WRKY group IId transcription factors interact with calmodulin

• Published in: FEBS letters Vol. 579; no. 6; pp. 1545 - 1550
• Main Authors: Park, Chan Young, Lee, Ju Huck, Yoo, Jae Hyuk, Moon, Byeong Cheol, Choi, Man Soo, Kang, Yun Hwan, Lee, Sang Min, Kim, Ho Soo, Kang, Kyu Young, Chung, Woo Sik, Lim, Chae Oh, Cho, Moo Je
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 28.02.2005
• Subjects: Amino Acid Sequence; Arabidopsis; Arabidopsis - chemistry; Arabidopsis - classification; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis calmodulin2; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - genetics; Arabidopsis Proteins - isolation & purification; Arabidopsis Proteins - metabolism; AtCaM2; Calcium; Calmodulin; Calmodulin - metabolism; Calmodulin-binding protein; Calmodulin-Binding Proteins - chemistry; Calmodulin-Binding Proteins - classification; Calmodulin-Binding Proteins - genetics; Calmodulin-Binding Proteins - metabolism; CaM; CaM-binding domain; CaM-binding protein; CaMBD; CaMBP; Glutathione S-transferase; GST; horseradish peroxidase; HRP; Molecular Sequence Data; PDE; Peptide Fragments - chemistry; Peptide Fragments - genetics; Peptide Fragments - metabolism; phosphodiesterase; Phylogeny; Protein Binding; Sequence Alignment; Transcription factor; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - isolation & purification; Transcription Factors - metabolism; Ubiquitin - metabolism; WRKY; CaMBP; WRKY; Calcium; Arabidopsis; HRP; GST; CaMBD; Calmodulin-binding protein; CaM; PDE; AtCaM2; Transcription factor; Calmodulin
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/j.febslet.2005.01.057

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 Ca 2+/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.