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Cloning of Arabidopsis thaliana phosphatidylinositol synthase and functional expression in the yeast pis mutant.
- Source :
- Plant Molecular Biology; Mar2000, Vol. 42 Issue 5, p757-764, 8p
- Publication Year :
- 2000
-
Abstract
- It is believed that phosphatidylinositol (PI) metabolism plays a central role in signalling pathways in both animals and higher plants. PI is synthesized from CDP-diacylglycerol (CDP-DG) and myo-inositol by phosphatidylinositol synthase (PI synthase, EC 2.7.8.11). Here we report the identification of a plant cDNA ( AtPIS1) encoding a 26 kDa PI synthase from Arabidopsis thaliana. The plant enzyme as deduced from its cDNA sequence shares 35–41% identical amino acids with PI synthases from Saccharomyces cerevisiae and mammals. AtPIS1 functionally complements a mutant of S. cerevisiae with a lesion in PI synthase, and recombinant AtPIS1 protein present in yeast membranes strongly depends on the two principal substrates, myo-inositol and CDP-DG, and requires Mg<superscript>2+</superscript> ions for full activity. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01674412
- Volume :
- 42
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Plant Molecular Biology
- Publication Type :
- Academic Journal
- Accession number :
- 49861325
- Full Text :
- https://doi.org/10.1023/A:1006308909105