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Journal articles on the topic 'Peptidylprolyl isomerase'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

Gudavicius, Geoff, Heddy Soufari, Santosh Upadhyay, Cameron D. Mackereth, and Christopher J. Nelson. "Resolving the functions of peptidylprolyl isomerases: insights from the mutagenesis of the nuclear FKBP25 enzyme." Biochemical Society Transactions 41, no. 3 (May 23, 2013): 761–68. http://dx.doi.org/10.1042/bst20130013.

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Peptidylprolyl isomerases have been implicated in chromatin regulation through their association with histones, chromatin-modifying enzymes and DNA-binding transcription factors. As with other post-translational modifications to proteins, a mechanistic understanding of the regulation of biological processes is fostered by loss-of-function studies both in vitro and in vivo. For peptidylprolyl isomerases, this can be accomplished with small-molecule inhibitors with high affinity for the isomerase active site or by mutation of amino acid residues that contribute to catalysis. In the present article, we review caveats to each of these approaches, and place emphasis on the thorough characterization of loss-of-function mutations in FKBPs (FK506-binding proteins). Using a case study of mutagenesis of the nuclear FKBP25 peptidylprolyl isomerase enzyme, we demonstrate that certain mutations generate a loss-of-function phenotype because they induce a complete loss of the FKBP domain fold, whereas other mutations are ‘surgical’ in that they ablate catalytic isomerase activity, while maintaining domain structure. Peptidylprolyl isomerases are thought to have both catalytic and non-catalytic functions, but differentiating between these mechanisms has proved to be challenging. The domain-destabilizing and surgical mutants described will facilitate the characterization of these two reported functions of peptidylprolyl isomerases.

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2

Fujisaki, Hiroshi, Yasushige Yonezawa, Motoyuki Shiga, Luca Maragliano, and Shin-ichi Tate. "Exploring Reaction Pathways for Peptidylprolyl-Isomerase." Biophysical Journal 112, no. 3 (February 2017): 449a. http://dx.doi.org/10.1016/j.bpj.2016.11.2407.

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3

Norville, Isobel H., Katherine O'Shea, Mitali Sarkar-Tyson, Suxin Zheng, Richard W. Titball, Gabriele Varani, and Nicholas J. Harmer. "The structure of a Burkholderia pseudomallei immunophilin–inhibitor complex reveals new approaches to antimicrobial development." Biochemical Journal 437, no. 3 (July 13, 2011): 413–22. http://dx.doi.org/10.1042/bj20110345.

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Mips (macrophage infectivity potentiators) are a subset of immunophilins associated with virulence in a range of micro-organisms. These proteins possess peptidylprolyl isomerase activity and are inhibited by drugs including rapamycin and tacrolimus. We determined the structure of the Mip homologue [BpML1 (Burkholderia pseudomallei Mip-like protein 1)] from the human pathogen and biowarfare threat B. pseudomallei by NMR and X-ray crystallography. The crystal structure suggests that key catalytic residues in the BpML1 active site have unexpected conformational flexibility consistent with a role in catalysis. The structure further revealed BpML1 binding to a helical peptide, in a manner resembling the physiological interaction of human TGFβRI (transforming growth factor β receptor I) with the human immunophilin FKBP12 (FK506-binding protein 12). Furthermore, the structure of BpML1 bound to the class inhibitor cycloheximide N-ethylethanoate showed that this inhibitor mimics such a helical peptide, in contrast with the extended prolyl-peptide mimicking shown by inhibitors such as tacrolimus. We suggest that Mips, and potentially other bacterial immunophilins, participate in protein–protein interactions in addition to their peptidylprolyl isomerase activity, and that some roles of Mip proteins in virulence are independent of their peptidylprolyl isomerase activity.

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4

Mori, Tadashi, and Takafumi Uchida. "Small Molecule Inhibitors of Peptidylprolyl cis/trans Isomerase." Current Enzyme Inhibition 6, no. 1 (February 1, 2010): 46–53. http://dx.doi.org/10.2174/157340810790712005.

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5

Nagaoka, Akiko, Naohiro Takizawa, Ryohei Takeuchi, Yutaka Inaba, Izumi Saito, Yoji Nagashima, Tomoyuki Saito, and Ichiro Aoki. "Possible involvement of peptidylprolyl isomerase Pin1 in rheumatoid arthritis." Pathology International 61, no. 2 (December 28, 2010): 59–66. http://dx.doi.org/10.1111/j.1440-1827.2010.02618.x.

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6

Alag, Reema, Asha Manikkoth Balakrishna, Sreekanth Rajan, Insaf A. Qureshi, Joon Shin, Julien Lescar, Gerhard Grüber, and Ho Sup Yoon. "Structural Insights into Substrate Binding by Pv FKBP35, a Peptidylprolyl cis-trans Isomerase from the Human Malarial Parasite Plasmodium vivax." Eukaryotic Cell 12, no. 4 (February 22, 2013): 627–34. http://dx.doi.org/10.1128/ec.00016-13.

