Kaur Gundeep, Singh Supreet, Dutta Tanima, Kaur Harsimran, Singh Brinderjit, Pareek Ashwani, Singh Prabhjeet
Department of Biotechnology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India.
Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi, 110021, India.
Biochim Open. 2015 Nov 30;2:9-15. doi: 10.1016/j.biopen.2015.11.003. eCollection 2016 Jun.
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 . The TaCypA-1 possesses peptidyl-prolyl isomerase (PPIase) activity that catalyses to 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.
在高温下生长是微生物工业应用所需的特性之一，因为这会减少污染并提高某些底物的溶解度。在本研究中，证明了小麦亲环蛋白TaCypA-1的异源表达赋予了[具体对象]耐热性。TaCypA-1具有肽基脯氨酰异构酶（PPIase）活性，可催化肽基脯氨酰键的[具体异构化过程]，这是蛋白质折叠中的限速步骤。缺乏PPIase活性的TaCypA-1缺失突变体的表达导致耐热性丧失，这首次证明该活性在细胞的应激耐受中起关键作用，并且可用于工业应用。此外，我们还证明TaCypA-1与钙调蛋白（CaM）相互作用，并且CaM结合域定位于N端区域的氨基酸残基51-71处。
