Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates

被引：56

作者：

de Groot, Natalia Sanchez ^{[1
]}

Ventura, Salvador ^{[1
]}

机构：

[1] Univ Autonoma Barcelona, Inst Biotecnol & Biomed, Dept Bioquim & Biol Mol, E-08193 Bellaterra, Spain

来源：

JOURNAL OF BIOTECHNOLOGY | 2006年 / 125卷 / 01期

关键词：

inclusion bodies; recombinant protein expression; protein aggregation; protein folding; Escherichia coli;

D O I：

10.1016/j.jbiotec.2006.02.026

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Recent data show that protein aggregation as bacterial inclusion bodies does not necessarily imply loss of biological activity. Here, we investigate the effect of a large set of single-point mutants of an aggregation-prone protein on its specific activity once deposited in inclusion bodies. The activity of such aggregates significantly correlates with the predicted aggregation rates for each mutant, suggesting that rationally tuning the kinetic competition between folding and aggregation might result in highly active, inclusion bodies. The exploration of this technology during recombinant protein production would have a significant biotechnological value. (c) 2006 Elsevier B.V. All rights reserved.

引用

页码：110 / 113

页数：4

共 8 条

[1] Recombinant protein folding and misfolding in Escherichia coli [J].