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ABSTRACT The immunosuppressive drug FK506 binding proteins (FKBPs), an immunophilin family with the immunosuppressive drug FK506 binding property, exhibit peptidylprolyl cis-trans isomerase (PPIase) activity. While the cyclophilin-catalyzed peptidylprolyl isomerization of X-Pro peptide bonds has been extensively studied, the mechanism of the FKBP-mediated peptidylprolyl isomerization remains uncharacterized. Thus, to investigate the binding of FKBP with its substrate and the underlying catalytic mechanism of the FKBP-mediated proline isomerization, here we employed the FK506 binding domain (FKBD) of the human malarial parasite Plasmodium vivax FK506 binding protein 35 ( Pv FKBP35) and examined the details of the molecular interaction between the isomerase and a peptide substrate. The crystallographic structures of apo Pv FKBD35 and its complex with the tetrapeptide substrate succinyl-Ala-Leu-Pro-Phe- p -nitroanilide (sALPFp) determined at 1.4 Å and 1.65 Å resolutions, respectively, showed that the substrate binds to Pv FKBD35 in a cis conformation. Nuclear magnetic resonance (NMR) studies demonstrated the chemical shift perturbations of D55, H67, V73, and I74 residues upon the substrate binding. In addition, the X-ray crystal structure, along with the mutational studies, shows that Y100 is a key residue for the catalytic activity. Taken together, our results provide insights into the catalytic mechanism of Pv FKBP35-mediated cis-trans isomerization of substrate and ultimately might aid designing substrate mimetic inhibitors targeting the malarial parasite FKBPs.

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7

Yu, Liang, Abdalla J. Mohamed, Leonardo Vargas, Anna Berglöf, Greg Finn, Kun Ping Lu, and C. I. Edvard Smith. "Regulation of Bruton Tyrosine Kinase by the Peptidylprolyl Isomerase Pin1." Journal of Biological Chemistry 281, no. 26 (April 27, 2006): 18201–7. http://dx.doi.org/10.1074/jbc.m603090200.

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8

Liu, Tao, Yu Liu, Hung-Ying Kao, and Dehua Pei. "Membrane Permeable Cyclic Peptidyl Inhibitors against Human Peptidylprolyl Isomerase Pin1." Journal of Medicinal Chemistry 53, no. 6 (March 25, 2010): 2494–501. http://dx.doi.org/10.1021/jm901778v.

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9

Mori, Tadashi, Seima Itami, Tomotaka Yanagi, Yota Tatara, Mari Takamiya, and Takafumi Uchida. "Use of a Real-Time Fluorescence Monitoring System for High-Throughput Screening for Prolyl Isomerase Inhibitors." Journal of Biomolecular Screening 14, no. 4 (April 2009): 419–24. http://dx.doi.org/10.1177/1087057109333979.

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Cyclophilin is a ubiquitous peptidyl prolyl cis/trans isomerase that plays critical roles in many biological processes. A number of cyclophilin inhibitors have been designed based on the structure of the immunosuppressant cyclosporin A. To discover inhibitors that have other structures, the authors established the high-throughput screening (HTS) method using FDSS6000 real-time fluorescence detector. The inhibitors identified with this HTS showed significant correlation with direct interaction as measured by surface plasmon resonance. This high-throughput assay system is a powerful tool for the discovery of peptidylprolyl isomerase inhibitors. ( Journal of Biomolecular Screening 2009:419-424)

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10

Riggs, Daniel L., Patricia J. Roberts, Samantha C. Chirillo, Joyce Cheung-Flynn, Viravan Prapapanich, Thomas Ratajczak, Richard Gaber, Didier Picard, and David F. Smith. "The Hsp90-binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo." EMBO Journal 22, no. 5 (March 3, 2003): 1158–67. http://dx.doi.org/10.1093/emboj/cdg108.

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11

Davis, Tara L., John R. Walker, Hui Ouyang, Farrell MacKenzie, Christine Butler-Cole, Elena M. Newman, Elan Z. Eisenmesser, and Sirano Dhe-Paganon. "The crystal structure of human WD40 repeat-containing peptidylprolyl isomerase (PPWD1)." FEBS Journal 275, no. 9 (April 4, 2008): 2283–95. http://dx.doi.org/10.1111/j.1742-4658.2008.06381.x.

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12

Humphreys, Sue, Gary Rowley, Andrew Stevenson, William J. Kenyon, Michael P. Spector, and Mark Roberts. "Role of Periplasmic Peptidylprolyl Isomerases in Salmonella enterica Serovar Typhimurium Virulence." Infection and Immunity 71, no. 9 (September 2003): 5386–88. http://dx.doi.org/10.1128/iai.71.9.5386-5388.2003.

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ABSTRACT FkpA is a peptidylprolyl isomerase whose expression is regulated by the alternative sigma factor, sigma factor E (σE). In contrast to the results of a previous report, inactivation of fkpA was found to have only a minor effect on the ability of Salmonella enterica serovar Typhimurium to invade and survive within epithelial and macrophage cell lines and cause infection in mice. However, an effect of the fkpA mutation on serovar Typhimurium virulence was seen if the mutation was combined with mutations in surA or htrA, two other σE-regulated genes, which encode proteins involved in protein folding and/or degradation in the periplasm.

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13

Lauranzano, Eliana, Silvia Pozzi, Laura Pasetto, Riccardo Stucchi, Tania Massignan, Katia Paolella, Melissa Mombrini, et al. "Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes." Brain 138, no. 4 (February 10, 2015): 974–91. http://dx.doi.org/10.1093/brain/awv005.

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14

Rajbhandari, Prashant, Mary Szatkowski Ozers, Natalia M. Solodin, Christopher L. Warren, and Elaine T. Alarid. "Peptidylprolyl Isomerase Pin1 Directly Enhances the DNA Binding Functions of Estrogen Receptor α." Journal of Biological Chemistry 290, no. 22 (April 12, 2015): 13749–62. http://dx.doi.org/10.1074/jbc.m114.621698.

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15

Song, Fei, Xin Zhang, Xiao-Bai Ren, Ping Zhu, Jing Xu, Li Wang, Yi-Fei Li, et al. "Cyclophilin A (CyPA) Induces Chemotaxis Independent of Its Peptidylprolyl Cis-Trans Isomerase Activity." Journal of Biological Chemistry 286, no. 10 (January 18, 2011): 8197–203. http://dx.doi.org/10.1074/jbc.c110.181347.

