Molecular Cloning, Bacterial Overexpression and Characterization of L-myo- inositol 1- Phosphate Synthase from a Monocotyledonous Resurrection Plant, Xerophyta viscosa Baker

Majee, Manoj ; Patra, Barunava ; Mundree, Sagadevan G. ; Majumder, Arun Lahiri (2005) Molecular Cloning, Bacterial Overexpression and Characterization of L-myo- inositol 1- Phosphate Synthase from a Monocotyledonous Resurrection Plant, Xerophyta viscosa Baker Journal of Plant Biochemistry and Biotechnology, 14 (2). pp. 95-99. ISSN 0971-7811

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Official URL: http://doi.org/10.1007/BF03263235

Related URL: http://dx.doi.org/10.1007/BF03263235

Abstract

L-myo-inositol 1-phosphate synthase (EC 5.5.1.4 ; MIPS ) , an evolutionary conserved enzyme-protein, catalyses the first and rate limiting step of inositol biosynthesis. Inositol and its derivatives play important roles in biological kingdom like growth regulation, membrane biogenesis, signal transduction and also acts as an osmolyte or osmoprotectant in abiotic stress tolerance. Here we report the cloning, sequencing and the characterization of the INO1 gene from Xerophyta viscosa (XINO1), a monocotyledonous resurrection plant. Nucleotide sequences of XINO1 show striking homology (70-99%) with a number of INO1 genes from plant sources particularly with the monocots. The gene is functionally identified through genetic complementation using a yeast inositol auxotrophic strain FY250. The gene is expressed in E. coli BL21, recombinant protein purified to homogeneity, biochemically characterized and compared with Oryza INO1 (RINO1) gene product. The XINO1 gene product is catalytically active in a broader range of lower temperature (between 10-40°C) than the RINO1 gene- product. This is the first report of MIPS gene from any resurrection plant.

Item Type:Article
Source:Copyright of this article belongs to Elsevier B.V.
Keywords:Inositol; MIPS; Resurrection plants; Temperature tolerance
ID Code:127834
Deposited On:14 Oct 2022 11:56
Last Modified:14 Oct 2022 11:56

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