Cloning and expression of rapeseed procruciferin in Escherichia coli and crystallization of the purified recombinant protein

被引:0
作者
Mary Rose G. Tandang
Motoyasu Adachi
Shigeru Utsumi
机构
[1] Kyoto University,Laboratory of Food Quality Design and Development, Graduate School of Agriculture
来源
Biotechnology Letters | 2004年 / 26卷
关键词
crystallization; expression; procruciferin; rapeseed;
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摘要
Two rapeseed cruciferin cDNAs (cru2/3a and cru2/3b) were cloned and sequenced. A comparison of their DNA and protein sequences with other cruciferins, indicated cru2/3b to be a novel clone and, among them, an inherent and highly conserved sequence of twelve amino acids was identified. Procruciferin 2/3a and 2/3b were expressed in Eschericha coli, and procruciferin 2/3a was obtained in a soluble form. The expressed procruciferin 2/3a has a trimeric structure and formed crystals although the quality was not good, suggesting that this expression system is useful for protein engineering of procruciferin 2/3a.
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页码:385 / 391
页数:6
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