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16

Miele, R., M. Borro, D. Fiocco, D. Barra, and M. Simmaco. "Cloning and biochemical characterization of a peptidylprolyl cis/trans isomerase from Xenopus laevis skin." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A256. http://dx.doi.org/10.1042/bst028a256a.

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17

Martinez-Gonzalez, Jose, and Fausto G. Hegardt. "Characterization of a cDNA Encoding a Cytosolic Peptidylprolyl Cis-Trans -Isomerase from Blattella Germanica." European Journal of Biochemistry 234, no. 1 (November 1995): 284–92. http://dx.doi.org/10.1111/j.1432-1033.1995.284_c.x.

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18

Wohlkönig, Alexandre, Hélène Hodak, Bernard Clantin, Magalie Sénéchal, Coralie Bompard, Françoise Jacob-Dubuisson, and Vincent Villeret. "Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 ofBordetella pertussis." Acta Crystallographica Section F Structural Biology and Crystallization Communications 64, no. 9 (August 9, 2008): 809–12. http://dx.doi.org/10.1107/s1744309108024731.

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19

Miele, R., M. Borro, D. Fiocco, D. Barra, and M. Simmaco. "Cloning and biochemical characterization of a peptidylprolyl cis/trans isomerase from Xenopus laevis skin." Biochemical Society Transactions 28, no. 5 (October 1, 2000): A492. http://dx.doi.org/10.1042/bst028a492b.

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20

Duncan, Kelly E., Brian R. Dempsey, Lauren E. Killip, Jarrett Adams, Melanie L. Bailey, Gilles A. Lajoie, David W. Litchfield, Christopher J. Brandl, Gary S. Shaw, and Brian H. Shilton. "Discovery and Characterization of a Nonphosphorylated Cyclic Peptide Inhibitor of the Peptidylprolyl Isomerase, Pin1." Journal of Medicinal Chemistry 54, no. 11 (June 9, 2011): 3854–65. http://dx.doi.org/10.1021/jm200156c.

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21

Paiva, Ricardo S., Camila V. Ramos, Sara R. Azenha, Carolina Alves, Afonso P. Basto, Luis Graca, and Vera C. Martins. "Peptidylprolyl isomerase C (Ppic) regulates invariant Natural Killer T cell (iNKT) differentiation in mice." European Journal of Immunology 51, no. 8 (May 5, 2021): 1968–79. http://dx.doi.org/10.1002/eji.202048924.

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22

Olejnik, Przemysław, and Katarzyna Nuc. "Cyklofiliny – białka o wielu funkcjach." Postępy Biochemii 64, no. 1 (November 22, 2018): 46–54. http://dx.doi.org/10.18388/pb.2018_104.

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Aktywne formy białek powstają w wyniku translacji oraz zmian zachodzących w trakcie, bądź po tym procesie (fałdowanie, potranslacyjne modyfikacje, kierowanie do odpowiedniego przedziału komórkowego). Struktura przestrzenna białka uzależniona jest od jego sekwencji aminokwasowej co udowodnił Christian Anfinsen, który badając fałdowanie rybonukleazy A, skupił się na odzyskiwaniu aktywności zdenaturowanego enzymu w wyniku prowadzonego procesu renaturacji (nagroda Nobla w dziedzinie chemii w 1972 r. razem z Stanfordem Moore’em i Williamem H. Steinem). Fałdowanie polipeptydów stabilizowane jest i wspomagane przez dwie grupy białek, są to czaperony (nazywane również białkami opiekuńczymi) oraz izomerazy: disulfidoizomerazy (PDI, ang. protein disulfide isomerase, EC 5.3.4.1) i izomerazy peptydyloprolilowe (PPI, ang. peptidylprolyl isomerase EC 5.2.1.8). Czaperony asystują podczas fałdowania białek utrzymując ich stany przejściowe i zapobiegają tworzeniu nieprawidłowych struktur, natomiast izomerazy prowadzą izomeryzację wiązań dwusiarczkowych (PDI) i peptydyloprolilowych (PPI). Praca ta w całościpoświęcona jest charakterystyce cyklofilin, należących do rodziny PPI ze szczególnym uwzględnieniem ich funkcji w procesach związanych z regulacją i patogenezą.

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23

Han, Ruifang, Ying Wang, Chen Chen, Zhuo Zhao, and Huaifeng Mi. "De-Novo Cloning of FKBP23 cDNA from Pig ER Using Nested PCR." Zeitschrift für Naturforschung C 64, no. 3-4 (April 1, 2009): 297–302. http://dx.doi.org/10.1515/znc-2009-3-423.

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FK506 binding proteins (FKBPs) in cells are known as immunophilins. We have identifi ed and characterized a cDNA encoding an endoplasmic reticulum (ER) immunophilin, FKBP23, from pig liver by nested PCR. The predicted amino acid sequence of pig FKBP23 shows high identity to those of human FKBP23 and mouse FKBP23. It possesses a conserved FKBP-type peptidylprolyl cis-trans isomerase (PPIase) domain and EF-hand domain. We constructed a plasmid to express pFKBP23. Furthermore, we proved that the recombinant pFKBP23 can specifi cally bind to natural BiP, the main protein of the molecular chaperone Hsp70 in ER lumen; the binding is interrelated with the Ca2+ concentration just as the FKBP23 from mice.

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24

Bianchi, Marzia, and Melania Manco. "Pin1 Modulation in Physiological Status and Neurodegeneration. Any Contribution to the Pathogenesis of Type 3 Diabetes?" International Journal of Molecular Sciences 19, no. 8 (August 8, 2018): 2319. http://dx.doi.org/10.3390/ijms19082319.

