메뉴 건너뛰기




Volumn 80, Issue 10, 2012, Pages 3471-3480

OxyR activation in Porphyromonas gingivalis in response to a hemin-limited environment

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; HEMIN; HYDROGEN PEROXIDE; IRON;

EID: 84867610361     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00680-12     Document Type: Article
Times cited : (23)

References (36)
  • 1
    • 0033025239 scopus 로고    scopus 로고
    • Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient
    • Abdul-Tehrani H, et al. 1999. Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. J. Bacteriol. 181:1415-1428.
    • (1999) J. Bacteriol. , vol.181 , pp. 1415-1428
    • Abdul-Tehrani, H.1
  • 3
    • 0032994431 scopus 로고    scopus 로고
    • Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status
    • Aslund F, Zheng M, Beckwith J, Storz G. 1999. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc. Natl. Acad. Sci. U. S. A. 96:6161- 6165.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 4
    • 78649990332 scopus 로고    scopus 로고
    • Community signalling between Streptococcus gordonii and Porphyromonas gingivalis is controlled by the transcriptional regulator CdhR
    • Chawla A, et al. 2010. Community signalling between Streptococcus gordonii and Porphyromonas gingivalis is controlled by the transcriptional regulator CdhR. Mol. Microbiol. 78:1510 -1522.
    • (2010) Mol. Microbiol. , vol.78 , pp. 1510-1522
    • Chawla, A.1
  • 5
    • 0025302020 scopus 로고
    • Clinical, microbiological and immunological studies on recurrent periodontal disease
    • Choi JI, Nakagawa T, Yamada S, Takazoe I, Okuda K. 1990. Clinical, microbiological and immunological studies on recurrent periodontal disease. J. Clin. Periodontol. 17:426-434.
    • (1990) J. Clin. Periodontol. , vol.17 , pp. 426-434
    • Choi, J.I.1    Nakagawa, T.2    Yamada, S.3    Takazoe, I.4    Okuda, K.5
  • 6
    • 63449142077 scopus 로고    scopus 로고
    • Response of Porphyromonas gingivalis to heme limitation in continuous culture
    • Dashper SG, et al. 2009. Response of Porphyromonas gingivalis to heme limitation in continuous culture. J. Bacteriol. 191:1044 -1055.
    • (2009) J. Bacteriol. , vol.191 , pp. 1044-1055
    • Dashper, S.G.1
  • 7
    • 33645221150 scopus 로고    scopus 로고
    • Role of oxyR in the oral anaerobe Porphyromonas gingivalis
    • Diaz PI, et al. 2006. Role of oxyR in the oral anaerobe Porphyromonas gingivalis. J. Bacteriol. 188:2454 -2462.
    • (2006) J. Bacteriol. , vol.188 , pp. 2454-2462
    • Diaz, P.I.1
  • 8
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr SB, Kogoma T. 1991. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 55:561-585.
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 9
    • 78650051418 scopus 로고    scopus 로고
    • Characterization of a hemophorelike protein from Porphyromonas gingivalis
    • Gao JL, Nguyen KA, Hunter N. 2010. Characterization of a hemophorelike protein from Porphyromonas gingivalis. J. Biol. Chem. 285:40028- 40038.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40028-40038
    • Gao, J.L.1    Nguyen, K.A.2    Hunter, N.3
  • 10
    • 80655125466 scopus 로고    scopus 로고
    • Regulation of perR expression by iron and PerR in Campylobacter jejuni
    • Kim M, Hwang S, Ryu S, Jeon B. 2011. Regulation of perR expression by iron and PerR in Campylobacter jejuni. J. Bacteriol. 193:6171- 6178.
    • (2011) J. Bacteriol. , vol.193 , pp. 6171-6178
    • Kim, M.1    Hwang, S.2    Ryu, S.3    Jeon, B.4
  • 11
    • 72249113435 scopus 로고    scopus 로고
    • Metal uptake in host-pathogen interactions: role of iron in Porphyromonas gingivalis interactions with host organisms
    • Lewis JP. 2010. Metal uptake in host-pathogen interactions: role of iron in Porphyromonas gingivalis interactions with host organisms. Periodontol. 2000 52:94 -116.
    • (2010) Periodontol , vol.2000 , pp. 94-116
    • Lewis, J.P.1
  • 12
    • 0033011371 scopus 로고    scopus 로고
    • Role of superoxide dismutase activity in the physiology of Porphyromonas gingivalis
