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AtbZIP16 and AtbZIP68, two new members of GBFs, can interact with other G group bZIPs in Arabidopsis thaliana

AtbZIP16 and AtbZIP68 are two putative G group bZIP transcription factors in Arabidopsis thaliana, the other three members of G group bZIPs are GBF1-3 which can bind G-box. Members of G group have conservative protein structure: highly homological basic region and a proline-rich domain in the N-term...

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Published in:BMB reports 2008-02, Vol.41 (2), p.132-138
Main Authors: Shen, Huaishun (Fudan University, Shanghai, PR China), Cao, Kaiming (Fudan University, Shanghai, PR China), Wang, Xiping (Fudan University, Shanghai, PR China), E-mail: xipingwang@hotmail.com
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Language:English
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Summary:AtbZIP16 and AtbZIP68 are two putative G group bZIP transcription factors in Arabidopsis thaliana, the other three members of G group bZIPs are GBF1-3 which can bind G-box. Members of G group have conservative protein structure: highly homological basic region and a proline-rich domain in the N-terminal region. Here, we report that AtbZIP16 and AtbZIP68 could bind cis elements with ACGT core, such as G-box, Hex, C-box and As-1, but with different binding affinities which from high to low were G-box greater than Hex greater than C-box greater than As-1; AtbZIP16 and AtbZIP68 could form homodimer and form heterodimer with other members of G group; N-terminal proline rich domain of AtbZIP16 had transactivation activity in yeast cells while that of AtbZIP68 did not AtbZIP16 and AtbZIP68 GFP fusion protein localized in the nucleus of onion epidermal cells. These results indicated that AtbZIP16 and AtbZIP68 were two new members of GBFs. In Arabidopsis, AtbZIP16 and AtbZIP68 may also participate in light-responsive process in which GBF1-3 are involved.
ISSN:1976-6696
DOI:10.5483/BMBRep.2008.41.2.132