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Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain

Bibliographic reference Bocian-Ostrzycka, Katarzyna M. ; Łasica, Anna M. ; Dunin-Horkawicz, Stanisław ; Grzeszczuk, Magdalena J. ; Drabik, Karolina ; et. al. Functional and evolutionary analyses of Helicobacter pylori HP0231 (DsbK) protein with strong oxidative and chaperone activity characterized by a highly diverged dimerization domain. In: Frontiers in Microbiology, Vol. 6, no. eCollection, p. 1065 (2015)
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  1. Baik S.-C., Kim K.-M., Song S.-M., Kim D.-S., Jun J.-S., Lee S.-G., Song J.-Y., Park J.-U., Kang H.-L., Lee W.-K., Cho M.-J., Youn H.-S., Ko G.-H., Rhee K.-H., Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Helicobacter pylori Strain 26695, 10.1128/jb.186.4.949-955.2004
  2. Bardwell James C.A., McGovern Karen, Beckwith Jon, Identification of a protein required for disulfide bond formation in vivo, 10.1016/0092-8674(91)90532-4
  3. Behrens W., Bonig T., Suerbaum S., Josenhans C., Genome Sequence of Helicobacter pylori hpEurope Strain N6, 10.1128/jb.00386-12
  4. Berkmen Mehmet, Production of disulfide-bonded proteins in Escherichia coli, 10.1016/j.pep.2011.10.009
  5. Biegert A., Mayer C., Remmert M., Soding J., Lupas A. N., The MPI Bioinformatics Toolkit for protein sequence analysis, 10.1093/nar/gkl217
  6. Bocian-Ostrzycka Katarzyna M., Grzeszczuk Magdalena J., Dziewit Lukasz, Jagusztyn-Krynicka Elżbieta K., Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems, 10.3389/fmicb.2015.00570
  7. Chim Nicholas, Harmston Christine A, Guzman David J, Goulding Celia W, Structural and biochemical characterization of the essential DsbA-like disulfide bond forming protein from Mycobacterium tuberculosis, 10.1186/1472-6807-13-23
  8. Cho Seung-Hyun, Collet Jean-Francois, Many Roles of the Bacterial Envelope Reducing Pathways, 10.1089/ars.2012.4962
  9. Cho S.-H., Parsonage D., Thurston C., Dutton R. J., Poole L. B., Collet J.-F., Beckwith J., A New Family of Membrane Electron Transporters and Its Substrates, Including a New Cell Envelope Peroxiredoxin, Reveal a Broadened Reductive Capacity of the Oxidative Bacterial Cell Envelope, 10.1128/mbio.00291-11
  10. Cho Seung-Hyun, Szewczyk Joanna, Pesavento Christina, Zietek Matylda, Banzhaf Manuel, Roszczenko Paula, Asmar Abir, Laloux Géraldine, Hov Ann-Kristin, Leverrier Pauline, Van der Henst Charles, Vertommen Didier, Typas Athanasios, Collet Jean-François, Detecting Envelope Stress by Monitoring β-Barrel Assembly, 10.1016/j.cell.2014.11.045
  11. Collet Jean-Francois, D'Souza Jonathan Conrad, Jakob Ursula, Bardwell James C. A., Thioredoxin 2, an Oxidative Stress-induced Protein, Contains a High Affinity Zinc Binding Site, 10.1074/jbc.m307818200
  12. Crooks G. E., WebLogo: A Sequence Logo Generator, 10.1101/gr.849004
  13. Daniels Robert, Mellroth Peter, Bernsel Andreas, Neiers Fabrice, Normark Staffan, von Heijne Gunnar, Henriques-Normark Birgitta, Disulfide Bond Formation and Cysteine Exclusion in Gram-positive Bacteria, 10.1074/jbc.m109.081398
  14. Delorenzi M., Speed T., An HMM model for coiled-coil domains and a comparison with PSSM-based predictions, 10.1093/bioinformatics/18.4.617