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Prolyl isomerases (Peptidylprolyl isomerase, PPIases) are enzymes that catalyze the isomerization between the cis/trans Pro conformations. Three subclasses belong to the class: FKBP (FK506 binding protein family), Cyclophilin and Parvulin family (Pin1 and Par14). Among Prolyl isomerases, Pin1 presents as distinctive feature, the ability of binding to the motif pSer/pThr-Pro that is phosphorylated by kinases. Modulation of Pin1 is implicated in cellular processes such as mitosis, differentiation and metabolism: The enzyme is dysregulated in many diverse pathological conditions, i.e., cancer progression, neurodegenerative (i.e., Alzheimer’s diseases, AD) and metabolic disorders (i.e., type 2 diabetes, T2D). Indeed, Pin1 KO mice develop a complex phenotype of premature aging, cognitive impairment in elderly mice and neuronal degeneration resembling that of the AD in humans. In addition, since the molecule modulates glucose homeostasis in the brain and peripherally, Pin1 KO mice are resistant to diet-induced obesity, insulin resistance, peripheral glucose intolerance and diabetic vascular dysfunction. In this review, we revise first critically the role of Pin1 in neuronal development and differentiation and then focus on the in vivo studies that demonstrate its pivotal role in neurodegenerative processes and glucose homeostasis. We discuss evidence that enables us to speculate about the role of Pin1 as molecular link in the pathogenesis of type 3 diabetes i.e., the clinical association of dementia/AD and T2D.

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25

Galigniana, Mario D., Yoshihiro Morishima, Philippe A. Gallay, and William B. Pratt. "Cyclophilin-A Is Bound through Its Peptidylprolyl Isomerase Domain to the Cytoplasmic Dynein Motor Protein Complex." Journal of Biological Chemistry 279, no. 53 (October 20, 2004): 55754–59. http://dx.doi.org/10.1074/jbc.m406259200.

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26

Banasavadi-Siddegowda, Yeshavanth K., Junbo Mai, Yifei Fan, Sumit Bhattacharya, David R. Giovannucci, Edwin R. Sanchez, Gunter Fischer, and Xiaodong Wang. "FKBP38 Peptidylprolyl Isomerase Promotes the Folding of Cystic Fibrosis Transmembrane Conductance Regulator in the Endoplasmic Reticulum." Journal of Biological Chemistry 286, no. 50 (October 26, 2011): 43071–80. http://dx.doi.org/10.1074/jbc.m111.269993.

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27

Xu, Chao, Yingqi Xu, Yajun Tang, Jihui Wu, Yunyu Shi, Qiuhua Huang, and Qinghua Zhang. "Letter to the Editor: Backbone and side chain assignments of human Peptidylprolyl Isomerase Like 1 (hPPIL1)." Journal of Biomolecular NMR 31, no. 2 (February 2005): 179–80. http://dx.doi.org/10.1007/s10858-004-8238-0.

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28

Cheng, Shaobing, Mengchao Luo, Chaofeng Ding, Chuanhui Peng, Zhen Lv, Rongliang Tong, Heng Xiao, et al. "Downregulation of Peptidylprolyl isomerase A promotes cell death and enhances doxorubicin-induced apoptosis in hepatocellular carcinoma." Gene 591, no. 1 (October 2016): 236–44. http://dx.doi.org/10.1016/j.gene.2016.07.020.

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29

Gemmill, Trent R., Xiaoyun Wu, and Steven D. Hanes. "Vanishingly Low Levels of Ess1 Prolyl-isomerase Activity Are Sufficient for Growth inSaccharomyces cerevisiae." Journal of Biological Chemistry 280, no. 16 (February 23, 2005): 15510–17. http://dx.doi.org/10.1074/jbc.m412172200.

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Ess1 is an essential peptidylprolyl-cis/trans-isomerase in the yeastSaccharomyces cerevisiae. Ess1 and its human homolog, Pin1, bind to phospho-Ser-Pro sites within proteins, including the carboxyl-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II (pol II). Ess1 and Pin1 are thought to control mRNA synthesis by catalyzing conformational changes in Rpb1 that affect interaction of cofactors with the pol II transcription complex. Here we have characterized wild-type and mutant Ess1 proteinsin vitroandin vivo. We found that Ess1 preferentially binds and isomerizes CTD heptad-repeat (YSPTSPS) peptides that are phosphorylated on Ser5. Binding by the mutant proteinsin vitrowas essentially normal, and the proteins were largely stablein vivo. However, their catalytic activities were reduced >1,000-fold. These data along with results ofin vivotitration experiments indicate that Ess1 isomerase activity is required for growth, but only at vanishingly low levels. We found that although wild-type cells contain about ∼200,000 molecules of Ess1, a level of fewer than 400 molecules per cell is sufficient for growth. In contrast, higher levels of Ess1 were required for growth in the presence of certain metabolic inhibitors, suggesting that Ess1 is important for tolerance to environmental challenge.

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30

Zhou, Z., K. Ying, J. Dai, R. Tang, W. Wang, Y. Huang, W. Zhao, Y. Xie, and Y. Mao. "Molecular cloning and characterization of a novel peptidylprolyl isomerase (cyclophilin)-like gene (PPIL3) from human fetal brain." Cytogenetic and Genome Research 92, no. 3-4 (2001): 231–36. http://dx.doi.org/10.1159/000056909.

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31

Küllertz, Gerhard, Sabine Lüthe, and Gunter Fischer. "Semiautomated microtiter plate assay for monitoring peptidylprolyl cis/trans isomerase activity in normal and pathological human sera." Clinical Chemistry 44, no. 3 (March 1, 1998): 502–8. http://dx.doi.org/10.1093/clinchem/44.3.502.

