Abstract
Calmodulin (CaM) is a ubiquitous Ca(2+)-binding protein known to regulate diverse cellular functions by modulating the activity of various target proteins. We isolated a cDNA encoding AtWRKY7, a novel CaM-binding transcription factor, from an Arabidopsis expression library with horseradish peroxidase-conjugated CaM. CaM binds specifically to the Ca(2+)-dependent CaM-binding domain (CaMBD) of AtWRKY7, as shown by site-directed mutagenesis, a gel mobility shift assay, a split-ubiquitin assay, and a competition assay using a Ca2+/CaM-dependent enzyme. Furthermore, we show that the CaMBD of AtWRKY7 is a conserved structural motif (C-motif) found in group IId of the WRKY protein family.
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 / chemistry
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Arabidopsis / classification
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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 / isolation & purification
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Arabidopsis Proteins / metabolism*
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Calmodulin / metabolism*
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Calmodulin-Binding Proteins / chemistry
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Calmodulin-Binding Proteins / classification
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Calmodulin-Binding Proteins / genetics
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Calmodulin-Binding Proteins / metabolism
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Phylogeny
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Protein Binding
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Sequence Alignment
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / isolation & purification
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Transcription Factors / metabolism*
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Ubiquitin / metabolism
Substances
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Arabidopsis Proteins
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Calmodulin
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Calmodulin-Binding Proteins
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Peptide Fragments
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Transcription Factors
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Ubiquitin
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WRKY7 protein, Arabidopsis