Strategies for the analysis of thioloxidorductases
References
- Agudo D., Mendoza M.T., Castanares C., Nombela C., Rotger R.: A proteomic approach to study Salmonella typhi periplasmic proteins altered by a lack of the DsbA thiol: disulfide isomerase. Proteomics, 4, 355–363 (2004)
- Arts I.S., Ball G., Leverrier P., Garvis S., Nicolaes V., Vertommen D., Ize B., Tamu Dufe V., Messens J., Voulhoux R., Collet J.F.: Dissecting the machinery that introduces disulfide bonds in Pseudomonas aeruginosa. mBio, 4, e00912–00913 (2013)
- Berkmen M.: Production of disulfide-bonded proteins in Escherichia coli. Protein Expr. Purif. 82, 240–251 (2012)
- Bocian-Ostrzycka K.M., Grzeszczuk M.J., Banaś A.M., Jastrząb K., Pisarczyk K., Kolarzyk A., Łasica A.M., Collet J.-F., Jagusztyn-Krynicka E.K.: Engineering of Helicobacter pyloriDimeric Oxidoreductase DsbK (HP0231). Frontiers in Microbiology, 7, 1158 (2016)
- Chim N., Harmston C.A., Guzman D.J., Goulding C.W.: Structural and biochemical characterization of the essential DsbA- -like disulfide bond forming protein from Mycobacterium tuberculosis. BMC Struct. Biol. 13, 23 (2013)
- Cho S.H., Collet J.F.: Many roles of the bacterial envelope reducing pathways. Antioxid. Redox Signal. 18, 1690–1698 (2013)
- 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. mBio, 3, e00291–11. (2012)
- Cho S.H., Szewczyk J., Pesavento C., Zietek M., Banzhaf M., Roszczenko P., Asmar A., Laloux G., Hov A.K., Leverrier P., Van der Henst C., Vertommen D., Typas A., Collet J.F.: Detecting envelope stress by monitoring beta-barrel assembly. Cell,159, 1652–1664 (2014)
- Daniels R., Mellroth P., Bernsel A., Neiers F., Normark S., von Heijne G., Henriques-Normark B.: Disulfide bond formation and cysteine exclusion in gram-positive bacteria. J. Biol. Chem.285, 3300–3309 (2010)
- Denoncin K., Collet J.F.: Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead. Antioxid. Redox Signal. 19, 63–71 (2013)
- Denoncin K., Vertommen D., Paek E., Collet J.F.: The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential beta-barrel protein LptD. J. Biol. Chem.285, 29425–29433 (2010)
- Denoncin K., Nicolaes V., Cho S.H., Leverrier P., Collet J.F.: Protein disulfide bond formation in the periplasm: determination of the in vivo redox state of cysteine residues. Methods Mol. Biol. 966, 325–336 (2013)
- 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. Science, 326, 1109–1111 (2009)
- Duprez W., Bachu P., Stoermer M.J., Tay S., McMahon R.M., Fairlie D.P., Martin J.L.: Virtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbA. PLoS ONE, 10, e0133805 (2015)
- Duprez W., Premkumar L., Halili M.A., Lindahl F., Reid R.C., Fairlie D.P., Martin J.L.: Peptide Inhibitors of the Escherichia coli DsbA Oxidative Machinery Essential for Bacterial Virulence. J. Med. Chem. 58, 577–587 (2015)
- Dutton R.J., Boyd D., Berkmen M., Beckwith J.: Bacterial species exhibit diversity in their mechanisms and capacity for protein disulfide bond formation. P. Natl. Acad. Sci. USA, 105, 11933– 11938 (2008)
- Grabowska A.D., Wywial E., Dunin-Horkawicz S., Lasica A.M., Wosten M.M., Nagy-Staron A., Godlewska R., Bocian-Ostrzycka K., Pienkowska K., Laniewski P., Bujnicki J.M., van Putten J.P., Jagusztyn-Krynicka E.K.: Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA. PLoS ONE, 9, e106247 (2014)
