메뉴 건너뛰기




Volumn 51, Issue 6, 2004, Pages 1745-1755

Induction of the sufA operon encoding Fe-S assembly proteins by superoxide generators and hydrogen peroxide: Involvement of OxyR, IHF and an unidentified oxidant-responsive factor

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYDROGEN PEROXIDE; IRON; OXIDIZING AGENT; SUFA PROTEIN; SULFUR; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 1642565394     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2003.03946.x     Document Type: Article
Times cited : (133)

References (40)
  • 1
    • 0028200484 scopus 로고
    • The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase
    • Altuvia, S., Almiron, M., Huisman, G., Kolter, R., and Storz, G. (1994) The dps promoter is activated by OxyR during growth and by IHF and sigma S in stationary phase. Mol Microbiol 13: 265-272.
    • (1994) Mol Microbiol , vol.13 , pp. 265-272
    • Altuvia, S.1    Almiron, M.2    Huisman, G.3    Kolter, R.4    Storz, G.5
  • 2
    • 0032724622 scopus 로고    scopus 로고
    • Mechanisms for redox control of gene expression
    • Bauer, C.E., Elsen, S., and Bird, T.H. (1999) Mechanisms for redox control of gene expression. Annu Rev Microbiol 53: 495-523.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 495-523
    • Bauer, C.E.1    Elsen, S.2    Bird, T.H.3
  • 3
    • 0032545367 scopus 로고    scopus 로고
    • Regulation of the Salmonella typhimurium flavohemoglobin gene: A new pathway for bacterial gene expression in response to nitric oxide
    • Crawford, M.J., and Goldberg, D.E. (1998) Regulation of the Salmonella typhimurium flavohemoglobin gene: a new pathway for bacterial gene expression in response to nitric oxide. J Biol Chem 273: 34028-34032.
    • (1998) J Biol Chem , vol.273 , pp. 34028-34032
    • Crawford, M.J.1    Goldberg, D.E.2
  • 4
    • 0037168511 scopus 로고    scopus 로고
    • Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron
    • D'Autreaux, B., Touati, D., Bersch, B., Latour, J.M., and Michaud-Soret, I. (2002) Direct inhibition by nitric oxide of the transcriptional ferric uptake regulation protein via nitrosylation of the iron. Proc Natl Acad Sci USA 99: 16619-16624.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16619-16624
    • D'Autreaux, B.1    Touati, D.2    Bersch, B.3    Latour, J.M.4    Michaud-Soret, I.5
  • 5
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint, D.H. (1996) Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J Biol Chem 271: 16068-16074.
    • (1996) J Biol Chem , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 6
    • 0025078495 scopus 로고
    • Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli
    • Greenberg, J.T., Monach, P., Chou, J.H., Josephy, P.D., and Demple, B. (1990) Positive control of a global antioxidant defense regulon activated by superoxide-generating agents in Escherichia coli. Proc Natl Acad Sci USA 87: 6181-6185.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 7
    • 0035985581 scopus 로고    scopus 로고
    • How oxygen damages microbes: Oxygen tolerance and obligate anaerobiosis
    • Imlay, J.A. (2002) How oxygen damages microbes: oxygen tolerance and obligate anaerobiosis. Adv Microb Physiol 46: 111-153.
    • (2002) Adv Microb Physiol , vol.46 , pp. 111-153
    • Imlay, J.A.1
  • 10
    • 0029012855 scopus 로고
    • Isolation of a novel paraquat-inducible (pqi) gene regulated by the soxRS locus in Escherichia coli
    • Koh, Y.S., and Roe, J.H. (1995) Isolation of a novel paraquat-inducible (pqi) gene regulated by the soxRS locus in Escherichia coli. J Bacteriol 177: 2673-2678.
    • (1995) J Bacteriol , vol.177 , pp. 2673-2678
    • Koh, Y.S.1    Roe, J.H.2
  • 11
    • 0032078778 scopus 로고    scopus 로고
    • Mechanism of regulation of 8-hydroxyguanine endonuclease by oxidative stress: Roles of FNR, ArcA, and Fur
    • Lee, H.S., Lee, Y.S., Kim, H.S., Choi, J.Y.H., Hassan, M., and Chung, M.H. (1998) Mechanism of regulation of 8-hydroxyguanine endonuclease by oxidative stress: roles of FNR, ArcA, and Fur. Free Radic Biol Med 24: 1193-1201.
    • (1998) Free Radic Biol Med , vol.24 , pp. 1193-1201
    • Lee, H.S.1    Lee, Y.S.2    Kim, H.S.3    Choi, J.Y.H.4    Hassan, M.5    Chung, M.H.6
  • 12
    • 3042954023 scopus 로고    scopus 로고
    • Isolation and characterization of paraquat-inducible promoters from Escherichia coli
    • Lee, J.H., and Roe, J.H. (1997) Isolation and characterization of paraquat-inducible promoters from Escherichia coli. J Microbiol 35: 277-283.
