A Fur-like protein PerR regulates two oxidative stress response related operons dpr and metQIN in Streptococcus suis

BMC Microbiology

Volumn 12, Issue , 2012, Pages

  Zhang, Tengfei ^a   Ding, Yi ^a   Li, Tingting ^a   Wan, Yun ^a   Li, Wei ^a   Chen, Huanchun ^a   Zhou, Rui ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DPR PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; HYDROGEN PEROXIDE; METHIONINE; METQIN PROTEIN; PERR PROTEIN; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BACTERIUM MUTANT; CONTROLLED STUDY; ELECTROPHORETIC MOBILITY; FEMALE; GENE DELETION; GENE EXPRESSION REGULATION; GENE FUSION; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OPERON; OXIDATIVE STRESS; PROMOTER REGION; REGULON; SEROTYPE; STREPTOCOCCUS SUIS; UPREGULATION; WILD TYPE;

AGOUTI SIGNALING PROTEIN; ANIMALS; ARTIFICIAL GENE FUSION; BACTERIAL PROTEINS; DISEASE MODELS, ANIMAL; DNA, BACTERIAL; DNA-BINDING PROTEINS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; GENE DELETION; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION, BACTERIAL; GENES, REPORTER; GREEN FLUORESCENT PROTEINS; HYDROGEN PEROXIDE; MEMBRANE TRANSPORT PROTEINS; MICE; OPERON; OXIDATIVE STRESS; PROMOTER REGIONS, GENETIC; PROTEIN BINDING; REGULON; REPRESSOR PROTEINS; STREPTOCOCCAL INFECTIONS; STREPTOCOCCUS SUIS; VIRULENCE FACTORS;

MUS; STREPTOCOCCUS SUIS;

EID: 84861556820     PISSN: None     EISSN: 14712180     Source Type: Journal    
DOI: 10.1186/1471-2180-12-85     Document Type: Article

References (45)

