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WRKY group IId transcription factors interact with calmodulin
- Source :
-
FEBS Letters . Feb2005, Vol. 579 Issue 6, p1545-1550. 6p. - Publication Year :
- 2005
-
Abstract
- Abstract: Calmodulin (CaM) is a ubiquitous Ca2+-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 Ca2+-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. [Copyright &y& Elsevier]
- Subjects :
- *ARABIDOPSIS
*TRANSCRIPTION factors
*HORSERADISH
*METALLOENZYMES
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 579
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 17427775
- Full Text :
- https://doi.org/10.1016/j.febslet.2005.01.057