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    J Biol Chem. 2000 Apr 7;275(14):10577-81.

    The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase.

    Landrieu I, De Veylder L, Fruchart JS, Odaert B, Casteels P, Portetelle D, Van Montagu M, Inzé D, Lippens G.

    Unité de Microbiologie, Faculté Universitaire des Sciences Agronomiques de Gembloux, B-5030 Gembloux, Belgium. isabelle.landrieu@pastair-lille.fr

    A homologue of the human site-specific prolyl cis/trans isomerase PIN1 was identified in Arabidopsis thaliana. The PIN1At gene encodes a protein of 119 amino acids that is 53% identical with the catalytic domain of the human PIN1 parvulin. Steady-state PIN1At mRNA is found in all plant tissues tested. We show by two-dimensional NMR spectroscopy that the PIN1At is a prolyl cis/trans isomerase with specificity for phosphoserine-proline bonds. PIN1At is the first example of an eukaryotic parvulin without N- or C-terminal extensions. The N-terminal WW domain of 40 amino acids, typical of all the phosphorylation-dependent eukaryotic parvulins, is absent. However, triple-resonance NMR experiments showed that PIN1At contained a hydrophobic helix similar to the alpha1 helix observed in PIN1 that could mediate the protein-protein interactions.

    PMID: 10744752 [PubMed - indexed for MEDLINE]

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