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Abstract An UV/VIS spectrophotometric assay technique was developed that was able to routinely monitor peptidylprolyl cis/trans isomerase (PPIase) activity of biological fluids in 96-well microtiter plates. The assay, based on monitoring the cis-to-trans isomerization of succinyl-Phe-cisPro-Phe-4-nitroanilide as substrate in a chymotrypsin-coupled reaction, yields a throughput of 96 samples per 30 min. The assay’s capacity was exemplified by dealing with the PPIase activity in several normal and pathological human sera. Reference values of 151 healthy subjects (83 females, 69 males, 17 to 60 years old) were found to possess significant sex-specific differences. PPIase activity factor K of the sera was significantly greater in males (5th, 50th, 95th percentiles: 17, 36, 55 K) than females (14, 30, 48 K). PPIase activities of sera from healthy donors (n = 151) were significantly higher (Mann–Whitney rank-sum test P <0.0001) than those of patients (n = 47). PPIase activity in serum samples stored at 4 °C was stable for at least 20 h.

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32

Zhang, Yi, Ying He, Ling-Li Lu, Zheng-Yu Zhou, Neng-Bin Wan, Guo-Peng Li, Xiao He, and Hong-Wu Deng. "miRNA-192-5p impacts the sensitivity of breast cancer cells to doxorubicin via targeting peptidylprolyl isomerase A." Kaohsiung Journal of Medical Sciences 35, no. 1 (January 2019): 17–23. http://dx.doi.org/10.1002/kjm2.12004.

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33

Geisler, Markus, H. Üner Kolukisaoglu, Rodolphe Bouchard, Karla Billion, Joachim Berger, Beate Saal, Nathalie Frangne, et al. "TWISTED DWARF1, a Unique Plasma Membrane-anchored Immunophilin-like Protein, Interacts with Arabidopsis Multidrug Resistance-like Transporters AtPGP1 and AtPGP19." Molecular Biology of the Cell 14, no. 10 (October 2003): 4238–49. http://dx.doi.org/10.1091/mbc.e02-10-0698.

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Null-mutations of the Arabidopsis FKBP-like immunophilin TWISTED DWARF1 (TWD1) gene cause a pleiotropic phenotype characterized by reduction of cell elongation and disorientated growth of all plant organs. Heterologously expressed TWD1 does not exhibit cis-trans-peptidylprolyl isomerase (PPIase) activity and does not complement yeast FKBP12 mutants, suggesting that TWD1 acts indirectly via protein-protein interaction. Yeast two-hybrid protein interaction screens with TWD1 identified cDNA sequences that encode the C-terminal domain of Arabidopsis multidrugresistance-like ABC transporter AtPGP1. This interaction was verified in vitro. Mapping of protein interaction domains shows that AtPGP1 surprisingly binds to the N-terminus of TWD1 harboring the cis-trans peptidyl-prolyl isomerase-like domain and not to the tetratrico-peptide repeat domain, which has been shown to mediate protein-protein interaction. Unlike all other FKBPs, TWD1 is shown to be an integral membrane protein that colocalizes with its interacting partner AtPGP1 on the plasma membrane. TWD1 also interacts with AtPGP19 (AtMDR1), the closest homologue of AtPGP1. The single gene mutation twd1-1 and double atpgp1-1/atpgp19-1 (atmdr1-1) mutants exhibit similar phenotypes including epinastic growth, reduced inflorescence size, and reduced polar auxin transport, suggesting that a functional TWD1-AtPGP1/AtPGP19 complex is required for proper plant development.

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34

Zarnt, T., K. Lang, H. Burtscher, and G. Fischer. "Time-dependent inhibition of peptidylprolyl cis-trans-isomerases by FK506 is probably due to cis-trans isomerization of the inhibitor's imide bond." Biochemical Journal 305, no. 1 (January 1, 1995): 159–64. http://dx.doi.org/10.1042/bj3050159.

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Free in solution, the immunosuppressive compounds cyclosporin A (CsA), FK506, ascomycin and rapamycin are present in many solvents in various slowly interconverting conformations. Together with their cellular receptor proteins, cyclophilin (CyP) and FK506-binding protein (FKBP), however, these inhibitors have been shown to have a homogeneous conformation. The existence of a slow cis-trans interconversion of an imidic bond in the inhibitor molecule during the course of the formation of the CsA-CyP18cy complex (where CyP18cy is human 18 kDa cytosolic CyP) prompted us to investigate the reaction of the peptidomacrolides FK506, ascomycin and rapamycin with two specific binding-proteins in more detail. Since formation of the FK506-FKBP complex results in the inhibition of the peptidylprolyl cis-trans-isomerase activity of the binding protein, we used the enzyme's decrease in enzymic activity to monitor binding of the inhibitors to their enzyme targets. For FK506, the kinetics of inhibition of human 12 kDa cytosolic FKBP (FKBP12cy) were clearly dependent on time. Subsequent to a rapid inactivation reaction, not resolved in its kinetics due to manual mixing, a slow dominant first-order inactivation process with a relaxation time of 1163 s at 10 degrees C was observed. Concomitantly the Ki value of the slow phase dropped 2.6-fold within the first 60 min of incubation. Using the FKBP12cy homologue 25 kDa membrane FKBP (FKBP25mem), a bacterial peptidylprolyl cis-trans-isomerase, the rate and amplitudes of the inhibition reactions were very similar to FKBP12cy. On the other hand, the kinetics and amplitudes of the inhibition of FKBP12cy varied significantly if rapamycin was used as an inhibitor instead of FK 506. Owing to reduced conformation transition in rapamycin upon binding to FKBP12cy, the slow phase during inhibition was significantly decreased in amplitude. A likely reason for this became apparent when the activation-enthalpy and the pH-dependence of the rate constants of the slow phase were determined. We conclude that the cis to trans interconversion of the pipecolinyl bond of the three peptidomacrolides may be responsible for the slow process. There was no indication of a suicide catalysis of this process by FKBPs.

