Transcriptional response of Desulfovibrio vulgaris Hildenborough to oxidative stress mimicking environmental conditions

Archives of Microbiology

Volumn 189, Issue 5, 2008, Pages 451-461

  Pereira, Patrícia M ^a,d   He, Qiang ^b,c,e   Xavier, António V ^a   Zhou, Jizhong ^b,c,f   Pereira, Inês A C ^a   Louro, Ricardo O ^a  

^a INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^b OAK RIDGE NATIONAL LABORATORY   (United States)

^c Virtual Institute for Microbial Stress and Survival   (United States)

^d UNIVERSITY OF AVEIRO   (Portugal)

^e University of Tennessee Knoxville   (United States)

^f UNIVERSITY OF OKLAHOMA   (United States)

Author keywords

Desulfovibrio; Fur; Genomics; Hmc; Metalloproteins; Oxidative stress; PerR; Thioredoxin

Indexed keywords

FERRIC UPTAKE REGULATOR; FORMATE DEHYDROGENASE; HEAT SHOCK PROTEIN; HYDROGEN; HYDROGENASE; METAL; METALLOPROTEIN; OXYGEN; PEPTIDASE; PEROXIDE;

ARTICLE; BACTERIAL CELL; CELL FUNCTION; CONCENTRATION (PARAMETERS); CYTOPLASM; DESULFOVIBRIO VULGARIS; DOWN REGULATION; ENERGY METABOLISM; ENVIRONMENTAL FACTOR; ENZYME MECHANISM; GENETIC TRANSCRIPTION; MEMBRANE; MOLECULAR GENETICS; NONHUMAN; OPERON; OXIDATIVE STRESS; PRIORITY JOURNAL; PROMOTER REGION; REDUCTION KINETICS; REGULATORY MECHANISM; UPREGULATION;

BACTERIAL PROTEINS; DESULFOVIBRIO VULGARIS; DNA, BACTERIAL; DOWN-REGULATION; ENVIRONMENTAL MICROBIOLOGY; GENE EXPRESSION REGULATION, BACTERIAL; HEAT-SHOCK PROTEINS; HYDROGENASE; OLIGONUCLEOTIDE ARRAY SEQUENCE ANALYSIS; OPERON; OXIDATION-REDUCTION; OXIDATIVE STRESS; THIOREDOXINS; TRANSCRIPTION, GENETIC; UP-REGULATION;

DESULFOVIBRIO; DESULFOVIBRIO VULGARIS; DESULFOVIBRIO VULGARIS SUBSP. VULGARIS STR. HILDENBOROUGH;

EID: 42449127558     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-007-0335-5     Document Type: Article

References (64)

