Elucidation of the Specific Formation of Homo- and Heterodimeric Forms of ThbZIP1 and Its Role in Stress

International Journal of Molecular Sciences

Xianguang Nie¹  Xiaoyu Ji³  Yujia Liu²  Lei Zheng¹ 

[1] State Key Laboratory of Tree Genetics and Breeding (Northeast Forestry University), 26 Hexing Road, Harbin 150040, China; E-Mails:;College of Food Engineering, Harbin University of Commerce, 1 Xuehai Street, Harbin 150028, China; E-Mail:;Key Laboratory of Biogeography and Bioresource in Arid Land, Xinjiang Institute of Ecology and Geography, Chinese Academy of Sciences, Urumqi 830011, China; E-Mail:

关键词: bZIP (basic leucine zipper proteins) transcription factors;    heterodimerization;    protein–protein interaction;    two-hybrid analysis;    Tamarix hispida;   

DOI  :  10.3390/ijms150610005

来源: mdpi

【 摘 要 】

Protein–protein interactions are important for the molecular understanding of the biological processes of proteins. The dimerization of bZIPs (basic leucine zipper proteins) is involved in modifying binding site specificities, altering dimer stability, and permitting a new set of specific protein-to-protein interactions to occur at the promoter. In the present study, we studied the whether ThbZIP1 form homo- and heterodimers using the yeast two-hybrid method. Five bZIP genes were cloned from Tamarix hispida to investigate their interaction with ThbZIP1. Our results showed that ThbZIP1 can form homodimers with itself, and three out of five bZIPs could interact with the ThbZIP1 protein to form heterodimers. Real-time RT-PCR results suggested that these ThbZIPs can all respond to abiotic stresses and abscisic acid (ABA), and shared very similar expression patterns in response to NaCl, ABA or PEG6000. Subcellular localization studies showed that all ThbZIPs are targeted to the nucleus. Our results showed that ThbZIP1 are dimeric proteins, which can form homo- or heterodimers.

【 授权许可】

CC BY   
© 2014 by the authors; licensee MDPI, Basel, Switzerland.