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Braun, Volkmar, Stephanie Helbig, and Silke I. Patzer. "Import of periplasmic bacteriocins targeting the murein." Biochemical Society Transactions 40, no. 6 (November 21, 2012): 1449–55. http://dx.doi.org/10.1042/bst20120175.

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Colicins are the only proteins imported by Escherichia coli and thus serve as tools to study the protein import mechanism. Most of the colicins studied degrade DNA, 16S RNA or tRNA in the cytoplasm, or form pores in the cytoplasmic membrane. Two bacteriocins, Cma (colicin M) and Pst (pesticin), affect the murein structure in the periplasm. These two bacteriocins must be imported only across the outer membrane and therefore represent the simplest system for studying protein import. Cma can be reversibly translocated across the outer membrane. Cma and Pst unfold during import. The crystal structure of Pst reveals a phage T4L (T4 lysozyme) fold of the activity domain. Both bacteriocins require energy for import which is translocated from the cytoplasmic membrane into the outer membrane by the Ton system. Cma kills cells only when the periplasmic FkpA PPIase (peptidylprolyl cis–trans isomerase)/chaperone is present.

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36

Köhler, Rolf, Jörg Fanghänel, Bettina König, Edeltraud Lüneberg, Matthias Frosch, Jens-Ulrich Rahfeld, Rolf Hilgenfeld, Gunter Fischer, Jörg Hacker, and Michael Steinert. "Biochemical and Functional Analyses of the Mip Protein: Influence of the N-Terminal Half and of Peptidylprolyl Isomerase Activity on the Virulence of Legionella pneumophila." Infection and Immunity 71, no. 8 (August 2003): 4389–97. http://dx.doi.org/10.1128/iai.71.8.4389-4397.2003.

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ABSTRACT The virulence factor Mip (macrophage infectivity potentiator) contributes to the intracellular survival of Legionella pneumophila, the causative agent of Legionnaires' disease. The protein consists of two domains that are connected via a very long α-helix (A. Riboldi-Tunnicliffe et al., Nat. Struct. Biol. 8:779-783, 2001). The fold of the C-terminal domain (residues 100 to 213) is closely related to human FK506-binding protein (FKBP12), and like FKBP12, Mip exhibits peptidylprolyl cis/trans isomerase (PPIase) activity. The α-helical N-terminal domain is responsible for the formation of very stable Mip homodimers. In order to determine the importance of the homodimeric state of Mip for its biochemical activities and for infectivity of Legionella, a truncated, monomeric Mip variant [Mip(77-213)] was overexpressed in Escherichia coli and characterized biochemically. In vitro isomerase activity assays revealed that the altered protein exhibits full isomerase activity towards peptide substrates. However, the deletion resulted in a dramatic loss in the efficiency of refolding of reduced and carboxy-methylated RNase T1. By cis complementation of the Mip-negative mutant strain L. pneumophila JR32-2, we constructed the strain L. pneumophila JR32-2.4, which expresses an N-terminally truncated variant of Mip. Infection studies with these strains revealed that the N-terminal part and the dimerization of Mip but not its PPIase activity are necessary for full virulence in Acanthamoeba castellanii. Infection of guinea pigs showed that strains with dimerization-deficient Mip (JR32-2.4) or a very low PPIase activity (JR32-2.2) were significantly attenuated in the animal model. These results suggest a different role of the PPIase activity and the N-terminally mediated dimeric state of Mip in monocellular systems and during the infection of guinea pigs.

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Miele, R. "A peptidylprolyl cis/trans isomerase from Xenopus laevis skin: cloning, biochemical characterization and putative role in the secretion." Peptides 24, no. 11 (November 2003): 1713–21. http://dx.doi.org/10.1016/j.peptides.2003.07.024.

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38

Maki, N., F. Sekiguchi, J. Nishimaki, K. Miwa, T. Hayano, N. Takahashi, and M. Suzuki. "Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin." Proceedings of the National Academy of Sciences 87, no. 14 (July 1, 1990): 5440–43. http://dx.doi.org/10.1073/pnas.87.14.5440.

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39

Hu, Ming-Kuan, Alison Badger, and Daniel H. Rich. "Cyclosporin Analogs Modified in the 3,7,8-Positions: Substituent Effects on Peptidylprolyl Isomerase Inhibition and Immunosuppressive Activity Are Nonadditive." Journal of Medicinal Chemistry 38, no. 21 (October 1995): 4164–70. http://dx.doi.org/10.1021/jm00021a005.

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40

Fischer, Gunter, Edith Berger, and Holger Bang. "Kinetic β-deuterium isotope effects suggest a covalent mechanism for the protein folding enzyme peptidylprolyl cis/trans -isomerase." FEBS Letters 250, no. 2 (July 3, 1989): 267–70. http://dx.doi.org/10.1016/0014-5793(89)80735-5.

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41

Feroze-Merzoug, F., I. M. Berquin, J. Dey, and Y. Q. Chen. "Peptidylprolyl Isomerase A (PPIA) as a Preferred Internal Control Over GAPDH and β-Actin in Quantitative RNA Analyses." BioTechniques 32, no. 4 (April 2002): 776–82. http://dx.doi.org/10.2144/02324st03.

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42

Cunningham, Earlene Brown. "An Inositolphosphate-Binding Immunophilin, IPBP12." Blood 94, no. 8 (October 15, 1999): 2778–89. http://dx.doi.org/10.1182/blood.v94.8.2778.420k10_2778_2789.

