absolute method, is recommended to draw more reliable conclusions about their structure. In vivo assays using E. coli have successfully demonstrated the protective role of LEA proteins upon stress (Zhang et al, 2014; Drira et al, 2015; Gao and Lan, 2016; Hu et al, 2016; Ling et al, 2016; Liu et al, 2016; Shi et al, 2016; Boothby et al, 2017; Jiang et al, 2017; Rakhra et al, 2017; Saucedo et al, 2017; Wang et al, 2017; Zhou et al, 2017). We found that several XsLEAs are able to improve bacterial growth under salt and osmotic stress, and the strains expressing XsLEA1-8 presented a faster stress recovery.…”

Section: Discussionmentioning

confidence: 99%

Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo

et al. 2019

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Late embryogenesis abundant (LEA) proteins are essential to the ability of resurrection plants and orthodox seeds to protect the subcellular milieu against irreversible damage associated with desiccation. In this work, we investigated the structure and function of six LEA proteins expressed during desiccation in the monocot resurrection species Xerophyta schlechteri (XsLEAs). In silico analyses suggested that XsLEAs are hydrophilic proteins with variable intrinsically disordered protein (IDP) properties. Circular dichroism (CD) analysis indicated that these proteins are mostly unstructured in water but acquire secondary structure in hydrophobic solution, suggesting that structural dynamics may play a role in their function in the subcellular environment. The protective property of XsLEAs was demonstrated by their ability to preserve the activity of the enzyme lactate dehydrogenase (LDH) against desiccation, heat and oxidative stress, as well as growth of Escherichia coli upon exposure to osmotic and salt stress. Subcellular localization analysis indicated that XsLEA recombinant proteins are differentially distributed in the cytoplasm, membranes and nucleus of Nicotiana benthamiana leaves. Interestingly, a LEA_1 family protein (XsLEA1-8), showing the highest disorder-to-order propensity and protective ability in vitro and in vivo, was also able to enhance salt and drought stress tolerance in Arabidopsis thaliana. Together, our results suggest that the structural plasticity of XsLEAs is essential for their protective activity to avoid damage of various subcellular components caused by water deficit stress. XsLEA1-8 constitutes a potential model protein for engineering structural stability in vitro and improvement of water-deficit stress tolerance in plants.

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Section: Discussionmentioning

confidence: 99%

Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo

et al. 2019

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“…One microliter of cDNA was used as a template for PCR amplification of CDS (protein coding sequence) encoding hydrophilic protein having K-segment with a pair of gene-specific primers ( WZY2 gene, LEA II family gene; accession no: EU395844) (Fig. 1) following Rakhra et a (2017) [2]. The gene was successfully accessioned in EMBL GenBank with accession number LN832556.…”

Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

Data set of in-silico analysis and 3D modelling of boiling stable stress-responsive protein from drought tolerant wheat

Sharma¹,

Rakhra²,

Vyas

2019

Data in Brief

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Boiling stable proteins are widespread, evolutionary conserved proteins from several kingdoms including plants, fungi and bacteria. Accumulation evidences in response to dehydration, suggest a wide spread adaptation and an evolutionary role of these protein families to protect cellular structures from water loss effects in a wide range of water potentials. Boiling stable proteins, although represents just 0.1% of total plant proteins, resist coagulation upon boiling and believed to be involved in water stress adaptation in plants. The present data profiles in-silico analysis of cloned boiling stable protein encoding gene wBsSRP from drought tolerant cultivar of wheat. The data presented here was of a gene isolated from total RNA/mRNA samples of wheat variety PBW 175 subjected to drought stress. The gene is available with EMBL data repository with accession number LN832556.

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“…DHNs protect biomacromolecules by nonspecific binding mode, called 'molecular shield' (Hughes et al, 2013). Several studies have reported that under different environmental stresses, DNH is able to directly bind to the metal ions to reduce the ROS, prevent membrane and protein aggregation (Halder et al, 2016(Halder et al, , 2017Rakhra et al, 2017), and protect the integrity of biomolecules (Abdul et al, 2021). In our previous studies, two DHNs (ApSK 3 and ApY 2 SK 2 ) as protective proteins were screened in embryogenic callus (EC) of Agapanthus praecox during cryopreservation by combined RNA-seq and proteomics analysis.…”

Section: Introductionmentioning

confidence: 99%

In vivo protective effect of late embryogenesis abundant protein (ApSK3 dehydrin) on Agapanthus praecox to promote post-cryopreservation survival

HUANG¹,

Deng²,

Sheng³

et al. 2022

Biocell

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Dehydrins (DHNs), as members of the late embryogenesis abundant protein family, play critical roles in the protection of seeds from dehydration and plant adaptation to multiple abiotic stresses. Vitrification is a basic method in plant cryopreservation and is characterized by forming a glassy state to prevent lethal ice crystals produced during cryogenic storage. In this study, ApSK 3 type DHN was genetically transformed into embryogenic calluses (EC) of Agapanthus praecox by overexpression (OE) and RNA interference (RNAi) techniques to evaluate the in vivo protective effect of DHNs during cryopreservation. The cell viability showed a completely opposite trend in OE and RNAi cell lines, the cell relative death ratio was decreased by 20.0% in ApSK 3 -OE EC and significantly increased by 66.15% in ApSK 3 -RNAi cells after cryopreservation. Overexpression of ApSK 3 increased the content of non-enzymatic antioxidants (AsA and GSH) and up-regulated the expression of CAT, SOD, POD, and GPX genes, while ApSK 3 -RNAi cells decreased antioxidant enzyme activities and FeSOD, POD, and APX genes expression during cryopreservation. These findings suggest that ApSK 3 affects ROS metabolism through chelating metal ions (Cu 2+ and Fe 3+ ), alleviates H 2 O 2 and OH• excessive generation, activates the antioxidant system, and improves cellular REDOX balance and membrane lipid peroxidation damage of plant cells during cryopreservation. DHNs can effectively improve cell stress tolerance and have great potential for in vivo or in vitro applications in plant cryopreservation.

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Molecular cloning, characterization, heterologous expression and in-silico analysis of disordered boiling soluble stress-responsive wBsSRP protein from drought tolerant wheat cv.PBW 175

Cited by 12 publications

References 31 publications

Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo

Structural Plasticity of Intrinsically Disordered LEA Proteins from Xerophyta schlechteri Provides Protection In Vitro and In Vivo

Data set of in-silico analysis and 3D modelling of boiling stable stress-responsive protein from drought tolerant wheat

In vivo protective effect of late embryogenesis abundant protein (ApSK3 dehydrin) on Agapanthus praecox to promote post-cryopreservation survival

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