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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

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Title 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
 
Creator Kaur, Harmeet
Verma, Pooja
Petla, Bhanu Prakash
Rao, Venkateswara
Saxena, Saurabh C.
Majee, Manoj
 
Subject Abiotic stresses
Functional complementation
Gene duplication
Promoter analysis
Subfunctionalization
Transgenic
 
Description Accepted date: 2 October 2012
Myo-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.
This 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.
 
Date 2015-11-05T05:17:00Z
2015-11-05T05:17:00Z
2013
 
Type Article
 
Identifier Planta, 237(1): 321-335
1432-2048
http://172.16.0.77:8080/jspui/handle/123456789/319
http://link.springer.com/article/10.1007%2Fs00425-012-1781-0
10.1007/s00425-012-1781-0
 
Language en_US
 
Publisher Springer