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A novel inositolphosphate-binding protein has been identified and shown to be an immunophilin. This protein, which was isolated from human erythrocyte membranes and from K562 (human erythroleukemia) cell membranes, has robust peptidylprolyl cis-trans isomerase activity that is strongly inhibited by nanomolar concentrations of FK506 or rapamycin, indicating a member of the FKBP (FK506-binding protein) class. However, unlike the cytosolic FKBP12, the isomerase activity of this membrane-associated immunophilin is strongly inhibited by nanomolar concentrations of inositol 1,4,5-trisphosphate (IP3), inositol 1,3,4,5-tetrakisphosphate (IP4), and phosphatidylinositol 4- and 4,5-phosphates, which are suggested to be physiological ligands. The demonstration of a single 12-kD protein that binds both IP4 or IP3and anti-FKBP12 provides strong support for the inositolphosphate-binding immunophilin having an apparent mass of 12 kD, and it is suggested that the protein might be called IPBP12 for 12-kD inositol phosphate binding protein. When an internal tryptic peptide derived from IPBP12 was sequenced, a sequence also present in human cytokeratin 10 was identified, suggesting a cytoskeletal localization for the immunophilin. While purifying IPBP12, it was found that it is immunoprecipitated with specific proteins that include a protein kinase and a phosphoprotein phosphatase. The latter is indicated to be phosphoprotein phosphatase 2A (PP-2A). It is suggested that immunophilins promote the assembly of multiprotein complexes that often include a protein kinase or a phosphoprotein phosphatase or both.

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Gao, Shandian, Junzheng Du, Zhancheng Tian, Qingli Niu, Dexuan Huang, Jidong Wang, Jianxun Luo, Guangyuan Liu, and Hong Yin. "A SYBR green I–based quantitative RT-PCR assay for bovine ephemeral fever virus and its utility for evaluating viral kinetics in cattle." Journal of Veterinary Diagnostic Investigation 32, no. 1 (December 17, 2019): 44–50. http://dx.doi.org/10.1177/1040638719895460.

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We developed a SYBR green I–based reverse-transcription quantitative PCR (RT-qPCR) assay for bovine ephemeral fever virus (BEFV). Analytical sensitivity of the assay was ~ 100 times higher than conventional RT-PCR. The precision of the RT-qPCR established for RNA standards was high, with intra-assay and inter-assay coefficients of variation of 0.23–0.89% and 0.23–1.02%, respectively. The test was highly specific for BEFV strains, with no cross-reactivity with other viruses of veterinary significance. The assay detected BEFV RNA as early as 1 d post-infection (dpi) and up to 7–8 dpi in the blood samples of experimentally infected cattle. The most stable reference gene, peptidylprolyl isomerase A ( PPIA), was selected for the quantification of BEFV. Viral RNA loads reached peak level at 3–5 dpi and then decreased rapidly through 7–8 dpi. Our assay provides a reliable approach for the detection of BEFV in the early infection stage and for use in the profiling of BEFV kinetics in vivo.

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Norville, Isobel H., Nicholas J. Harmer, Sarah V. Harding, Gunter Fischer, Karen E. Keith, Katherine A. Brown, Mitali Sarkar-Tyson, and Richard W. Titball. "A Burkholderia pseudomallei Macrophage Infectivity Potentiator-Like Protein Has Rapamycin-Inhibitable Peptidylprolyl Isomerase Activity and Pleiotropic Effects on Virulence." Infection and Immunity 79, no. 11 (August 22, 2011): 4299–307. http://dx.doi.org/10.1128/iai.00134-11.

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ABSTRACTMacrophage infectivity potentiators (Mips) are a group of virulence factors encoded by pathogenic bacteria such asLegionella,Chlamydia, andNeisseriaspecies. Mips are part of the FK506-binding protein (FKBP) family, whose members typically exhibit peptidylprolylcis-transisomerase (PPIase) activity which is inhibitable by the immunosuppressants FK506 and rapamycin. Here we describe the identification and characterization of BPSS1823, a Mip-like protein in the intracellular pathogenBurkholderia pseudomallei. Recombinant BPSS1823 protein has rapamycin-inhibitable PPIase activity, indicating that it is a functional FKBP. A mutant strain generated by deletion ofBPSS1823inB. pseudomalleiexhibited a reduced ability to survive within cells and significant attenuationin vivo, suggesting that BPSS1823 is important forB. pseudomalleivirulence. In addition, pleiotropic effects were observed with a reduction in virulence mechanisms, including resistance to host killing mechanisms, swarming motility, and protease production.

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45

Nair, S. C., R. A. Rimerman, E. J. Toran, S. Chen, V. Prapapanich, R. N. Butts, and D. F. Smith. "Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor." Molecular and Cellular Biology 17, no. 2 (February 1997): 594–603. http://dx.doi.org/10.1128/mcb.17.2.594.

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A cDNA for human FKBP51 has been cloned and sequenced, and protein products have been expressed in both in vitro and bacterial systems. The deduced amino acid sequence for human FKBP51 is 90% identical to sequences of recently described murine proteins and is 55% identical to the sequence of human FKBP52. Human FKBP51 mRNA is expressed in a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by FK506 but not cyclosporine. FKBP51 is the same as a previously described progesterone receptor-associated immunophilin that, similar to FKBP52 and cyclophilin 40, is an Hsp90-binding protein and appears in functionally mature steroid receptor complexes along with Hsp90 and p23. Each of the three receptor-associated immunophilins displays interactions with progesterone receptor that are more dynamic than Hsp90-receptor interactions. Whereas FKBP52 and FKBP51 compete about equally well for binding to Hsp90 in a purified system, FKBP51 accumulates preferentially in progesterone receptor complexes assembled in a cell-free system. This observation provides a precedent for differential interactions between Hsp90-associated immunophilins and target proteins such as steroid receptors.