- Greiner-Stoeffele T., Grunow M., Hahn U.: A general ribonuclease assay using methylene blue. Anal. Biochem.240, 24–28 (1996)
- Grimshaw J.P., Stirnimann C.U., Brozzo M.S., Malojcic G., Grutter M.G., Capitani G., Glockshuber R.: DsbL and DsbI form a specific dithiol oxidase system for periplasmic arylsulfate sulfotransferase in uropathogenic Escherichia coli. J. Mol. Biol. 380, 667–680 (2008)
- Hatahet F., Boyd D., Beckwith J.: Disulfide bond formation in prokaryotes: history, diversity and design. Biochim. Biophys. Acta, 1844, 1402–1414 (2014)
- Heras B., Edeling M.A., Schirra H.J., Raina S., Martin J.L.: Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. P. Natl. Acad. Sci. USA, 101, 8876–8881 (2004)
- Heras B., Shouldice S.R., Totsika M., Scanlon M.J., Schembri M.A., Martin J.L.: DSB proteins and bacterial pathogenicity. Nat. Rev. Microbiol. 7, 215–225 (2009)
- Heras B., Kurz M., Jarrott R., Shouldice S.R., Frei P., Robin G., Cemazar M., Thony-Meyer L., Glockshuber R., Martin J.L.: Staphylococcus aureus DsbA does not have a destabilizing disulfide. A new paradigm for bacterial oxidative folding. J. Biol. Chem.283, 4261–4271 (2008)
- Hiniker A., Bardwell J.C.: In vivo substrate specificity of periplasmic disulfide oxidoreductases. J. Biol. Chem.279, 12967–12973 (2004)
- Hiniker A., Collet J.F., Bardwell J.C.: Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J. Biol. Chem.280, 33785–33791 (2005)
- Hiniker A., Ren G., Heras B., Zheng Y., Laurinec S., Jobson R.W., Stuckey J.A., Martin J.L., Bardwell J.C.: Laboratory evolution of one disulfide isomerase to resemble another. P. Natl. Acad. Sci. USA, 104, 11670–11675 (2007)
- Inaba K., Ito K.: Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine. Biochim. Biophys. Acta, 1783, 520–529 (2008)
- Inaba K., Murakami S., Suzuki M., Nakagawa A., Yamashita E., Okada K., Ito K.: Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation. Cell, 127, 789–801 (2006)
- Jameson-Lee M., Garduno R.A., Hoffman P.S.: DsbA2 (27 kDa Com1-like protein) of Legionella pneumophila catalyses extracytoplasmic disulphide-bond formation in proteins including the Dot/Icm type IV secretion system. Mol. Microbiol. 80, 835– 852 (2011)
- Kadokura H., Katzen F., Beckwith J.: Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 72, 111–135 (2003)
- Kadokura H., Tian H., Zander T., Bardwell J.C., Beckwith J.: Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science, 303, 534–537 (2004)
- Katzen F., Deshmukh M., Daldal F., Beckwith J.: Evolutionary domain fusion expanded the substrate specificity of the transmembrane electron transporter DsbD. EMBO J. 21, 3960–3969 (2002)
- Koniger V., Holsten L., Harrison U., Busch B., Loell E., Zhao Q., Bonsor D.A., Roth A., Kengmo-Tchoupa A., Smith S.I., Mueller S., Sundberg E.J., Zimmermann W., Fischer W., Hauck C.R., Haas R.: Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA. Nat. Microbiol. 2, 16188 (2016)
- Kpadeh Z.Z., Day S.R., Mills B.W., Hoffman P.S.: Legionella pneumophila utilizes a single-player disulfide-bond oxidore-ductase system to manage disulfide bond formation and isomerization. Mol. Microbiol. 95, 1054–1069 (2015)
- 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. J. Bacteriol. 195, 1825–1833 (2013)
- Kurz M., Iturbe-Ormaetxe I., Jarrott R., Cowieson N., Robin G., Jones A., King G.J., Frei P., Glockshuber R., O’Neill S.L., Heras B., Martin J.L.: Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis. Protein Expr. Purif. 59, 266–273 (2008)
