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Degradation of Extracytoplasmic Catalysts for Protein Folding in Bacillus subtilis

机译：枯草芽孢杆菌蛋白质折叠的胞质外催化剂的降解

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The general protein secretion pathway of Bacillus subtilis has a high capacity for protein export from the cytoplasm, which is exploited in the biotechnological production of a wide range of enzymes. These exported proteins pass the membrane in an unfolded state, and accordingly, they have to fold into their active and protease-resistant conformations once membrane passage is completed. The lipoprotein PrsA and the membrane proteins HtrA and HtrB facilitate the extracytoplasmic folding and quality control of exported proteins. Among the native exported proteins of B. subtilis are at least 10 proteases that have previously been implicated in the degradation of heterologous secreted proteins. Recently, we have shown that these proteases also degrade many native membrane proteins, lipoproteins, and secreted proteins. The present studies were therefore aimed at assessing to what extent these proteases also degrade extracytoplasmic catalysts for protein folding. To this end, we employed a collection of markerless protease mutant strains that lack up to 10 different extracytoplasmic proteases. The results show that PrsA, HtrA, and HtrB are indeed substrates of multiple extracytoplasmic proteases. Thus, improved protein secretion by multiple-protease-mutant strains may be related to both reduced proteolysis and improved posttranslocational protein folding and quality control.
机译：枯草芽孢杆菌的一般蛋白质分泌途径具有从细胞质中输出蛋白质的能力，这在多种酶的生物技术生产中得到了利用。这些输出的蛋白质以未折叠状态通过膜，因此，一旦膜通过完成，它们就必须折叠成它们的活性和耐蛋白酶构象。脂蛋白PrsA和膜蛋白HtrA和HtrB有助于胞外折叠和输出蛋白的质量控制。在枯草芽孢杆菌的天然输出蛋白中，至少有10种蛋白酶先前与异源分泌蛋白的降解有关。最近，我们已经显示这些蛋白酶还降解许多天然膜蛋白，脂蛋白和分泌的蛋白。因此，本研究旨在评估这些蛋白酶在多大程度上降解蛋白质折叠的胞外催化剂。为此，我们采用了无标记蛋白酶突变菌株的集合，这些菌株缺乏多达10种不同的胞外蛋白酶。结果显示，PrsA，HtrA和HtrB确实是多种胞质蛋白酶的底物。因此，多种蛋白酶突变株改善的蛋白质分泌可能与减少的蛋白水解作用以及改善的易位蛋白折叠和质量控制有关。

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