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박찬영

Park, Chan Young
Calcium Dynamics Lab.
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WRKY group IId transcription factors interact with calmodulin

Author(s)
Park, Chan YoungLee, JHYoo, JHMoon, BCChoi, MSKang, YHLee, SMKim, HSKang, KYChung, WSLim, COCho, Moo Je
Issued Date
2005-02
DOI
10.1016/j.febslet.2005.01.057
URI
https://scholarworks.unist.ac.kr/handle/201301/7192
Fulltext
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=20044362714
Citation
FEBS LETTERS, v.579, no.6, pp.1545 - 1550
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.
Publisher
ELSEVIER SCIENCE BV
ISSN
0014-5793
Keyword (Author)
calmodulin-binding proteintranscription factorWRKYArabidopsiscalciumcalmodulin
Keyword
BINDING PROTEINSTARGET RECOGNITIONPEPTIDE COMPLEXPLANT DEFENSEARABIDOPSISFAMILYSUPERFAMILYACTIVATORSDOMAINS

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