1. Opening the iron box: transcriptional metalloregulation by the Fur protein. Escolar L, Perez-Martin J, de Lorenzo V, J Bacteriol 1999 181 20 6223 6229 10515908 (Pubitemid 29512928)
2. The galvanization of biology: a growing appreciation for the roles of zinc. Berg JM, Shi Y, Science 1996 271 5252 1081 1085 10.1126/science.271.5252. 1081 8599083 (Pubitemid 26075222)
3. Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. Gonzalez-Flecha B, Demple B, J Biol Chem 1995 270 23 13681 13687 10.1074/jbc.270.23.13681 7775420
4. Innate immune and chemically triggered oxidative stress modifies translational fidelity. Netzer N, Goodenbour JM, David A, Dittmar KA, Jones RB, Schneider JR, Boone D, Eves EM, Rosner MR, Gibbs JS, et al. Nature 2009 462 7272 522 526 10.1038/nature08576 19940929
5. The mode of action of hydrogen peroxide on deoxyribonucleic acid. Uchida Y, Shigematu H, Yamafuji K, Enzymologia 1965 29 6 369 376 5886616
6. Cell and tissue responses to oxidative damage. Janssen YM, Van Houten B, Borm PJ, Mossman BT, Lab Invest 1993 69 3 261 274 8377469 (Pubitemid 23315710)
7. Peroxide stress elicits adaptive changes in bacterial metal ion homeostasis. Faulkner MJ, Helmann JD, Antioxid Redox Signal 2011 15 1 175 189 10.1089/ars.2010.3682 20977351
8. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Hantke K, Mol Gen Genet 1981 182 2 288 292 10.1007/BF00269672 7026976 (Pubitemid 11007701)
9. The bacterial irr protein is required for coordination of heme biosynthesis with iron availability. Hamza I, Chauhan S, Hassett R, O'Brian MR, J Biol Chem 1998 273 34 21669 21674 10.1074/jbc.273.34.21669 9705301 (Pubitemid 28405340)
10. The ZnuABC high-affinity zinc uptake system and its regulator Zur in Escherichia coli. Patzer SI, Hantke K, Mol Microbiol 1998 28 6 1199 1210 10.1046/j.1365-2958.1998.00883.x 9680209 (Pubitemid 28293543)
11. Characterization of a manganese-dependent regulatory protein, TroR, from Treponema pallidum. Posey JE, Hardham JM, Norris SJ, Gherardini FC, Proc Natl Acad Sci U S A 1999 96 19 10887 10892 10.1073/pnas.96.19.10887 10485921 (Pubitemid 29442239)
12. Nur, a nickel-responsive regulator of the Fur family, regulates superoxide dismutases and nickel transport in Streptomyces coelicolor. Ahn BE, Cha J, Lee EJ, Han AR, Thompson CJ, Roe JH, Mol Microbiol 2006 59 6 1848 1858 10.1111/j.1365-2958.2006.05065.x 16553888
13. Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Bsat N, Herbig A, Casillas-Martinez L, Setlow P, Helmann JD, Mol Microbiol 1998 29 1 189 198 10.1046/j.1365-2958.1998.00921.x 9701813 (Pubitemid 28318573)
14. Identification of a zinc-specific metalloregulatory protein, Zur, controlling zinc transport operons in Bacillus subtilis. Gaballa A, Helmann JD, J Bacteriol 1998 180 22 5815 5821 9811636 (Pubitemid 28514195)
15. Streptococcus suis: an emerging human pathogen. Wertheim HF, Nghia HD, Taylor W, Schultsz C, Clin Infect Dis 2009 48 5 617 625 10.1086/596763 19191650
16. Streptococcal toxic shock syndrome caused by Streptococcus suis serotype 2. Tang J, Wang C, Feng Y, Yang W, Song H, Chen Z, Yu H, Pan X, Zhou X, Wang H, et al. PLoS Med 2006 3 5 151 10.1371/journal.pmed.0030151 16584289 (Pubitemid 43807036)
17. Streptococcus suis: an emerging zoonotic pathogen. Lun ZR, Wang QP, Chen XG, Li AX, Zhu XQ, Lancet Infect Dis 2007 7 3 201 209 10.1016/S1473-3099(07) 70001-4 17317601 (Pubitemid 46274507)
18. Functional definition and global regulation of Zur, a zinc uptake regulator in a Streptococcus suis serotype 2 strain causing streptococcal toxic shock syndrome. Feng Y, Li M, Zhang H, Zheng B, Han H, Wang C, Yan J, Tang J, Gao GF, J Bacteriol 2008 190 22 7567 7578 10.1128/JB.01532-07 18723622
19. Contribution of the FeoB transporter to Streptococcus suis virulence. Aranda J, Cortes P, Garrido ME, Fittipaldi N, Llagostera M, Gottschalk M, Barbe J, Int Microbiol 2009 12 2 137 143 19784934
20. The regulator PerR is involved in oxidative stress response and iron homeostasis and is necessary for full virulence of Streptococcus pyogenes. Ricci S, Janulczyk R, Bjorck L, Infect Immun 2002 70 9 4968 4976 10.1128/IAI.70.9. 4968-4976.2002 12183543
21. The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Brenot A, King KY, Caparon MG, Mol Microbiol 2005 55 1 221 234 15612930 (Pubitemid 40127898)
22. PerR confers phagocytic killing resistance and allows pharyngeal colonization by group A Streptococcus. Gryllos I, Grifantini R, Colaprico A, Cary ME, Hakansson A, Carey DW, Suarez-Chavez M, Kalish LA, Mitchell PD, White GL, et al. PLoS Pathog 2008 4 9 1000145 10.1371/journal.ppat.1000145 18773116
23. The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation. Lee JW, Helmann JD, Nature 2006 440 7082 363 367 10.1038/nature04537 16541078
