WRKY group IId transcription factors interact with calmodulin

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• 作者：Park ; Chan Young ; Lee ; Ju Huck ; Yoo ; Jae Hyuk ; Moon ; Byeong Cheol ; Choi ; Man Soo ; Kang ; Yun Hwan ; et. al.
• 关键词：AtCaM2 ; Arabidopsis calmodulin2 ; CaM ; calmodulin ; CaMBD ; CaM-binding domain ; CaMBP ; CaM-binding protein ; GST ; Glutathione S-transferase ; HRP ; horseradish peroxidase ; PDE ; phosphodiesterase ; Calcium ; Calmodulin ; Calmodulin-binding protein ; Tr
• 刊名：FEBS Letters
• 出版年：2005
• 出版时间：February 28, 2005
• 年：2005
• 卷：579
• 期：6
• 页码：1545-1550
• 全文大小：407 K

文摘

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.