title: The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase.
abstract: 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.
authors.affiliation: Unité de Microbiologie, Faculté Universitaire des Sciences Agronomiques de Gembloux, B-5030 Gembloux, Belgium. isabelle.landrieu@pastair-lille.fr
authors.forename: I
authors.initials: I
authors.lastname: Landrieu
authors.forename: L
authors.initials: L
authors.lastname: De Veylder
authors.forename: J S
authors.initials: JS
authors.lastname: Fruchart
authors.forename: B
authors.initials: B
authors.lastname: Odaert
authors.forename: P
authors.initials: P
authors.lastname: Casteels
authors.forename: D
authors.initials: D
authors.lastname: Portetelle
authors.forename: M
authors.initials: M
authors.lastname: Van Montagu
authors.forename: D
authors.initials: D
authors.lastname: Inzé
authors.forename: G
authors.initials: G
authors.lastname: Lippens
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics*; D029681:Arabidopsis Proteins; D003001:Cloning, Molecular; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D017343:Genes, Plant; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D010766:Phosphorylation; D018514:Plant Structures / Q000201:enzymology; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
chemical_list: D029681:Arabidopsis Proteins; D029968:Escherichia coli Proteins; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; C000606847:PIN1AT protein, Arabidopsis; D011994:Recombinant Proteins; C000606846:PIN1 protein, human; D019696:Peptidylprolyl Isomerase; C000606851:parvA protein, E coli