    • (1997) J Microbiol , vol.35 , pp. 277-283
    • Lee, J.H.1    Roe, J.H.2
  • 13
    • 0037781685 scopus 로고    scopus 로고
    • Regulation of the sufABCDSE operon by Fur
    • Lee, J.H., Yeo, W.S., and Roe, J.H. (2003) Regulation of the sufABCDSE operon by Fur. J Microbiol 41: 109-114.
    • (2003) J Microbiol , vol.41 , pp. 109-114
    • Lee, J.H.1    Yeo, W.S.2    Roe, J.H.3
  • 14
    • 0141532194 scopus 로고    scopus 로고
    • Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
    • Loiseau, L., Ollagnier-De-Choudens, S., Nachin, L., Fontecave, M., and Barras, F. (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem 278: 38352-38359.
    • (2003) J Biol Chem , vol.278 , pp. 38352-38359
    • Loiseau, L.1    Ollagnier-De-Choudens, S.2    Nachin, L.3    Fontecave, M.4    Barras, F.5
  • 15
    • 0037077310 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein
    • Mansy, S.S., Wu, G., Surerus, K.K., and Cowan, J.A. (2002) Iron-sulfur cluster biosynthesis. Thermatoga maritima IscU is a structured iron-sulfur cluster assembly protein. J Biol Chem 277: 21397-21404.
    • (2002) J Biol Chem , vol.277 , pp. 21397-21404
    • Mansy, S.S.1    Wu, G.2    Surerus, K.K.3    Cowan, J.A.4
  • 16
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse, E., and Gottesman, S. (2002) A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc Natl Acad Sci USA 99: 4620-4625.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 17
    • 0039963175 scopus 로고    scopus 로고
    • Paraquat regulation of hmp (Flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S
    • Membrillo-Hernàndez, J., Kim, S.O., Cook, G.M., and Poole, R.K. (1997) Paraquat regulation of hmp (Flavohemoglobin) gene expression in Escherichia coli K-12 is SoxRS independent but modulated by sigma S. J Bacteriol 179: 3164-3170.
    • (1997) J Bacteriol , vol.179 , pp. 3164-3170
    • Membrillo-Hernàndez, J.1    Kim, S.O.2    Cook, G.M.3    Poole, R.K.4
  • 18
    • 0030963659 scopus 로고    scopus 로고
    • Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme
    • Mihara, H., Kurihara, T., Yoshimura, T., Soda, K., and Esaki, N. (1997) Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme. J Biol Chem 272: 22417-22424.
    • (1997) J Biol Chem , vol.272 , pp. 22417-22424
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Soda, K.4    Esaki, N.5
  • 19
    • 0034093325 scopus 로고    scopus 로고
    • Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between 1-cysteine desulfurase and 1-selenocysteine lyase reactions
    • Mihara, H., Kurihara, T., Yoshimura, T., and Esaki, N. (2000) Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between 1-cysteine desulfurase and 1-selenocysteine lyase reactions. J Biochem 127: 559-567.
    • (2000) J Biochem , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 21
    • 0035116079 scopus 로고    scopus 로고
    • SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: The key role of SufC, an orphan ABC ATPase
    • Nachin, L., El Hassouni, M., Loiseau, L., Expert, D., and Barras, F. (2001) SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol Microbiol 39: 960-972.
    • (2001) Mol Microbiol , vol.39 , pp. 960-972
    • Nachin, L.1    El Hassouni, M.2    Loiseau, L.3    Expert, D.4    Barras, F.5
  • 22
    • 0037415722 scopus 로고    scopus 로고
    • SufC: An unorthodox cytoplasmic ABC/ATPase required for (Fe-S) biogenesis under oxidative stress
    • Nachin, L., Loiseau, L., Expert, D., and Barras, F. (2003) SufC: an unorthodox cytoplasmic ABC/ATPase required for (Fe-S) biogenesis under oxidative stress. EMBO J 22: 427-437.
    • (2003) EMBO J , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 23
    • 0027440247 scopus 로고
    • Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages
    • Nunoshiba, T., deRoyas-Walker, J.S., Wishnok, J.S., Tannenbaum, S.R., and Demple, B. (1993) Activation by nitric oxide of an oxidative-stress response that defends Escherichia coli against activated macrophages. Proc Natl Acad Sci USA 90: 9993-9997.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 9993-9997
    • Nunoshiba, T.1    DeRoyas-Walker, J.S.2    Wishnok, J.S.3    Tannenbaum, S.R.4    Demple, B.5
  • 24
    • 0035933791 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: Characterization of IscA and evidence for a specific and functional complex with ferredoxin
    • Ollagnier-de-Choudens, S.T., Mattioli, Y., Takahashi, Y., and Fontecave, M. (2001) Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin. J Biol Chem 276: 22604-22607.
