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Structure of RNA-interacting cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants.

ABSTRACT: Soil salinity problems are widespread around the globe with increased risk of spreading over the years. The fungus Piriformospora indica, identified in Indian Thar desert, colonizes the roots of monocotyledon plants and provides resistance towards biotic as well as abiotic stress conditions. We have identified a cyclophilin A-like protein from P. indica (PiCypA), which shows higher expression levels during salinity stress. The transgenic tobacco plants overexpressing PiCypA develop osmotic tolerance and exhibit normal growth under osmotic stress conditions. The crystal structure and NMR spectroscopy of PiCypA show a canonical cyclophilin like fold exhibiting a novel RNA binding activity. The RNA binding activity of the protein and identification of the key residues involved in the RNA recognition is unique for this class of protein. Here, we demonstrate for the first time a direct evidence of countering osmotic stress tolerance in plant by genetic modification using a P. indica gene.

SUBMITTER: Trivedi DK

PROVIDER: S-EPMC3801112 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Structure of RNA-interacting cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants.

Trivedi Dipesh Kumar DK Bhatt Harshesh H Pal Ravi Kant RK Tuteja Renu R Garg Bharti B Johri Atul Kumar AK Bhavesh Neel Sarovar NS Tuteja Narendra N

Scientific reports 20131021

Soil salinity problems are widespread around the globe with increased risk of spreading over the years. The fungus Piriformospora indica, identified in Indian Thar desert, colonizes the roots of monocotyledon plants and provides resistance towards biotic as well as abiotic stress conditions. We have identified a cyclophilin A-like protein from P. indica (PiCypA), which shows higher expression levels during salinity stress. The transgenic tobacco plants overexpressing PiCypA develop osmotic toler ...[more]

PMID: 24141523

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Project description:BackgroundCyclophilins (CyP), conserved in all genera, are known to have regulatory responses of various cellular processes including stress tolerance. Interestingly, CyP has a crucial role as peptidyl-prolyl cis-trans isomerases (PPIases). Our earlier in silico based approach resulted into the identification of cyclophilin family from rice, Arabidopsis and yeast. In our recent report, we discovered a new OsCYP-25 from rice. Here, we identified a novel cyclophylin A-like protein (PiCyP) from Piriformospora indica which is responsible for abiotic stress tolerance in E. coli.ResultsCyclophylin A-like protein (CyPA) (accession number GQ214003) was selected from cDNA library. The genomic organization CyPA revealed a 1304 bp of CyPA in P. indica genome, showing 10 exons and 9 introns. Further, CyPA was evident in PCR with gDNA and cDNA and Southern blot analysis. The phylogenetic examination of CyPA of P. indica showed that it is closed to human cyclophilin. The uniqueness of PiCyPA protein was apparent in western blot study. Kinetics of purified PiCyPA protein for its PPIas activity was determined via first order rate constant (0.104 s-1) in the presence of 1 μg of PiCyPA, with increasing PiCyPA concentration, in the presence of cyclosporin A (CsA) and the inhibition constant (4.435 nM) of CsA for inhibition of PiCyPA. The differential response of E. coli harbouring pET28a-PiCypA was observed for their different degree of tolerance to different abiotic stresses as compared to empty pET28a vector.ConclusionsOverexpression of PiCyPA protein E. coli cells confer enhanced tolerance to wide range of abiotic stresses. Thus, this study provides the significance of PiCypA as a molecular chaperone which advanced cellular stress responses of E. coli cells under adverse conditions, and it, furthermore, confirms the mounting the sustainability of E. coli for exploitation in recombinant proteins production. Additionally, the PiCyPA gene cooperates substantial functions in cellular network of stress tolerance mechanism, essentially required for various developmental stages, and might be a potential paramount candidate for crop improvement and its sustainable production under adverse conditions.

Dataset Information

Structure of RNA-interacting cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants.

Publications

Structure of RNA-interacting cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants.

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