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

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          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.

          Highlights

          • •

            Heterologous expression of a wheat cyclophilin, TaCypA-1, confers thermotolerance to E. coli.

          • •

            PPIase activity is essential for heat stress tolerance of E. coli cells.

          • •

            TaCypA-1 binds calmodulin in vitro in a Ca 2+ -dependent manner.

          • •

            CaM-binding domain is localized to 51–71 amino acid residues in the N-terminus of TaCypA-1.

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          A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase.

          Kathleen Harding, A Galat, Rebecca Schreiber … (1989)
          The structurally novel macrolide FK506 (refs 1,2) has recently been demonstrated to have potent immunosuppressive activity at concentrations several hundredfold lower than cyclosporin A (CsA). Cyclosporin A, a cyclic peptide, has found widespread clinical use in the prevention of graft rejection following bone marrow and organ transplantation. The mechanisms of immunosuppression mediated by FK506 and CsA appear to be remarkably similar, suggesting that these unrelated structures act on a common receptor or on similar molecular targets, perhaps the CsA receptor, cyclophilin, which has recently been shown by Fischer et al. and Takahashi et al. to have cis-trans peptidyl-prolyl isomerase activity. We have prepared an FK506 affinity matrix and purified a binding protein for FK506 from bovine thymus and from human spleen. This FK506-binding protein (FKBP) has a relative molecular mass (Mr) of approximately 14,000(14K), a pI of 8.8-8.9, and does not cross-react with antisera against cyclophilin. The first 40 N-terminal residues of the bovine and 16 residues of the human FKBP were determined; the 16-residue fragments are identical to each other and unrelated to any known sequences. This protein catalyses the cis-trans isomerization of the proline amide in a tetrapeptide substrate and FK506 inhibits the action of this new isomerase. The FKBP and cyclophilin appear to be members of an emerging class of novel proteins that regulate T cell activation and other metabolic processes, perhaps by the recognition (and possibly the isomerization) of proline-containing epitopes in target proteins.
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            Cyclophilins

            Sumita Kumari, Suchismita Roy, Prabhjeet Singh … (2012)
            Cyclophilins constitute a subgroup of large family of proteins called immunophilins, which also include FKBPs and Parvulins. They are remarkably conserved in all genera, highlighting their pivotal role in important cellular processes. Most cyclophilins display PPIase enzymatic activity, multiplicity, diverse cellular locations and active role in protein folding which render them to be included in the class of diverse set of proteins called molecular chaperones. Due to their distinct PPIase function, besides protein disulfide isomerases and protein foldases, cyclophilins have been deemed necessary for in vivo chaperoning activity. Unlike other cellular chaperones, these proteins are specific in their respective targets. Not all cyclophilin proteins possess PPIase activity, indicating a loss of their PPIase activity during the course of evolution and gain of function independent of their PPIase activity. The PPIase function of cyclophilins is also compensated by their functional homologs, like FKBPs. Multiple cyclophilin members in plants like Arabidopsis and rice have been reported to be associated with diverse functions and regulatory pathways through their foldase, scaffolding, chaperoning or other unknown activities. Although many functions of plant cyclophilins were reported or suggested, the physiological relevance and molecular basis of stress-responsive expression of plant cyclophilins is still largely unknown. However, their wide distribution and ubiquitous nature signifies their fundamental importance in plant survival. Several of these members have also been directly linked to multiple stresses. This review attempts to deal with plant cyclophilins with respect to their role in stress response.
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              [Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides].

              C Mech, Edgar G. Fischer, Kyong H. Bang (1983)
              The rates of cis to trans interconversion of Glt-(Ala)n-Pro-Phe-4-nitroanilides (n = 1-3) were estimated by means of a two-step process with chymotrypsin as the trans-substrate cleaving activity. By the aid of this system, pig kidney and several other tissues contained demonstrable catalytic activity against the cis to trans interconversion of the proline containing peptides. The active protein fraction was purified 38-fold from pig kidney cortex by ammonium sulfate precipitation and a series of column chromatographic techniques. Activity was detected against the cis to trans interconversion of Glt-Ala-Ala-Pro-Phe-4-nitroanilide to a different extent. No activity was found with Phe-Pro-4-nitroanilide. With respect to the substrate specificity, this enzyme must be classified as a peptidyl-prolyl cis-trans-isomerase. The enzyme was strongly inactivated by p-chloromercuribenzoate, sodium dodecylsulfate, Hg2+- and Cu2+-ions, but was not inhibited by metal chelators, diisopropylphosphorofluoridate and chlorotosylamidophenylbutane. The activity is abolished by incubation with trypsin. The enzyme is heat sensitive at 50 degrees C. The results presented in this paper suggest a new type of enzymes, characterized by catalytic activity against conformational interconversions. The possibility of the location of the enzyme on ribosomal particles is discussed.
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                Author and article information

                Contributors
                Prabhjeet Singh
                Journal
                Journal ID (nlm-ta): Biochim Open
                Journal ID (iso-abbrev): Biochim Open
                Title: Biochimie Open
                Publisher: Elsevier
                ISSN (Electronic): 2214-0085
                Publication date PMC-release: 30 November 2015
                Publication date Collection: June 2016
                Publication date (Electronic): 30 November 2015
                Volume: 2
                Pages: 9-15
                Affiliations
                [a ]Department of Biotechnology, Guru Nanak Dev University, Amritsar, 143005, Punjab, India
                [b ]Department of Plant Molecular Biology, University of Delhi South Campus, New Delhi, 110021, India
                [c ]Stress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India
                Author notes
                [∗ ]Corresponding author. singhprabhjeet62@ 123456gmail.com
                [1]

                Contributed equally.

                Article
                Publisher ID: S2214-0085(15)00010-3
                DOI: 10.1016/j.biopen.2015.11.003
                PMC ID: 5889472
                PubMed ID: 29632833
                SO-VID: 50048d84-afa4-46f4-afc4-77aee4c2486a
                Copyright © © 2015 The Authors
                License:

                This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

                History
                Date received : 9 October 2015
                Date accepted : 19 November 2015
                Categories
                Subject: Research paper

                Keywords: cyclophilin,escherichia coli,heat stress,peptidyl-prolyl cis-trans isomerase activity,wheat
                Data availability:
                Keywords: cyclophilin, escherichia coli, heat stress, peptidyl-prolyl cis-trans isomerase activity, wheat

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