Ectopic expression of the ABA-inducible dehydration-responsive chickpea L-myo-inositol 1-phosphate synthase 2 (CaMIPS2) in Arabidopsis enhances tolerance to salinity and dehydration stress

dc.contributor.authorKaur, Harmeet
dc.contributor.authorVerma, Pooja
dc.contributor.authorPetla, Bhanu Prakash
dc.contributor.authorRao, Venkateswara
dc.contributor.authorSaxena, Saurabh C.
dc.contributor.authorMajee, Manoj
dc.date.accessioned2015-11-05T05:17:00Z
dc.date.available2015-11-05T05:17:00Z
dc.date.issued2013
dc.descriptionAccepted date: 2 October 2012en_US
dc.description.abstractMyo-inositol participates in many different aspects of plant physiology and myo-inositol 1-phosphate synthase (MIPS; EC 5.5.1.4) catalyzes the rate limiting step of inositol biosynthetic pathway. Chickpea (Cicer arietinum), a drought-tolerant leguminous crop plant, is known to accumulate increased inositol during dehydration stress. Previously, we reported two differentially expressed divergent genes (CaMIPS1 and CaMIPS2) encoding two MIPS isoforms in chickpea. In this communication, we demonstrated that CaMIPS2 is an early dehydration-responsive gene and is also rapidly induced by exogenous ABA application, while CaMIPS1 expression is not much influenced by dehydration or ABA. The regulation of expression of these two genes has been studied by examining their promoter activity through GUS reporter gene and differential promoter activity has been observed. Moreover, unlike CaMIPS1 promoter, CaMIPS2 promoter contains CRT/DRE cis-regulatory element which seems to play a key role in dehydration-induced expression of CaMIPS2. Furthermore, CaMIPS1 and CaMIPS2 have been successfully complemented and shown to repair the defect of seedling growth and altered seed phenotype of Atmips1 mutant. Moreover, Arabidopsis transgenic plants overexpressing CaMIPS1 or CaMIPS2 exhibit improved tolerance to salinity and dehydration stresses and such tolerance of transgenic plants is correlated with their elevated level of inositol. Remarkably, CaMIPS2 transgenic lines perform better in all attributes than CaMIPS1 transformants under such stress conditions, due to comparatively unabated production of inositol by CaMIPS2 enzyme, as this enzyme retains significant activity under stress conditions.en_US
dc.description.sponsorshipThis work was supported by the grant (BT/ PR12919/AGR/02/676/2009) from Department of Biotechnology, Government of India. H.K. B.P, V.R and P.V. thank Council of Scientific and Industrial Research and University Grant Commission, Government of India, for research fellowships. We are grateful to Dr. Glenda Gillaspy, Virginia Tech., USA, for providing us the Atmips1 mutant (Atmips1-2, SALK_023626). We are grateful to Dr. S.K. Pattanaik, University of Kentucky, for providing pKYLX 70:GUS vector.en_US
dc.identifier.citationPlanta, 237(1): 321-335en_US
dc.identifier.doi10.1007/s00425-012-1781-0en_US
dc.identifier.issn1432-2048
dc.identifier.officialurlhttp://link.springer.com/article/10.1007%2Fs00425-012-1781-0en_US
dc.identifier.urihttp://172.16.0.77:8080/jspui/handle/123456789/319
dc.language.isoen_USen_US
dc.publisherSpringeren_US
dc.subjectAbiotic stressesen_US
dc.subjectFunctional complementationen_US
dc.subjectGene duplicationen_US
dc.subjectPromoter analysisen_US
dc.subjectSubfunctionalizationen_US
dc.subjectTransgenicen_US
dc.titleEctopic expression of the ABA-inducible dehydration-responsive chickpea L-myo-inositol 1-phosphate synthase 2 (CaMIPS2) in Arabidopsis enhances tolerance to salinity and dehydration stressen_US
dc.typeArticleen_US

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