  15. Denoncin Katleen, Collet Jean-François, Disulfide Bond Formation in the Bacterial Periplasm: Major Achievements and Challenges Ahead, 10.1089/ars.2012.4864
  16. Denoncin Katleen, Nicolaes Valérie, Cho Seung-Hyun, Leverrier Pauline, Collet Jean-François, Protein Disulfide Bond Formation in the Periplasm: Determination of the In Vivo Redox State of Cysteine Residues, Methods in Molecular Biology (2013) ISBN:9781627032445 p.325-336, 10.1007/978-1-62703-245-2_20
  17. Depuydt M., Leonard S. E., Vertommen D., Denoncin K., Morsomme P., Wahni K., Messens J., Carroll K. S., Collet J.-F., A Periplasmic Reducing System Protects Single Cysteine Residues from Oxidation, 10.1126/science.1179557
  18. Depuydt Matthieu, Messens Joris, Collet Jean-Francois, How Proteins Form Disulfide Bonds, 10.1089/ars.2010.3575
  19. Edgar R. C., MUSCLE: multiple sequence alignment with high accuracy and high throughput, 10.1093/nar/gkh340
  20. Erlendsson L. S., Moller M., Hederstedt L., Bacillus subtilis StoA Is a Thiol-Disulfide Oxidoreductase Important for Spore Cortex Synthesis, 10.1128/jb.186.18.6230-6238.2004
  21. Frickey T., Lupas A., CLANS: a Java application for visualizing protein families based on pairwise similarity, 10.1093/bioinformatics/bth444
  22. Han H., Wilson A. C., The Two CcdA Proteins of Bacillus anthracis Differentially Affect Virulence Gene Expression and Sporulation, 10.1128/jb.00917-13
  23. Hatahet Feras, Boyd Dana, Beckwith Jon, Disulfide bond formation in prokaryotes: History, diversity and design, 10.1016/j.bbapap.2014.02.014
  24. Heras B., Edeling M. A., Schirra H. J., Raina S., Martin J. L., Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide, 10.1073/pnas.0402769101
  25. Heras Begoña, Kurz Mareike, Jarrott Russell, Shouldice Stephen R., Frei Patrick, Robin Gautier, Čemažar Maša, Thöny-Meyer Linda, Glockshuber Rudi, Martin Jennifer L., Staphylococcus aureusDsbA Does Not Have a Destabilizing Disulfide : A NEW PARADIGM FOR BACTERIAL OXIDATIVE FOLDING, 10.1074/jbc.m707838200
  26. Heuermann D., A stable shuttle vector system for efficient genetic complementation of Helicobacter pylori strains by transformation and conjugation, 10.1007/s004380050677
  27. Hiniker Annie, Collet Jean-Francois, Bardwell James C. A., Copper Stress Causes anin VivoRequirement for theEscherichia coliDisulfide Isomerase DsbC, 10.1074/jbc.m505742200
  28. Inaba Kenji, Protein disulfide bond generation inEscherichia coliDsbB–DsbA, 10.1107/s090904950706061x
  29. Inaba Kenji, MBSJ MCC Young Scientist Award 2009
REVIEW: Structural basis of protein disulfide bond generation in the cell : Protein disulfide bond generation in the cell, 10.1111/j.1365-2443.2010.01434.x
  30. Inaba K., Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade, 10.1093/emboj/21.11.2646
  31. Inaba Kenji, Ito Koreaki, Structure and mechanisms of the DsbB–DsbA disulfide bond generation machine, 10.1016/j.bbamcr.2007.11.006
  32. Kadokura Hiroshi, Beckwith Jon, Mechanisms of Oxidative Protein Folding in the Bacterial Cell Envelope, 10.1089/ars.2010.3187
  33. Kadokura H., Nichols L., Beckwith J., Mutational Alterations of the Key cis Proline Residue That Cause Accumulation of Enzymatic Reaction Intermediates of DsbA, a Member of the Thioredoxin Superfamily, 10.1128/jb.187.4.1519-1522.2005
