Refolding, purification, and preliminary structural characterization of the DNA-binding domain of the quorum sensing receptor RhlR from Pseudomonas aeruginosa
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- 作者：Carolina Lixaa ; Adriana F. Marquesb ; Juliana R. Cortinesc ; Bianca C. Nevesa ; Danielle M.P. Oliveiraa ; Cristiane D. Anoboma ; Luí ; s Maurí ; cio T.R. Limab ; Anderson S. Pinheiroa ; pinheiro@iq.ufrj.br" class="auth_mail" title="E-mail the corresponding author
- 关键词：RhlR ; Quorum sensing ; Receptor ; Refolding ; Purification
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：121
- 期：Complete
- 页码：31-40
- 全文大小：1276 K
文摘
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RhlR DBD was refolded in the presence of the charged amino acids l-arginine and l-glutamate.
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2 mg/L culture of highly purified RhlR DBD were obtained.
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RhlR DBD is folded and monomeric.
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RhlR DBD is functional as it is capable of recognizing the rhlAB promoter.
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This refolding and purification protocol will enable further biochemical and structural studies on RhlR DBD.