1. Abreu IA, Xavier AV, LeGall J, Cabelli DE, Teixeira M (2002) Superoxide scavenging by neelaredoxin: dismutation and reduction activities of anaerobes. J Biol Inorg Chem 7:668-674
2. Almeida CC, Romao CV, Lindley PF, Teixeira M, Saraiva LM (2006) The role of the hybrid-cluster protein in oxidative stress defense. J Biol Chem 281:32445-32450
3. Ariza RR, Cohen SP, Bachhawat N, Levy SB, Demple B (1994) Repressor mutations in the marRAB operon that activate oxidative stress genes and multiple antibiotic resistance in Escherichia coli. J Bacteriol 176:143-148
4. Baumgarten A, Redenius I, Kranczoch J, Cypionka H (2001) Periplasmic oxygen reduction by Desulfovibrio species. Arch Microbiol 176:306-309
5. Bender KS et al (2007) Analysis of ferric uptake regulator (Fur) mutant of Desulfovibrio vulgaris Hildenborough. Appl Environ Microbiol 73:5389-5400
6. Buck M, Gallegos MT, Studholme DJ, Guo Y, Gralla JD (2000) The bacterial enhancer-dependent sigma(54) (sigma(N)) transcription factor. J Bacteriol 182:4129-4136
7. Bukau B, Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92:351-366
8. Chen L, Liu MY, Legall J, Fareleira P, Santos H, Xavier AV (1993) Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas. Eur J Biochem 216:443-448
9. Chhabra SR et al (2006) Global analysis of heat shock response in Desulfovibrio vulgaris Hildenborough. J Bacteriol 188:1817-1828
10. Clark ME et al (2006) Temporal transcriptomic analysis as Desulfovibrio vulgaris Hildenborough transitions into stationary phase during electron donor depletion. Appl Environ Microbiol 72:5578-5588
11. Coulter ED, Shenvi NV, Kurtz DM Jr (1999) NADH peroxidase activity of rubrerythrin. Biochem Biophys Res Commun 255:317-323
12. Cypionka H (2000) Oxygen respiration by Desulfovibrio species. Annu Rev Microbiol 54:827-848
13. Darwin AJ (2005) The phage-shock-protein response. Mol Microbiol 57:621-628
14. Deckers HM, Voordouw G (1996) The dcr gene family of Desulfovibrio: implications from the sequence of dcrH and phylogenetic comparison with other mcp genes. Antonie Van Leeuwenhoek 70:21-29
15. Dolla A, Fu R, Brumlik JM, Voordouw G (1992) Nucleotide sequence of dcrA, a Desulfovibrio vulgaris Hildenborough chemoreceptor gene, and its expression in Escherichia coli. J Bacteriol 174:1726-1733
16. Dolla A, Pohorelic BK, Voordouw JK, Voordouw G (2000) Deletion of the hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment. Arch Microbiol 174:143-151
17. Dolla A, Fournier M, Dermoun Z (2006) Oxygen defense in sulfate-reducing bacteria. J Biotechnol 126:87-100
18. dos Santos WG, Pacheco I, Liu M-Y, Teixeira M, Xavier AV, LeGall J (2000) Purification and characterization of an iron superoxide dismutase and a catalase from the sulphate reducing bacterium Desulfovibrio gigas. J Bacteriol 182:796-804
19. Eschemann A, Kuhl M, Cypionka H (1999) Aerotaxis in Desulfovibrio. Environ Microbiol 1:489-494
20. Escolar L, Perez-Martin J, de Lorenzo V (1999) Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181:6223-6229
21. Fournier M et al (2003) Function of oxygen resistance proteins in the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. J Bacteriol 185:71-79
22. Fournier M, Dermoun Z, Durand MC, Dolla A (2004) A new function of the Desulfovibrio vulgaris Hildenborough [Fe] hydrogenase in the protection against oxidative stress. J Biol Chem 279:1787-1793
23. Fournier M, Aubert C, Dermoun Z, Durand MC, Moinier D, Dolla A (2006) Response of the anaerobe Desulfovibrio vulgaris Hildenborough to oxidative conditions: proteome and transcript analysis. Biochimie 88:85-94
24. Fu R, Wall JD, Voordouw G (1994) DcrA, a c-type heme-containing methyl-accepting protein from Desulfovibrio vulgaris Hildenborough, senses the oxygen concentration or redox potential of the environment. J Bacteriol 176:344-350
25. Fuangthong M, Herbig AF, Bsat N, Helmann JD (2002) Regulation of the Bacillus subtilis fur and perR genes by PerR: not all members of the PerR regulon are peroxide inducible. J Bacteriol 184:3276-3286
26. Hantke K (2001) Iron and metal regulation in bacteria. Curr Opin Microbiol 4:172-177
27. Hatchikian EC, Henry YA (1977) An iron containing superoxide dismutase from the strict anaerobe Desulfovibrio desulfuricans (Norway 4). Biochimie 59:153-161
28. Haveman SA, Greene EA, Stilwell CP, Voordouw JK, Voordouw G (2004) Physiological and gene expression analysis of inhibition of Desulfovibrio vulgaris Hildenborough by nitrite. J Bacteriol 186:7944-7950
29. He Q et al (2006) Energetic consequences of nitrite stress in Desulfovibrio vulgaris Hildenborough, inferred from global transcriptional analysis. Appl Environ Microbiol 72:4370-4381
30. Heidelberg JF et al (2004) The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Nat Biotechnol 22:554-559
31. Johnson DC, Dean DR, Smith AD, Johnson MK (2005) Structure, function and formation of biological iron-sulfur clusters. Annu Rev Biochem 74:247-281
32. Kleerebezem M, Crielaard W, Tommassen J (1996) Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the proton motive force under stress conditions. EMBO J 15:162-171