  34. Katzen Federico, Beckwith Jon, Transmembrane Electron Transfer by the Membrane Protein DsbD Occurs via a Disulfide Bond Cascade, 10.1016/s0092-8674(00)00180-x
  35. Katzen F., Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD, 10.1093/emboj/cdf405
  36. Kpadeh Zegbeh Z., Day Shandra R., Mills Brandy W., Hoffman Paul S., Legionella pneumophilautilizes a single-player disulfide-bond oxidoreductase system to manage disulfide bond formation and isomerization : Single-player disulfide-bond oxidoreductase system, 10.1111/mmi.12914
  37. Kpadeh Z. Z., Jameson-Lee M., Yeh A. J., Chertihin O., Shumilin I. A., Dey R., Day S. R., Hoffman P. S., Disulfide Bond Oxidoreductase DsbA2 of Legionella pneumophila Exhibits Protein Disulfide Isomerase Activity, 10.1128/jb.01949-12
  38. Landeta Cristina, Blazyk Jessica L, Hatahet Feras, Meehan Brian M, Eser Markus, Myrick Alissa, Bronstain Ludmila, Minami Shoko, Arnold Holly, Ke Na, Rubin Eric J, Furie Barbara C, Furie Bruce, Beckwith Jon, Dutton Rachel, Boyd Dana, Compounds targeting disulfide bond forming enzyme DsbB of Gram-negative bacteria, 10.1038/nchembio.1752
  39. Lester Jeffrey, Kichler Sari, Oickle Brandon, Fairweather Spencer, Oberc Alexander, Chahal Jaspreet, Ratnayake Dinath, Creuzenet Carole, Characterization ofHelicobacter pylori HP0231 (DsbK): role in disulfide bond formation, redox homeostasis and production ofHelicobactercystein-rich protein HcpE : Characterization ofHelicobacter pylori DsbK, 10.1111/mmi.12923
  40. Leverrier Pauline, Declercq Jean-Paul, Denoncin Katleen, Vertommen Didier, Hiniker Annie, Cho Seung-Hyun, Collet Jean-François, Crystal Structure of the Outer Membrane Protein RcsF, a New Substrate for the Periplasmic Protein-disulfide Isomerase DsbC, 10.1074/jbc.m111.224865
  41. Li Weikai, Schulman Sol, Dutton Rachel J., Boyd Dana, Beckwith Jon, Rapoport Tom A., Structure of a bacterial homologue of vitamin K epoxide reductase, 10.1038/nature08720
  42. Lupas A., Van Dyke M., Stock J., Predicting coiled coils from protein sequences, 10.1126/science.252.5009.1162
  43. Luthy, J. Mol. Biol., 340, 829 (2004)
  44. Metcalf Peter, McCarthy Andrew A., Haebel Peter W., Törrönen Anneli, Rybin Vladimir, Baker Edward N., 10.1038/73295
  45. McMahon Róisín M., Premkumar Lakshmanane, Martin Jennifer L., Four structural subclasses of the antivirulence drug target disulfide oxidoreductase DsbA provide a platform for design of subclass-specific inhibitors, 10.1016/j.bbapap.2014.01.013
  46. Messens Joris, Collet Jean-Francois, Van Belle Karolien, Brosens Elke, Loris Remy, Wyns Lode, The Oxidase DsbA Folds a Protein with a Nonconsecutive Disulfide, 10.1074/jbc.m705236200
  47. Myers J. D., A sulphite respiration system in the chemoheterotrophic human pathogen Campylobacter jejuni, 10.1099/mic.0.27573-0
  48. Paxman Jason J., Borg Natalie A., Horne James, Thompson Philip E., Chin Yanni, Sharma Pooja, Simpson Jamie S., Wielens Jerome, Piek Susannah, Kahler Charlene M., Sakellaris Harry, Pearce Mary, Bottomley Stephen P., Rossjohn Jamie, Scanlon Martin J., The Structure of the Bacterial Oxidoreductase Enzyme DsbA in Complex with a Peptide Reveals a Basis for Substrate Specificity in the Catalytic Cycle of DsbA Enzymes, 10.1074/jbc.m109.011502
