The peptidyl-prolyl cis-trans isomerase activity of the wheat cyclophilin, TaCypA-1, is essential for inducing thermotolerance in Escherichia coli

Biochimie open Pub Date : 2016-06-01 DOI:10.1016/j.biopen.2015.11.003

Gundeep Kaur , Supreet Singh , Tanima Dutta , Harsimran Kaur , Brinderjit Singh , Ashwani Pareek , Prabhjeet Singh

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引用次数: 14

Abstract

Growth at high temperatures is one of the desired features for industrial applications of microbes, as it results in decrease in contamination and enhanced solubility of certain substrates. In this study, it is demonstrated that heterologous expression of a wheat cyclophilin, TaCypA-1, confers thermotolerance to Escherichia coli. The TaCypA-1 possesses peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyses cis to trans isomerization of the peptidyl prolyl bonds, a rate limiting step in protein folding. Expression of deleted mutants of TaCypA-1, that lacked PPIase activity, resulted in abrogation of thermotolerance, providing the first evidence that this activity plays a key role in stress tolerance of cells and can be exploited for industrial applications. Further, we also demonstrate that TaCypA-1 interacts with calmodulin (CaM), and the CaM-binding domain is localized to amino acid residues 51–71 in the N-terminus region.

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小麦亲环蛋白TaCypA-1的肽基脯氨酸顺式反式异构酶活性对诱导大肠杆菌耐热性至关重要

在高温下生长是微生物工业应用的理想特征之一，因为它可以减少污染并增强某些底物的溶解度。在这项研究中，证明了小麦亲环蛋白TaCypA-1的异源表达赋予大肠杆菌耐热性。TaCypA-1具有肽基脯氨酸顺式-反式异构酶(PPIase)活性，催化肽基脯氨酸键的顺式到反式异构化，这是蛋白质折叠的限速步骤。缺乏PPIase活性的TaCypA-1缺失突变体的表达导致了热耐受性的丧失，首次证明了该活性在细胞的耐受性中起着关键作用，可以用于工业应用。此外，我们还证明了TaCypA-1与钙调蛋白(CaM)相互作用，CaM结合域定位于n端区域的51-71氨基酸残基。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Biochimie open

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