Interactomic Profile of MicroProtein-like Heat Shock Factor Binding Protein, a Negative Regulator of Heat Shock Response, Under Heat Stress and Recovery Stages
Date Issued
2014
Date
2014
Author(s)
Liu, Chin-Cheng
Abstract
Transcription factors could be regulated by small single-domain proteins that disturb the formation of active oligomers. Heat shock factor (HSF) binding protein (HSBP) is a 10-kDa protein with a coiled-coil motif that interacts with the oligomerization domain of HSFs and is a negative regulatorof the heat stress response (HSR). In Arabidopsis (Arabidopsis thaliana), HSBP is a cytoplasmic protein that translocates to the nucleus after HS for HSF interaction. To uncover the cytoplasmic interacting proteins of HSBP and characterize the interaction with HSF members, we used mass spectrometry after HSBP co-immunoprecipitation (co-IP) and HSBP–HSF bimolecular fluorescence complementation assays. Mass spectrometry after co-IP revealed 14 cytoplasmic HSBP-interacting candidates responding to HS in Arabidopsis seedlings. The candidates were cytosolic HSP70s and all components of the MAIGO 2 complex; the most robust candidates were COP1-interactive protein 1 and kinesin-like protein for actin-based chloroplast movement 1, predicted to contain at least one coiled-coil domain. As well, 16 HSFs interacted with HSBP, predominantly in the nucleus, and included factors reported to be involved in the HS signaling cascade, antioxidant mechanisms, and seed maturation. As a small regulatory protein, HSBP interacts with HSFs and cytoplasmic coiled-coil–containing partners in response to numerous stress and developmental conditions.
Subjects
捲曲螺旋結構蛋白
熱休克轉錄因子結合蛋白
熱休克轉錄因子
熱逆境訊息傳導
熱逆境
蛋白質交互作用體
微蛋白
Type
thesis
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