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Proc Natl Acad Sci U S A. 2004 Sep 7;101(36):13380-5. Epub 2004 Aug 25.

A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.

Author information

  • 1Unité Mixte de Recherche 8525 Centre National de la Recherche Scientifique-Lille2, Institut de Biologie de Lille/Pasteur Institute of Lille, 59019 Lille Cedex, France. isabelle.landrieu@ibl.fr

Erratum in

  • Proc Natl Acad Sci U S A. 2004 Nov 16;101(46):16391.

Abstract

The dual-specificity CDC25 phosphatases are critical positive regulators of cyclin-dependent kinases (CDKs). Even though an antagonistic Arabidopsis thaliana WEE1 kinase has been cloned and tyrosine phosphorylation of its CDKs has been demonstrated, no valid candidate for a CDC25 protein has been reported in higher plants. We identify a CDC25-related protein (Arath;CDC25) of A. thaliana, constituted by a sole catalytic domain. The protein has a tyrosine-phosphatase activity and stimulates the kinase activity of Arabidopsis CDKs. Its tertiary structure was obtained by NMR spectroscopy and confirms that Arath;CDC25 belongs structurally to the classical CDC25 superfamily with a central five-stranded beta-sheet surrounded by helices. A particular feature of the protein, however, is the presence of an additional zinc-binding loop in the C-terminal part. NMR mapping studies revealed the interaction with phosphorylated peptidic models derived from the conserved CDK loop containing the phosphothreonine-14 and phosphotyrosine-15. We conclude that despite sequence divergence, Arath;CDC25 is structurally and functionally an isoform of the CDC25 superfamily, which is conserved in yeast and in plants, including Arabidopsis and rice.

PMID:
15329414
[PubMed - indexed for MEDLINE]
PMCID:
PMC516575
Free PMC Article

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