- Lafaye C., Iwema T., Carpentier P., Jullian-Binard C., Kroll J.S., Collet J.F., Serre L.: Biochemical and structural study of the homologues of the thiol-disulfide oxidoreductase DsbA in Neisseria meningitidis. J. Mol. Biol. 392, 952–966 (2009)
- Lasica A.M., Jagusztyn-Krynicka E.K.: The role of Dsb proteins of Gram-negative bacteria in the process of pathogenesis. FEMS Microbiol. Rev. 31, 626–636 (2007)
- Lasica A.M., Wyszynska A., Szymanek K., Majewski P., Jagusztyn-Krynicka E.K.: Campylobacter protein oxidation influences epithelial cell invasion or intracellular survival as well as intestinal tract colonization in chickens. J. Appl. Genet. 51, 383–393 (2010)
- Leverrier P., Declercq J.P., Denoncin K., Vertommen D., Hini- ker A., Cho S.H., Collet J.F.: Crystal structure of the outer membrane protein RcsF, a new substrate for the periplasmic protein-disulfide isomerase DsbC. J. Biol. Chem.286, 16734–16742 (2011)
- Lin H.H., Tseng L.Y.: DBCP: a web server for disulfide bonding connectivity pattern prediction without the prior knowledge of the bonding state of cysteines. Nucleic Acids Res. 38, W503–507 (2010)
- Marquez-Chamorro A.E., Aguilar-Ruiz J.S.: Soft Computing Methods for Disulfide Connectivity Prediction. Evol. Bioinform. Online, 11, 223–229 (2015)
- McCarthy A.A., Haebel P.W., Torronen A., Rybin V., Baker E.N., Metcalf P.: Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 7, 196–199 (2000)
- McMahon R.M., Premkumar L., Martin J.L.: Four structural subclasses of the antivirulence drug target disulfide oxidoreductase DsbA provide a platform for design of subclass-specific inhibitors. Biochim. Biophys. Acta. 1844, 1391–1401 (2014)
- Messens J., Collet J.F.: Pathways of disulfide bond formation in Escherichia coli. Int. J. Biochem. Cell Biol. 38, 1050–1062 (2006)
- Messens J., Collet J.F., Van Belle K., Brosens E., Loris R., Wyns L.: The oxidase DsbA folds a protein with a nonconsecutive disulfide. J. Biol. Chem. 282, 31302–31307 (2007)
- Premkumar L., Heras B., Duprez W., Walden P., Halili M., Kurth F., Fairlie D.P., Martin J.L.: Rv2969c, essential for optimal growth in Mycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfide oxidases. Acta Crystallogr. D Biol. Crystallogr.69, 1981–1994 (2013)
- Quan S., Schneider I., Pan J., Von Hacht A., Bardwell J.C.: The CXXC motif is more than a redox rheostat. J. Biol. Chem.. 282, 28823–28833 (2007)
- Raines R.T.: Ribonuclease A. Chem. Rev. 98, 1045–1066 (1998)
- Ren G., Champion M.M., Huntley J.F.: Identification of disulfide bond isomerase substrates reveals bacterial virulence factors. Mol. Microbiol.. 94, 926–944 (2014)
- Ren G., Stephan D., Xu Z., Zheng Y., Tang D., Harrison R.S., Kurz M., Jarrott R., Shouldice S.R., Hiniker A., Martin J.L., Heras B., Bardwell J.C.: Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J. Biol. Chem. 284, 10150–10159 (2009)
- Roszczenko P., Radomska K.A., Wywial E., Collet J.F., Jagusztyn-Krynicka E.K.: A novel insight into the oxidoreductase activity of Helicobacter pylori HP0231 protein. PLoS ONE, 7, e46563 (2012)
- Roszczenko P., Grzeszczuk M., Kobierecka P., Wywial E., Urbanowicz P., Wincek P., Nowak E., Jagusztyn-Krynicka E.K.: Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231. BMC Microbiol. 15, 135 (2015)
