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. 2005 Feb 28;579(6):1545-50.
doi: 10.1016/j.febslet.2005.01.057.

WRKY group IId transcription factors interact with calmodulin

Chan Young Park  1 , Ju Huck Lee, Jae Hyuk Yoo, Byeong Cheol Moon, Man Soo Choi, Yun Hwan Kang, Sang Min Lee, Ho Soo Kim, Kyu Young Kang, Woo Sik Chung, Chae Oh Lim, Moo Je Cho
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Free article

WRKY group IId transcription factors interact with calmodulin

Chan Young Park et al. FEBS Lett. .
Free article

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.

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