    • Lynch MC, Kuramitsu HK. 1999. Role of superoxide dismutase activity in the physiology of Porphyromonas gingivalis. Infect. Immun. 67:3367- 3375.
    • (1999) Infect. Immun. , vol.67 , pp. 3367-3375
    • Lynch, M.C.1    Kuramitsu, H.K.2
  • 14
    • 0036047508 scopus 로고    scopus 로고
    • Regulation of inducible peroxide stress responses
    • Mongkolsuk S, Helmann JD. 2002. Regulation of inducible peroxide stress responses. Mol. Microbiol. 45:9 -15.
    • (2002) Mol. Microbiol. , vol.45 , pp. 9-15
    • Mongkolsuk, S.1    Helmann, J.D.2
  • 15
    • 78751685287 scopus 로고    scopus 로고
    • Antibacterial action of polyphosphate on Porphyromonas gingivalis
    • Moon JH, Park JH, Lee JY. 2011. Antibacterial action of polyphosphate on Porphyromonas gingivalis. Antimicrob. Agents Chemother. 55:806- 812.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 806-812
    • Moon, J.H.1    Park, J.H.2    Lee, J.Y.3
  • 16
    • 0041335299 scopus 로고    scopus 로고
    • Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83
    • Nelson KE, et al. 2003. Complete genome sequence of the oral pathogenic bacterium Porphyromonas gingivalis strain W83. J. Bacteriol. 185:5591- 5601.
    • (2003) J. Bacteriol. , vol.185 , pp. 5591-5601
    • Nelson, K.E.1
  • 17
    • 6344241451 scopus 로고    scopus 로고
    • A regulation cascade controls expression of Porphyromonas gingivalis fimbriae via the FimR response regulator
    • Nishikawa K, Yoshimura F, Duncan MJ. 2004. A regulation cascade controls expression of Porphyromonas gingivalis fimbriae via the FimR response regulator. Mol. Microbiol. 54:546 -560.
    • (2004) Mol. Microbiol. , vol.54 , pp. 546-560
    • Nishikawa, K.1    Yoshimura, F.2    Duncan, M.J.3
  • 18
    • 33645543011 scopus 로고    scopus 로고
    • Superoxide dismutase-encoding gene of the obligate anaerobe Porphyromonas gingivalis is regulated by the redox-sensing transcription activator OxyR
    • Ohara N, Kikuchi Y, Shoji M, Naito M, Nakayama K. 2006. Superoxide dismutase-encoding gene of the obligate anaerobe Porphyromonas gingivalis is regulated by the redox-sensing transcription activator OxyR. Microbiology 152:955-966.
    • (2006) Microbiology , vol.152 , pp. 955-966
    • Ohara, N.1    Kikuchi, Y.2    Shoji, M.3    Naito, M.4    Nakayama, K.5
  • 20
    • 0029682161 scopus 로고    scopus 로고
    • In vitro recombination and mutagenesis by overlap extension PCR
    • Pogulis RJ, Vallejo AN, Pease LR. 1996. In vitro recombination and mutagenesis by overlap extension PCR. Methods Mol. Biol. 57:167-176.
    • (1996) Methods Mol. Biol. , vol.57 , pp. 167-176
    • Pogulis, R.J.1    Vallejo, A.N.2    Pease, L.R.3
  • 21
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: the SoxR and OxyR transcription factors
    • Pomposiello PJ, Demple B. 2001. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol. 19:109 -114.
    • (2001) Trends Biotechnol , vol.19 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 23
    • 77952524570 scopus 로고    scopus 로고
    • Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization
    • Shoji M, et al. 2010. Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization. BMC Microbiol. 10:152.
    • (2010) BMC Microbiol , vol.10 , pp. 152
    • Shoji, M.1
  • 24
    • 0032080290 scopus 로고    scopus 로고
    • The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the mu-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism
    • Smalley JW, Silver J, Marsh PJ, Birss AJ. 1998. The periodontopathogen Porphyromonas gingivalis binds iron protoporphyrin IX in the mu-oxo dimeric form: an oxidative buffer and possible pathogenic mechanism. Biochem. J. 331:681- 685.
    • (1998) Biochem. J. , vol.331 , pp. 681-685
    • Smalley, J.W.1    Silver, J.2    Marsh, P.J.3    Birss, A.J.4
  • 25
    • 0029041226 scopus 로고
    • Lethal oxidative damage and mutagenesis are generated by iron in Δfur mutants of Escherichia coli: protective role of superoxide dismutase
