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
Division of Applied Life Science (BK21 program), Plant Molecular Biology and Biotechnology Research Center, Gyeongsarg National University, Jinju 660-701, Republic of Keorea.
FEBS Lett. 2005 Feb 28;579(6):1545-50. 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 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.
钙调蛋白（CaM）是一种普遍存在的钙结合蛋白，已知其通过调节各种靶蛋白的活性来调控多种细胞功能。我们用辣根过氧化物酶偶联的钙调蛋白从拟南芥表达文库中分离出一个编码AtWRKY7（一种新型钙调蛋白结合转录因子）的cDNA。定点诱变、凝胶迁移率变动分析、分裂泛素分析以及使用钙/钙调蛋白依赖性酶的竞争分析表明，钙调蛋白特异性结合AtWRKY7的钙依赖性钙调蛋白结合结构域（CaMBD）。此外，我们发现AtWRKY7的CaMBD是WRKY蛋白家族IId组中一个保守的结构基序（C基序）。
