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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.
Keywords
GENOME, CELL-CYCLE, NMR, KINASE, FISSION YEAST, CRYSTAL-STRUCTURE, CATALYTIC DOMAIN, CHEMICAL-SHIFT, PROTEIN, SEQUENCE

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Chicago
Landrieu, Isabelle, Marco da Costa, Lieven De Veylder, Frédérique Dewitte, Klaas Vandepoele, Sahar Hassan, Jean-Michel Wieruszeski, et al. 2004. “A Small CDC25 Dual-specificity Tyrosine-phosphatase Isoform in Arabidopsis Thaliana.” Proceedings of the National Academy of Sciences of the United States of America 101 (36): 13380–13385.
APA
Landrieu, I., da Costa, M., De Veylder, L., Dewitte, F., Vandepoele, K., Hassan, S., Wieruszeski, J.-M., et al. (2004). A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 101(36), 13380–13385.
Vancouver
1.
Landrieu I, da Costa M, De Veylder L, Dewitte F, Vandepoele K, Hassan S, et al. A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2004;101(36):13380–5.
MLA
Landrieu, Isabelle, Marco da Costa, Lieven De Veylder, et al. “A Small CDC25 Dual-specificity Tyrosine-phosphatase Isoform in Arabidopsis Thaliana.” PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 101.36 (2004): 13380–13385. Print.
@article{298873,
  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.},
  author       = {Landrieu, Isabelle and da Costa, Marco and De Veylder, Lieven and Dewitte, Fr{\'e}d{\'e}rique and Vandepoele, Klaas and Hassan, Sahar and Wieruszeski, Jean-Michel and Corellou, Florence and Faure, Jean-Denis and Van Montagu, Marc and Inz{\'e}, Dirk and Lippens, Guy},
  issn         = {0027-8424},
  journal      = {PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA},
  language     = {eng},
  number       = {36},
  pages        = {13380--13385},
  title        = {A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana},
  url          = {http://dx.doi.org/10.1073/pnas.0405248101},
  volume       = {101},
  year         = {2004},
}

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