    • Touati D, Jacques M, Tardat B, Bouchard L, Despied S. 1995. Lethal oxidative damage and mutagenesis are generated by iron in Δfur mutants of Escherichia coli: protective role of superoxide dismutase. J. Bacteriol. 177:2305-2314.
    • (1995) J. Bacteriol. , vol.177 , pp. 2305-2314
    • Touati, D.1    Jacques, M.2    Tardat, B.3    Bouchard, L.4    Despied, S.5
  • 26
    • 0037371197 scopus 로고    scopus 로고
    • Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis
    • Ueshima J, et al. 2003. Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect. Immun. 71:1170 -1178.
    • (2003) Infect. Immun. , vol.71 , pp. 1170-1178
    • Ueshima, J.1
  • 27
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg ED. 1978. Iron and infection. Microbiol. Rev. 42:45- 66.
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 28
    • 42449090566 scopus 로고    scopus 로고
    • OxyR is involved in coordinate regulation of expression of fimA and sod genes in Porphyromonas gingivalis
    • Wu J, Lin X, Xie H. 2008. OxyR is involved in coordinate regulation of expression of fimA and sod genes in Porphyromonas gingivalis. FEMS Microbiol. Lett. 282:188 -195.
    • (2008) FEMS Microbiol. Lett. , vol.282 , pp. 188-195
    • Wu, J.1    Lin, X.2    Xie, H.3
  • 29
    • 58149484802 scopus 로고    scopus 로고
    • Regulation of hemin binding proteins by a novel transcriptional activator in Porphyromonas gingivalis
    • Wu J, Lin X, Xie H. 2009. Regulation of hemin binding proteins by a novel transcriptional activator in Porphyromonas gingivalis. J. Bacteriol. 191:115-122.
    • (2009) J. Bacteriol. , vol.191 , pp. 115-122
    • Wu, J.1    Lin, X.2    Xie, H.3
  • 30
    • 0030927595 scopus 로고    scopus 로고
    • Environmental regulation of fimbrial gene expression in Porphyromonas gingivalis
    • Xie H, Cai S, Lamont RJ. 1997. Environmental regulation of fimbrial gene expression in Porphyromonas gingivalis. Infect. Immun. 65:2265- 2271.
    • (1997) Infect. Immun. , vol.65 , pp. 2265-2271
    • Xie, H.1    Cai, S.2    Lamont, R.J.3
  • 31
    • 0842348750 scopus 로고    scopus 로고
    • Porphyromonas gingivalis genes involved in fimA regulation
    • Xie H, Kozlova N, Lamont RJ. 2004. Porphyromonas gingivalis genes involved in fimA regulation. Infect. Immun. 72:651- 658.
    • (2004) Infect. Immun. , vol.72 , pp. 651-658
    • Xie, H.1    Kozlova, N.2    Lamont, R.J.3
  • 32
    • 0034303273 scopus 로고    scopus 로고
    • Microbial composition of supra- and subgingival plaque in subjects with adult periodontitis
    • Ximenez-Fyvie LA, Haffajee AD, Socransky SS. 2000. Microbial composition of supra- and subgingival plaque in subjects with adult periodontitis. J. Clin. Periodontol. 27:722-732.
    • (2000) J. Clin. Periodontol. , vol.27 , pp. 722-732
    • Ximenez-Fyvie, L.A.1    Haffajee, A.D.2    Socransky, S.S.3
  • 33
    • 33744808002 scopus 로고    scopus 로고
    • Thioredoxins in bacteria: functions in oxidative stress response and regulation of thioredoxin genes
    • Zeller T, Klug G. 2006. Thioredoxins in bacteria: functions in oxidative stress response and regulation of thioredoxin genes. Naturwissenschaften 93:259 -266.
    • (2006) Naturwissenschaften , vol.93 , pp. 259-266
    • Zeller, T.1    Klug, G.2
  • 34
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng M, Aslund F, Storz G. 1998. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279:1718 -1721.
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 35
    • 0034943657 scopus 로고    scopus 로고
    • Computation-directed identification of OxyR DNA binding sites in Escherichia coli
    • Zheng M, et al. 2001. Computation-directed identification of OxyR DNA binding sites in Escherichia coli. J. Bacteriol. 183:4571- 4579.
    • (2001) J. Bacteriol. , vol.183 , pp. 4571-4579
    • Zheng, M.1
  • 36
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng M, et al. 2001. DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J. Bacteriol. 183:4562- 4570.
    • (2001) J. Bacteriol. , vol.183 , pp. 4562-4570
    • Zheng, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.