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WRKY group IId transcription factors interact with calmodulin

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
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]

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