Cold shock stress-induced proteins in Bacillus subtilis
Cold shock stress-induced proteins in Bacillus subtilis
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DOI：
10.1128/jb.178.15.4611-4619.1996
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发表时间：
1996-08-01
影响因子：
3.2
通讯作者：
Marahiel, MA
中科院分区：
文献类型：
--
作者：
Graumann, P;Schroder, K;Marahiel, MA
细菌对温度降低的反应是诱导被归类为冷诱导蛋白（CIP）的蛋白质。利用双向凝胶电泳技术，我们分析了枯草芽孢杆菌的冷休克反应。在从37 ℃转变到15 ℃后，大多数蛋白质的合成受到抑制;相反，37种蛋白质的合成速率高于转变前的速率。冷休克后1h，CIP的诱导减少，2 h后，一般蛋白质合成恢复。从二维凝胶中切下鉴定的主要CIP并进行微测序。三个小的酸性蛋白，表现出最高的相对诱导冷休克后是高度同源的，属于一个蛋白质家族，其中的一个成员，主要的冷休克蛋白，CspB，以前已被鉴定。cspB无效突变体的二维凝胶分析显示，CspB影响几种CIP的诱导水平。其他鉴定的CIP在细胞生理学的各种水平发挥功能，例如趋化性（CheY）、糖摄取（Hpr）、翻译（核糖体蛋白S6和L7/L12）、蛋白质折叠（PPiB）和一般代谢（CysK、IlvC、Gap和磷酸丙糖异构酶）。
Bacteria respond to a decrease in temperature with the induction of proteins that are classified as cold-induced proteins (CIPs). Using two-dimensional gel electrophoresis, we analyzed the cold shock response in Bacillus subtilis. After a shift from 37 to 15 degrees C, the synthesis of a majority of proteins was repressed; in contrast, 37 proteins were synthesized at rates higher than preshift rates. One hour after cold shock, the induction of CIPs decreased, and after 2 h, general protein synthesis resumed. The identified main CIPs were excised from two-dimensional gels and were subjected to microsequencing. Three small acidic proteins that showed the highest relative induction after cold shock were highly homologous and belonged to a protein family of which one member, the major cold shock protein, CspB, has previously been characterized. Two-dimensional gel analyses of a cspB null mutant revealed that CspB affects the level of induction of several CIPs. Other identified CIPs function at various levels of cellular physiology, such as chemotaxis (CheY), sugar uptake (Hpr), translation (ribosomal proteins S6 and L7/L12), protein folding (PPiB), and general metabolism (CysK, IlvC, Gap, and triosephosphate isomerase).