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首页> 外文期刊>Journal of Molecular Biology >Novel interaction between the major bacterial heat shock chaperone (GroESL) and an RNA chaperone (CspC)
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Novel interaction between the major bacterial heat shock chaperone (GroESL) and an RNA chaperone (CspC)

机译：主要细菌热休克伴侣（GroESL）和RNA伴侣（CspC）之间的新型相互作用

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摘要

The heat shock response is one of the main global regulatory networks in all organisms and involves an increased cellular level of chaperones and proteases to enable correct protein folding and balanced growth. One of the major heat shock chaperones in Escherichia coli is GroESL, composed of GroES and GroEL (the bacterial Hsp10 and Hsp60 homologues), which is essential for refolding of misfolded proteins. GroESL was previously shown to play a role in the regulation of the heat shock response by promoting the proteolysis of the regulatory protein - sigma32 (RpoH), the heat shock transcription activator. Here we show the involvement of GroESL in another proteolytic process, this of the major RNA chaperone - CspC - that specifically stabilizes the transcripts of several stress-related genes. Evidence is provided for an interaction between GroESL and CspC that results in enhanced, temperature-dependent proteolysis of the latter. This interaction is of regulatory importance, as reduction in the cellular levels of CspC leads to a decrease in stability of the major heat shock gene transcripts.
机译：热休克反应是所有生物中主要的全球调节网络之一，涉及提高伴侣蛋白和蛋白酶的细胞水平，以实现正确的蛋白质折叠和平衡的生长。大肠杆菌中主要的热休克伴侣蛋白之一是GroESL，它由GroES和GroEL（细菌的Hsp10和Hsp60同源物）组成，这对于错误折叠的蛋白质的重新折叠是必不可少的。以前已证明GroESL通过促进调节蛋白-热激转录激活因子sigma32（RpoH）的蛋白水解在热激反应的调节中发挥作用。在这里，我们显示了GroESL参与另一种蛋白水解过程，即主要的RNA分子伴侣-CspC-该蛋白可以稳定几种胁迫相关基因的转录本。提供了GroESL和CspC之间相互作用的证据，该相互作用导致后者的增强的温度依赖性蛋白水解作用。这种相互作用具有调节重要性，因为CspC细胞水平的降低导致主要热休克基因转录本的稳定性降低。

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