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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Arabidopsis / enzymology
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Arabidopsis / genetics*
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Arabidopsis Proteins
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Cloning, Molecular
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Escherichia coli
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Escherichia coli Proteins
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Genes, Plant
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Humans
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Kinetics
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Molecular Sequence Data
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NIMA-Interacting Peptidylprolyl Isomerase
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Nuclear Magnetic Resonance, Biomolecular
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Peptidylprolyl Isomerase / chemistry
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Peptidylprolyl Isomerase / genetics*
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Peptidylprolyl Isomerase / metabolism
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Phosphorylation
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Plant Structures / enzymology
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Protein Conformation
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Recombinant Proteins / chemistry
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Recombinant Proteins / metabolism
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Arabidopsis Proteins
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Escherichia coli Proteins
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NIMA-Interacting Peptidylprolyl Isomerase
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PIN1AT protein, Arabidopsis
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Recombinant Proteins
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PIN1 protein, human
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Peptidylprolyl Isomerase
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parvA protein, E coli