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46

Kabbage, Maria, Karim Chahed, Bechr Hamrita, Christelle Lemaitre Guillier, Mounir Trimeche, Sami Remadi, Johan Hoebeke, and Lotfi Chouchane. "Protein Alterations in Infiltrating Ductal Carcinomas of the Breast as Detected by Nonequilibrium pH Gradient Electrophoresis and Mass Spectrometry." Journal of Biomedicine and Biotechnology 2008 (2008): 1–10. http://dx.doi.org/10.1155/2008/564127.

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Improvement of breast-cancer detection through the identification of potential cancer biomarkers is considered as a promising strategy for effective assessment of the disease. The current study has used nonequilibrium pH gradient electrophoresis with subsequent analysis by mass spectrometry to identify protein alterations in invasive ductal carcinomas of the breast from Tunisian women. We have identified multiple protein alterations in tumor tissues that were picked, processed, and unambiguously assigned identities by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF). The proteins identified span a wide range of functions and are believed to have potential clinical applications as cancer biomarkers. They include glycolytic enzymes, molecular chaperones, cytoskeletal-related proteins, antioxydant enzymes, and immunologic related proteins. Among these proteins, enolase 1, phosphoglycerate kinase 1, deoxyhemoglobin, Mn-superoxyde dismutase,α-B-crystallin, HSP27, Raf kinase inhibitor protein, heterogeneous nuclear ribonucleoprotein A2/B1, cofilin 1, and peptidylprolyl isomerase A were overexpressed in tumors compared with normal tissues. In contrast, the IGHG1 protein, the complement C3 component C3c, which are two newly identified protein markers, were downregulated in IDCA tissues.

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Hayano, Toshiya, Nobuhiro Takahashi, Setsuko Kato, Noboru Maki, and Masanori Suzuki. "Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells." Biochemistry 30, no. 12 (March 26, 1991): 3041–48. http://dx.doi.org/10.1021/bi00226a009.

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48

Liu, Tongzheng, Ryan A. Schneider, Nam Y. Lee, and Dale G. Hoyt. "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 (PIN1) regulates pulmonary effects of endotoxin and tumor necrosis factor-α in mice." Biochemical and Biophysical Research Communications 452, no. 3 (September 2014): 468–72. http://dx.doi.org/10.1016/j.bbrc.2014.08.089.

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49

PAGE, Antony P., Kenneth MacNIVEN, and Michael O. HENGARTNER. "Cloning and biochemical characterization of the cyclophilin homologues from the free-living nematode Caenorhabditis elegans." Biochemical Journal 317, no. 1 (July 1, 1996): 179–85. http://dx.doi.org/10.1042/bj3170179.

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Cyclosporin A (CsA) is the most widely used immunosuppressive agent, whose properties are exerted via an interaction with cyclophilin, resulting in down-regulation of signal-transduction events in the T-cell. Cyclophilin is identical with peptidylprolyl cis–trans isomerase (PPI; EC 5.2.1.8), an enzyme which catalyses the isomerization between the two proline conformations in proteins, thereby acting as a catalyst in protein-folding events. Several reports indicate that CsA has potent anti-parasitic activity, effective against both protozoan and helminth species. In order to understand the various biological roles that cyclophilins play we have initiated a study of these proteins in the genetically tractable nematode Caenorhabditis elegans. Here we describe the cloning and characterization of 11 cyclophilin genes (cyp-1 to -11) derived from this nematode; this is currently the greatest number of isoforms described in a single species. Southern blotting and physical mapping indicated that these genes are dispersed throughout the nematode genome. A high degree of conservation exists between several isoforms, which also share characteristics with the ubiquitous isoforms previously described. The remaining isoforms are divergent, having altered CsA-binding domains and additional non-cyclophilin domains, which may impart compartmental specificity. Ten of these isoforms have been expressed in Escherichia coli, and the resultant fusion proteins have been examined biochemically for PPI activity, which they all possess. Isomerase activity is highest in the conserved and lowest in divergent isoforms, perhaps indicating a more specific substrate for the latter. Analysis of the C. elegans cyp genes will provide answers as to the roles played by cyclophilins in protein folding and signal transduction.

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Fan, Guoliang, Lin Wang, Jia Xu, Ping Jiang, Wei Wang, Ying Huang, Minggang Lv, and Shaoting Liu. "Knockdown of the prolyl isomerase Pin1 inhibits Hep-2 cell growth, migration, and invasion by targeting the β-catenin signaling pathway." Biochemistry and Cell Biology 96, no. 6 (December 2018): 734–41. http://dx.doi.org/10.1139/bcb-2017-0334.

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There is increasing evidence indicating that peptidylprolyl cis/trans isomerase, NIMA-interacting 1 (Pin1) plays a decisive role in a variety of cancers. Nevertheless, its function in laryngeal squamous cell carcinoma (LSCC) has not been elaborated. The aim of this study is to determine the role of Pin1 in LSCC. Here, we established stably transfected Hep-2 cells with low expression of Pin1. Intriguingly, cell proliferation, migration, and invasion was significantly inhibited in Pin1-silenced Hep-2 cells. Similarly, knockdown of Pin1 induced apoptosis of Hep-2 cells, as evidenced by increased expression of cleaved-caspase-3, cleaved-PARP, and bax, and decreased expression of bcl2. We also demonstrated that silencing of Pin1 down-regulated β-catenin and cyclin D1 expression. Inversely, over-expression of β-catenin reversed the inhibiting effect of Pin1 silencing on Hep-2 cells. Moreover, we proved that knockdown of Pin1 inhibited tumorigenesis of Hep-2 cells in vivo. Taken together, we demonstrate that silencing of Pin1 effectively suppresses the growth of Hep-2 cells through β-catenin, indicating that Pin1 possess the potential to serve as a therapeutic target for the treatment of LSCC.

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