- Ruiz N., Chng S.S., Hiniker A., Kahne D., Silhavy T.J.: Nonconsecutive disulfide bond formation in an essential integral outer membrane protein. P. Natl. Acad. Sci. USA, 107, 12245–12250 (2010)
- Ruoppolo M., Torella C., Kanda F., Panico M., Pucci P., Marino G., Morris H.R.: Identification of disulphide bonds in the refolding of bovine pancreatic RNase A. Fold. Des. 1, 381–390 (1996)
- Segatori L., Paukstelis P.J., Gilbert H.F., Georgiou G.: Engineered DsbC chimeras catalyze both protein oxidation and disulfide-bond isomerization in Escherichia coli: Reconciling two competing pathways. P. Natl. Acad. Sci. USA, 101, 10018–10023 (2004)
- Shouldice S.R., Heras B., Walden P.M., Totsika M., Schembri M.A., Martin J.L.: Structure and function of DsbA, a key bacterial oxidative folding catalyst. Antioxid. Redox Signal. 14, 1729–1760 (2011)
- Singh R.: A review of algorithmic techniques for disulfide-bond determination. Brief. Funct. Genomic. Proteomic. 7, 157–172 (2008)
- Sinha S., Langford P.R., Kroll J.S.: Functional diversity of three different DsbA proteins from Neisseria meningitidis. Microbiology, 150, 2993–3000 (2004)
- Stirnimann C.U., Grutter M.G., Glockshuber R., Capitani G.: nDsbD: a redox interaction hub in the Escherichia coli periplasm. Cell Mol. Life Sci. 63, 1642–1648 (2006)
- Stirnimann C.U., Rozhkova A., Grauschopf U., Bockmann R.A., Glockshuber R., Capitani G., Grutter M.G.: High-resolution structures of Escherichia coli cDsbD in different redox states: A combined crystallographic, biochemical and computational study. J. Mol. Biol. 358, 829–845 (2006)
- Tinsley C.R., Voulhoux R., Beretti J.L., Tommassen J., Nassif X.: Three homologues, including two membrane-bound proteins, of the disulfide oxidoreductase DsbA in Neisseria meningitidis: effects on bacterial growth and biogenesis of functional type IV pili. J. Biol. Chem.279, 27078–27087 (2004)
- Wang X., Dutton R.J., Beckwith J., Boyd D.: Membrane topology and mutational analysis of Mycobacterium tuberculosis VKOR, a protein involved in disulfide bond formation and a homologue of human vitamin K epoxide reductase. Antioxid. Redox Signal. 14, 1413–1420 (2011)
- Watanabe M.M., Laurindo F.R., Fernandes D.C.: Methods of measuring protein disulfide isomerase activity: a critical overview. Frontiers in chemistry. 2, 73 (2014)
- Williamson J.A., Cho S.H., Ye J., Collet J.F., Beckwith J.R., Chou J.J.: Structure and multistate function of the transmembrane electron transporter CcdA. Nat. Struct. Mol. Biol. 22, 809–814 (2015)
- Wunderlich M., Glockshuber R.: Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli. Protein Sci. 2, 717–726 (1993)
- Yoon J.Y., Kim J., Lee S.J., Kim H.S., Im H.N., Yoon H.J., Kim K.H., Kim S.J., Han B.W., Suh S.W.: Structural and functional characterization of Helicobacter pylori DsbG. FEBS Lett. 585, 3862–3867 (2011)
- Zhou Y., Cierpicki T., Jimenez R.H., Lukasik S.M., Ellena J.F., Cafiso D.S., Kadokura H., Beckwith J., Bushweller J.H.: NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol. Cell. 31, 896–908 (2008)
Language: English, Polish
Page range: 326 - 334
Submitted on: Jan 1, 2017
Accepted on: Mar 1, 2017
Published on: May 22, 2019
Published by: Polish Society of Microbiologists
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© 2019 Elżbieta Katarzyna Jagusztyn-Krynicka, Anna Marta Banaś, Magdalena Joanna Grzeszczuk, published by Polish Society of Microbiologists
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