Abstract
The B3 DNA binding domain is shared amongst various plant-specific transcription factors, including factors involved in auxin-regulated and abscisic acid-regulated transcription. Herein, we report the NMR solution structure of the B3 domain of the Arabidopsis thaliana cold-responsive transcription factor RAV1. The structure consists of a seven-stranded open beta-barrel and two alpha-helices located at the ends of the barrel and is significantly similar to the structure of the noncatalytic DNA binding domain of the restriction enzyme EcoRII. An NMR titration experiment revealed a DNA recognition interface that enabled us to propose a structural model of the protein-DNA complex. The locations of the DNA-contacting residues are also likely to be similar to those of the EcoRII DNA binding domain.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acclimatization / physiology
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Amino Acid Sequence / physiology
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Arabidopsis / genetics
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Arabidopsis / metabolism*
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Arabidopsis Proteins / chemistry*
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Arabidopsis Proteins / genetics
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Arabidopsis Proteins / metabolism*
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Binding Sites / genetics
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Cold Temperature
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DNA / metabolism*
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Deoxyribonucleases, Type II Site-Specific / chemistry
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Deoxyribonucleases, Type II Site-Specific / metabolism
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Evolution, Molecular
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Models, Molecular
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Molecular Conformation
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Nuclear Magnetic Resonance, Biomolecular
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Phylogeny
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Protein Structure, Secondary / physiology
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Protein Structure, Tertiary / genetics
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Sequence Homology, Amino Acid
Substances
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Arabidopsis Proteins
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DNA-Binding Proteins
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RAV1 protein, Arabidopsis
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DNA
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CCWGG-specific type II deoxyribonucleases
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Deoxyribonucleases, Type II Site-Specific