  49. Puig, J. Biol. Chem., 269, 7764 (1994)
  50. Puig, J. Biol. Chem., 269, 19128 (1994)
  51. Raczko A. M., Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria, 10.1099/mic.0.27483-0
  52. Remmert Michael, Biegert Andreas, Hauser Andreas, Söding Johannes, HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment, 10.1038/nmeth.1818
  53. Ren Guoping, Stephan Daniel, Xu Zhaohui, Zheng Ying, Tang Danming, Harrison Rosemary S., Kurz Mareike, Jarrott Russell, Shouldice Stephen R., Hiniker Annie, Martin Jennifer L., Heras Begoña, Bardwell James C. A., Properties of the Thioredoxin Fold Superfamily Are Modulated by a Single Amino Acid Residue, 10.1074/jbc.m809509200
  54. Roszczenko Paula, Grzeszczuk Magdalena, Kobierecka Patrycja, Wywial Ewa, Urbanowicz Paweł, Wincek Piotr, Nowak Elzbieta, Jagusztyn-Krynicka E. Katarzyna, Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231, 10.1186/s12866-015-0471-z
  55. Roszczenko Paula, Radomska Katarzyna A., Wywial Ewa, Collet Jean-Francois, Jagusztyn-Krynicka Elzbieta K., A Novel Insight into the Oxidoreductase Activity of Helicobacter pylori HP0231 Protein, 10.1371/journal.pone.0046563
  56. Saleh Malek, Bartual Sergio G., Abdullah Mohammed R., Jensch Inga, Asmat Tauseef M., Petruschka Lothar, Pribyl Thomas, Gellert Manuela, Lillig Christopher H., Antelmann Haike, Hermoso Juan A., Hammerschmidt Sven, Molecular architecture ofStreptococcus pneumoniaesurface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence : Pneumococcal surface oxidative resistance system, 10.1002/emmm.201202435
  57. Sambrook, Molecular Cloning: A Laboratory Manual. (2001)
  58. Shao Feng, Bader Martin W., Jakob Ursula, Bardwell James C. A., DsbG, a Protein Disulfide Isomerase with Chaperone Activity, 10.1074/jbc.275.18.13349
  59. Shouldice Stephen R., Heras Begoña, Walden Patricia M., Totsika Makrina, Schembri Mark A., Martin Jennifer L., Structure and Function of DsbA, a Key Bacterial Oxidative Folding Catalyst, 10.1089/ars.2010.3344
  60. Stirnimann C. U., Grütter M. G., Glockshuber R., Capitani G., nDsbD: a redox interaction hub in the Escherichia coli periplasm, 10.1007/s00018-006-6055-1
  61. Stirnimann Christian U., Rozhkova Anna, Grauschopf Ulla, Böckmann Rainer A., Glockshuber Rudi, Capitani Guido, Grütter Markus G., High-resolution Structures of Escherichia coli cDsbD in Different Redox States: A Combined Crystallographic, Biochemical and Computational Study, 10.1016/j.jmb.2006.02.030
  62. Studier F. William, Protein production by auto-induction in high-density shaking cultures, 10.1016/j.pep.2005.01.016
  63. Yoon Ji Young, Kim Jieun, Lee Sang Jae, Kim Hyoun Sook, Im Ha Na, Yoon Hye-Jin, Kim Kyoung Hoon, Kim Soon-Jong, Han Byung Woo, Suh Se Won, Structural and functional characterization ofHelicobacter pyloriDsbG, 10.1016/j.febslet.2011.10.042
  64. Zhao Zhen, Peng Yi, Hao Shu-feng, Zeng Zong-hao, Wang Chih-chen, Dimerization by Domain Hybridization Bestows Chaperone and Isomerase Activities, 10.1074/jbc.m306945200
  65. Zheng Wei-dong, Quan Hui, Song Jiu-li, Yang Sheng-li, Wang Chih-chen, Does DsbA Have Chaperone-like Activity?, 10.1006/abbi.1996.9783