Folding Optimization In Vivo Uncovers New Chaperones.
Folding Optimization In Vivo Uncovers New Chaperones.
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DOI：
10.1016/j.jmb.2015.05.013
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发表时间：
2015-09-11
影响因子：
5.6
通讯作者：
Bardwell JC
中科院分区：
文献类型：
--
作者：
Lennon CW;Thamsen M;Friman ET;Cacciaglia A;Sachsenhauser V;Sorgenfrei FA;Wasik MA;Bardwell JC
通过采用基因选择，迫使细胞折叠不稳定的、容易聚集的测试蛋白以生存，我们产生了具有增强的周质折叠能力的细菌菌株。这些菌株提高了测试蛋白的可溶稳态水平。我们分离的大多数细菌变异株都过度表达一种或多种周质蛋白，包括OsmY、Ivy、DPPA、OPPA和HdeB。在这些蛋白质中，只有HdeB先前被令人信服地被证明在体内起到伴侣的作用。通过给细菌在死亡和稳定折叠不良的蛋白质之间的严峻选择，我们现在产生了设计细菌，因为他们有能力稳定特定的蛋白质。
By employing a genetic selection that forces the cell to fold an unstable, aggregation prone test protein in order to survive, we have generated bacterial strains with enhanced periplasmic folding capacity. These strains enhance the soluble steady state level of the test protein. Most of the bacterial variants we isolated were found to overexpress one or more periplasmic proteins including OsmY, Ivy, DppA, OppA, and HdeB. Of these proteins, only HdeB has convincingly been previously shown to function as chaperone in vivo. By giving bacteria the stark choice between death and stabilizing a poorly folded protein, we have now generated designer bacteria selected for their ability to stabilize specific proteins.