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Cloning of Arabidopsis thaliana phosphatidylinositol synthase and functional expression in the yeast pis mutant.

Authors :
Xue, Hong-Wei
Hosaka, Kohei
Plesch, Gunnar
Mueller-Roeber, Bernd
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