Abstract
We analyzed a tertiary structure of systemin, the first identified polypeptide plant hormone, using two-dimensional NMR spectroscopy. From these data and molecular dynamics calculations we concluded that the peptide can adopt a Z-like-beta-sheet structure, which has previously been found in many specific DNA-binding proteins. Using DNA-cellulose affinity chromatography, we showed that systemin binds strongly to DNA. We suggest that the specific systemin-DNA interaction, particularly in a promoter region of the proteinase inhibitors, could effect gene expression and thus explain the biological activity of systemin.
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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Base Sequence
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Chromatography, Affinity
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Computer Graphics
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DNA / metabolism*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / metabolism
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Gene Expression Regulation, Plant
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Lactoferrin / metabolism
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Magnetic Resonance Spectroscopy
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / metabolism
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Peptides / chemistry*
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Peptides / metabolism
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Peptides / pharmacology
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Plant Proteins / chemistry*
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Plant Proteins / metabolism
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Plant Proteins / pharmacology
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Protease Inhibitors / metabolism*
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Solanum lycopersicum / chemistry
Substances
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DNA-Binding Proteins
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Peptide Fragments
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Peptides
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Plant Proteins
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Protease Inhibitors
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systemin
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DNA
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Lactoferrin