33. Krekeler D, Sigalevich P, Teske A, Cypionka H, Cohen Y (1997) Sulfate-reducing bacterium form the oxic layer of a microbial mat from Solar lake (Sinai), Desulfovibrio sp. nov. Arch Microbiol 167:369-375
34. Krekeler D, Teske A, Cypionka H (1998) Strategies of sulfate-reducing bacteria to escape oxygen stress in a cyanobacterial mat. FEMS Microbiol Ecol 25:89-96
35. Lemos RS, Gomes CM, Santana M, LeGall J, Xavier AV, Teixeira M (2001) The "strict anaerobe" Desulfovibrio gigas contains a membrane-bound oxygen-reducing respiratory chain. FEBS Lett 496:40-43
36. Lindquist S, Craig EA (1988) The heat-shock proteins. Annu Rev Genet 22:631-677
37. Lobo SAL, Melo AMP, Carita JN, Teixeira M, Saraiva LM (2007) The anaerobe Desulfovibrio desulfuricans ATCC 27774 grows at nearly atmospheric oxygen levels. FEBS Lett 581:433-436
38. Lombard M, Fontecave M, Touati D, Niviere V (2000) Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity. J Biol Chem 275:115-121
39. 3. J Biol Inorg Chem 12:1-10
40. Mogk A, Homuth G, Scholz C, Kim L, Schmid FX, Schumann W (1997) The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J 16:4579-4590
41. Moskovitz J (2005) Roles of methionine sulfoxide reductases in antioxidant defense, protein regulation and survival. Curr Pharm Des 11:1451-1457
42. Moura I et al (1990) Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center. J Biol Chem 265:21596-21602
43. Mukhopadhyay A et al (2006) Salt stress in Desulfovibrio vulgaris Hildenborough: an integrated genomics approach. J Bacteriol 188:4068-4078
44. Mukhopadhyay A et al (2007) Cell wide response to low-oxygen exposure in Desulfovibrio vulgaris Hildenborough. J Bacteriol 189:5996-6010
45. Peterson JD, Umayam LA, Dickinson T, Hickey EK, White O (2001) The comprehensive microbial resource. Nucleic Acids Res 29:123-125
46. Pierik AJ, Wolbert RB, Portier GL, Verhagen MF, Hagen WR (1993) Nigerythrin and rubrerythrin from Desulfovibrio vulgaris each contain two mononuclear iron centers and two dinuclear iron clusters. Eur J Biochem 212:237-245
47. Pires RH, Lourenço AI, Morais F, Teixeira M, Xavier AV, Pereira IA (2003) A novel membrane-bound respiratory complex from Desulfovibrio desulfuricans ATCC 27774. Biochim Biophys Acta 1605:67-82
48. Pires RH, Venceslau SS, Morais F, Teixeira M, Xavier AV, Pereira IAC (2006) Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex-a membrane-bound redox complex involved in sulfate respiration. Biochemistry 45:249-262
49. Postgate JR (1984) The sulphate-reducing bacteria, 2nd edn. Cambridge University Press, Cambridge
50. Rabus R, Hansen T, Widdel F (2000) Dissimilatory sulfate- and sulfur-reducing prokaryotes. In: Dworkin M et al (eds) The prokaryotes: an evolving electronic resource for the microbiological community. Springer, New York
51. Rodionov DA, Dubchak I, Arkin A, Alm E, Gelfand MS (2004) Reconstruction of regulatory and metabolic pathways in metal-reducing delta-proteobacteria. Genome Biol 5:R90
52. Rossi M, Pollock WB, Reij MW, Keon RG, Fu R, Voordouw G (1993) The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex. J Bacteriol 175:4699-4711
53. Scholten JCM, Culley DE, Nie L, Munn LC, Brockman FJ, Zhang W (2007) Development and assessment of whole-genome oligonucleotide microarrays to analyze an anaerobic microbial community and its responses to oxidative stress. Biochem Biophys Res Commun 358:571-577
54. Sigalevich P, Meshorer E, Helman Y, Cohen Y (2000) Transition from anaerobic to aerobic growth conditions for the sulfate-reducing bacterium Desulfovibrio oxyclinae results in flocculation. Appl Environ Microbiol 66:5005-5012
55. Valente FM et al (2005) Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase. J Biol Inorg Chem 10:667-682
56. Valente FMA, Almeida CC, Pacheco I, Carita J, Saraiva LM, Pereira IAC (2006) Selenium is involved in regulation of periplasmic hydrogenase gene expression in Desulfovibrio vulgaris Hildenborough. J Bacteriol 188:3228-3235
57. Voordouw JK, Voordouw G (1998) Deletion of the rbo gene increases the oxygen sensitivity of the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Appl Environ Microbiol 64:2882-2887
58. Wall JD, Krumholtz LR (2006) Uranium reduction. Annu Rev Microbiol 60:149-166
59. Weiss R (1970) The solubility of nitrogen, oxygen and argon in water and seawater. Deep Sea Res 17:721-735
60. Wiegert T, Schumann W (2003) Analysis of a DNA-binding motif of the Bacillus subtilis HrcA repressor protein. FEMS Microbiol Lett 223:101-106
61. Xiong J, Kurtz DM Jr, Ai J, Sanders-Loehr J (2000) A hemerythrin-like domain in a bacterial chemotaxis protein. Biochemistry 39:5117-5125
62. Yura T, Nakahigashi K (1999) Regulation of the heat-shock response. Curr Opin Microbiol 2:153-158
63. Zeller T, Klug G (2006) Thioredoxins in bacteria: functions in oxidative stress response and regulation of thioredoxin genes. Naturwissenschaften 93:259-266
64. Zhang W, Culley DE, Hogan M, Vitiritti L, Brockman FJ (2006) Oxidative stress and heat-shock responses in Desulfovibrio vulgaris by genome-wide transcriptomic analysis. Antonie Van Leeuwenhoek 90:41-55