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	Prokaryotic expression and purification of a cotton dehydration responsive element binding protein GhDBP1 and its DNA binding activity
	Huang, B ; Liu, JY
	2010-05-11 ; 2010-05-11
关键词	Gossypium hirsutum DRE-binding protein prokaryotic expression purification electrophoretic mobility shift assay (EMSA) homology modeling TRANSCRIPTION FACTOR GENE-EXPRESSION LOW-TEMPERATURE FREEZING TOLERANCE AP2 DOMAIN BRASSICA-NAPUS HIGH-SALT COLD ARABIDOPSIS DROUGHT Biochemistry & Molecular Biology Biophysics
中文摘要	Cotton (Gossypium hirsulum) is one of the most important economic crops in the world. Its growth and productivity were affected by environment stresses such as drought, cold and high salinity. Thus, the enhanced stress tolerance in this Plant is of great importance. As the dehydration responsive element (DPE) binding protein (DBP) plays an important role in the regulation of plant resistance to environmental stresses and is quite useful for generating transgenic plants tolerant to these stresses, isolation and functional analysis of DBPs in cotton are important to cotton production. In the previous work, a DBP gene from cotton, named as GhDBP1, was isolated and its expression patterns in cotton plants was demonstrated at the transcriptional level. Here, the expression, purification and DNA binding activity of GhDBP1 were reported. The entire coding region of the GhDBP1 gene was inserted into an expression vector, pET28a, and transformed into Escherichia coli BL21 (DE3). The fusion protein was successfully expressed under IPTG induction and the purified recombinant protein was obtained by Ni-NTA affinity chromatography. Non-radioactive electrophoretic mobility shift assay revealed that the purified GhDBP1 protein was able to form a specific complex with the previously characterized DRE element. In addition, the computer modeling of the DNA-binding domain of GhDBP1 were performed using SWISS-MODEL software. The main-chain structures and the folding patterns of the DNA-binding domain of GhDBP1 were similar to the known structure of the DNA-binding domain of the A rabidopsis thaliana GCC box-binding protein AtEPF1. These results indicate that GhDBP1 is a DRE-binding transcription factor and might use the structure similar to that of AtERF1 to interact with DRE sequence.
语种	英语 ; 英语
出版者	SCIENCE PRESS ; BEIJING ; 16 DONGHUANGCHENGGEN NORTH ST, BEIJING 100717, PEOPLES R CHINA
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/26677]
专题	清华大学
推荐引用方式 GB/T 7714	Huang, B,Liu, JY. Prokaryotic expression and purification of a cotton dehydration responsive element binding protein GhDBP1 and its DNA binding activity[J],2010, 2010.
APA	Huang, B,&Liu, JY.(2010).Prokaryotic expression and purification of a cotton dehydration responsive element binding protein GhDBP1 and its DNA binding activity..
MLA	Huang, B,et al."Prokaryotic expression and purification of a cotton dehydration responsive element binding protein GhDBP1 and its DNA binding activity".(2010).

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