1. Expression, Purification, and Secondary Structure Prediction of Pentatricopeptide Repeat Protein RF1A from Rice
- Author
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Li Shaoqing, Gao Feng, Zhu Yingguo, Zhu Renshan, and Wang Kun
- Subjects
Circular dichroism ,Oryza sativa ,food and beverages ,Plant Science ,Biology ,medicine.disease_cause ,Proteomics ,Metabolomics ,Biochemistry ,Protein purification ,medicine ,Pentatricopeptide repeat ,Molecular Biology ,Escherichia coli ,Protein secondary structure - Abstract
Pentatricopeptide repeat protein (PPR) proteins are putative RNA-binding proteins which are particularly prevalent in terrestrial plants. Previous research has reported the great difficulty in purifying soluble PPR proteins in Escherichia coli, therefore hindering further study of their functions. In this paper, we report the use of the pMAL ™ prokaryotic expression system to acquire a soluble expression of a PPR protein, RF1A from rice (Oryza sativa L.). After purification, we identified RF1A by ESI-TOF-MS/MS. We also made an estimation of its secondary structure using the circular dichroism spectroscopy. These results supported the bioinformatic prediction of helical-hairpin model about PPR proteins.
- Published
- 2010