24. Molecular basis of H2O2 resistance mediated by Streptococcal Dpr: Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. Pulliainen AT, Haataja S, Kahkonen S, Finne J, J Biol Chem 2003 278 10 7996 8005 10.1074/jbc.M210174200 12501248 (Pubitemid 36800538)
25. The cation-uptake regulators AdcR and Fur are necessary for full virulence of Streptococcus suis. Aranda J, Garrido ME, Fittipaldi N, Cortes P, Llagostera M, Gottschalk M, Barbe J, Vet Microbiol 2010 144 1-2 246 249 20133089
26. PerR acts as a switch for oxygen tolerance in the strict anaerobe Clostridium acetobutylicum. Hillmann F, Fischer RJ, Saint-Prix F, Girbal L, Bahl H, Mol Microbiol 2008 68 4 848 860 10.1111/j.1365-2958.2008.06192.x 18430081 (Pubitemid 351596334)
27. PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Horsburgh MJ, Clements MO, Crossley H, Ingham E, Foster SJ, Infect Immun 2001 69 6 3744 3754 10.1128/IAI.69.6.3744-3754.2001 11349039 (Pubitemid 32493293)
28. Derepression of the Bacillus subtilis PerR peroxide stress response leads to iron deficiency. Faulkner MJ, Ma Z, Fuangthong M, Helmann JD, J Bacteriol 2012 194 5 1226 1235 10.1128/JB.06566-11 22194458
29. Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Herbig AF, Helmann JD, Mol Microbiol 2001 41 4 849 859 11532148 (Pubitemid 34208994)
30. Dps-like proteins: structural and functional insights into a versatile protein family. Haikarainen T, Papageorgiou AC, Cell Mol Life Sci 2010 67 3 341 351 10.1007/s00018-009-0168-2 19826764
31. Dps/Dpr ferritin-like protein: insights into the mechanism of iron incorporation and evidence for a central role in cellular iron homeostasis in Streptococcus suis. Pulliainen AT, Kauko A, Haataja S, Papageorgiou AC, Finne J, Mol Microbiol 2005 57 4 1086 1100 10.1111/j.1365-2958.2005.04756.x 16091046 (Pubitemid 41139868)
32. Structural and thermodynamic characterization of metal ion binding in Streptococcus suis Dpr. Haikarainen T, Thanassoulas A, Stavros P, Nounesis G, Haataja S, Papageorgiou AC, J Mol Biol 2010 405 2 448 460 21056572
33. Methionine sulfoxide reductases and virulence of bacterial pathogens. Sasindran SJ, Saikolappan S, Dhandayuthapani S, Future Microbiol 2007 2 6 619 630 10.2217/17460913.2.6.619 18041903
34. Methionine sulfoxide reductases: relevance to aging and protection against oxidative stress. Cabreiro F, Picot CR, Friguet B, Petropoulos I, Ann N Y Acad Sci 2006 1067 37 44 10.1196/annals.1354.006 16803968 (Pubitemid 43806307)
35. Methionine sulfoxide reductases in prokaryotes. Ezraty B, Aussel L, Barras F, Biochim Biophys Acta 2005 1703 2 221 229 10.1016/j.bbapap.2004.08.017 15680230 (Pubitemid 40170445)
36. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Moskovitz J, Biochim Biophys Acta 2005 1703 2 213 219 10.1016/j.bbapap.2004.09.003 15680229 (Pubitemid 40170444)
37. The metNPQ operon of Bacillus subtilis encodes an ABC permease transporting methionine sulfoxide, D- and L-methionine. Hullo MF, Auger S, Dassa E, Danchin A, Martin-Verstraete I, Res Microbiol 2004 155 2 80 86 10.1016/j.resmic.2003.11.008 14990259 (Pubitemid 38249557)
38. Grifantini R, Toukoki C, Colaprico A The Peroxide Stimulon and the Role of PerR in Group A Streptococcus. J Bacteriol, Gryllos I 2011
39. Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein. Traore DA, El Ghazouani A, Jacquamet L, Borel F, Ferrer JL, Lascoux D, Ravanat JL, Jaquinod M, Blondin G, Caux-Thang C, et al. Nat Chem Biol 2009 5 1 53 59 10.1038/nchembio.133 19079268
40. Identification of Streptococcus suis genes preferentially expressed under iron starvation by selective capture of transcribed sequences. Li W, Liu L, Chen H, Zhou R, FEMS Microbiol Lett 2009 292 1 123 133 10.1111/j.1574-6968.2008. 01476.x 19191874
41. Growth characteristics of group A streptococci in a new chemically defined medium. van de Rijn I, Kessler RE, Infect Immun 1980 27 2 444 448 6991416 (Pubitemid 10144935)
42. Thermosensitive suicide vectors for gene replacement in Streptococcus suis. Takamatsu D, Osaki M, Sekizaki T, Plasmid 2001 46 2 140 148 10.1006/plas.2001.1532 11591139 (Pubitemid 32980676)
43. Aerotolerance and peroxide resistance in peroxidase and PerR mutants of Streptococcus pyogenes. King KY, Horenstein JA, Caparon MG, J Bacteriol 2000 182 19 5290 5299 10.1128/JB.182.19.5290-5299.2000 10986229
44. Construction and characterization of Streptococcus suis-Escherichia coli shuttle cloning vectors. Takamatsu D, Osaki M, Sekizaki T, Plasmid 2001 45 2 101 113 10.1006/plas.2000.1510 11322824 (Pubitemid 32221956)
45. Shuttle vectors containing a multiple cloning site and a lacZ alpha gene for conjugal transfer of DNA from Escherichia coli to gram-positive bacteria. Trieu-Cuot P, Carlier C, Poyart-Salmeron C, Courvalin P, Gene 1991 102 1 99 104 10.1016/0378-1119(91)90546-N 1864514