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Published on February 24, 2006; 10.1104/pp.105.075150

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Received December 6, 2005
Returned for revision December 23, 2005
Accepted January 5, 2006

An insight into the molecular basis of salt-tolerance of L-myo-inositol 1-phosphate synthase (PcINO1 ) from Porteresia coarctata (Roxb.) Tateoka, a halophytic wild rice

Krishnarup Ghosh Dastidar , Susmita Maitra , Lily Goswami , Debjani Roy , Kali Pada Das , and Arun Lahiri Majumder *

Plant Molecular and Cellular Genetics, Bose Institute (Centenary Building), P-1/12, C.I.T Scheme-VIIM, Kolkata: 700 054, India
Plant Molecular and Cellular Genetics, Bose Institute (Centenary Building), P-1/12, C.I.T Scheme-VIIM, Kolkata: 700 054, India
Bioinformatics Center, Bose Institute (Centenary Building), P-1/12, C.I.T Scheme-VIIM, Kolkata: 700 054, India
Department of Chemistry, Bose Institute (Centenary Building), P-1/12, C.I.T Scheme-VIIM, Kolkata: 700 054, India

* Corresponding author; email: lahiri{at}bic.boseinst.ernet.in.

The molecular basis of salt-tolerance of L-myo-inositol 1-phosphate synthase, (EC 5.5.1.4, MIPS) from Porteresia coarctata (Roxb.) Tateoka (PcINO1, AF412340) earlier reported from this laboratory has been analyzed by in vitro mutant and hybrid generation and subsequent biochemical and biophysical studies of the recombinant proteins. A 37 amino acid (aa) stretch between Trp-174 and Ser-210 has been confirmed as the "salt-tolerance determinant" domain in PcINO1 both by loss or gain of salt-tolerance by either deletion or by addition to salt-sensitive MIPS(s) of Oryza (OsINO1) and Brassica juncea (BjINO1). This was further verified by growth analysis under salt environment of Schizosaccharomyces pombe transformed with the various gene constructs and studies on the differential behavior of mutant and wild proteins by tryptophan fluorescence, aggregation and CD spectra in presence of salt. Bis-ANS binding experiment revealed a lower hydrophobic surface on PcINO1 than OsINO1 contributed by this 37 aa stretch explaining the differential behavior of OsINO1 and PcINO1 both with respect to their enzymatic functions and thermodynamic stability in high salt environment. Detailed amino acid sequence comparison and modeling studies revealed the interposition of polar and charged residues and a well-connected hydrogen-bonding network formed by Ser and Thr in this stretch of PcINO1. On the contrary, hydrophobic residues clustered in two continuous stretches in the corresponding region of OsINO1 form a strong hydrophobic patch on the surface. It is conceivable that salt-tolerant MIPS proteins may be designed out of the salt-sensitive plant MIPS proteins by replacement of the corresponding amino acid stretch by the designated 37 aa stretch of PcINO1.




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