    • (2001) J Biol Chem , vol.276 , pp. 22604-22607
    • Ollagnier-de-Choudens, S.T.1    Mattioli, Y.2    Takahashi, Y.3    Fontecave, M.4
  • 25
    • 0038381472 scopus 로고    scopus 로고
    • SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly
    • Ollagnier-de-Choudens, S.T., Nachin, L., Sanakis, Y., Loiseau, L., Barras, F., and Fontecave, M. (2003) SufA from Erwinia chrysanthemi. Characterization of a scaffold protein required for iron-sulfur cluster assembly. J Biol Chem 278: 17993-18001.
    • (2003) J Biol Chem , vol.278 , pp. 17993-18001
    • Ollagnier-de-Choudens, S.T.1    Nachin, L.2    Sanakis, Y.3    Loiseau, L.4    Barras, F.5    Fontecave, M.6
  • 26
    • 0242664733 scopus 로고    scopus 로고
    • The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in E. coli
    • Outten, F.W., Wood, M.J. Munoz, F.M., and Storz, G. (2003) The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in E. coli. J Biol Chem 278: 45713-45719.
    • (2003) J Biol Chem , vol.278 , pp. 45713-45719
    • Outten, F.W.1    Wood, M.J.2    Munoz, F.M.3    Storz, G.4
  • 27
    • 0032933919 scopus 로고    scopus 로고
    • SufS is a NifS-like protein, and SufD is necessary for stability of the (2Fe-2S) FhuF protein in Escherichia coli
    • Patzer, S.I., and Hantke, K. (1999) SufS is a NifS-like protein, and SufD is necessary for stability of the (2Fe-2S) FhuF protein in Escherichia coli. J Bacteriol 181: 3307-3309.
    • (1999) J Bacteriol , vol.181 , pp. 3307-3309
    • Patzer, S.I.1    Hantke, K.2
  • 28
    • 0035985625 scopus 로고    scopus 로고
    • Global adjustment of microbial physiology during free radical stress
    • Pomposiello, P.J., and Demple, B. (2002) Global adjustment of microbial physiology during free radical stress. Adv Microb Physiol 46: 319-341.
    • (2002) Adv Microb Physiol , vol.46 , pp. 319-341
    • Pomposiello, P.J.1    Demple, B.2
  • 29
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello, P.J., Bennik, M.H., and Demple, B. (2001) Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate. J Bacteriol 183: 3890-3902.
    • (2001) J Bacteriol , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 30
    • 0029831326 scopus 로고    scopus 로고
    • Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12
    • Poole, R.K., Anjum, M.F., Membrillo-Hernàndez, J., Kim, S.O., Hughes, M.N., and Stewart, V. (1996) Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) gene expression in Escherichia coli K-12. J Bacteriol 178: 5487-5492.
    • (1996) J Bacteriol , vol.178 , pp. 5487-5492
    • Poole, R.K.1    Anjum, M.F.2    Membrillo-Hernàndez, J.3    Kim, S.O.4    Hughes, M.N.5    Stewart, V.6
  • 31
    • 0035909963 scopus 로고    scopus 로고
    • IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins
    • Schwartz, C.J., Giel, J.L., Patschkowski, T., Luther, C., Ruzicka, F.J., Beinert, H., and Kiley, P.J. (2001) IscR, an Fe-S cluster-containing transcription factor, represses expression of Escherichia coli genes encoding Fe-S cluster assembly proteins. Proc Natl Acad Sci USA 98: 14895-14900.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14895-14900
    • Schwartz, C.J.1    Giel, J.L.2    Patschkowski, T.3    Luther, C.4    Ruzicka, F.J.5    Beinert, H.6    Kiley, P.J.7
  • 33
    • 0023255472 scopus 로고
    • Improved single and multicopy lacZ-based cloning vectors for protein and operon fusions
    • Simons, R.W., Houman, F., and Kleckner, N. (1987) Improved single and multicopy lacZ-based cloning vectors for protein and operon fusions. Gene 53: 85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 35
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in Archaea and plastids
    • Takahashi, Y., and Tokumoto, U. (2002) A third bacterial system for the assembly of iron-sulfur clusters with homologs in Archaea and plastids. J Biol Chem 277: 28380-28383.
    • (2002) J Biol Chem , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2
  • 36
    • 0028809521 scopus 로고
    • Mapping of the OxyR protein contact site in the C-terminal region of RNA polymerase alpha subunit
    • Tao, K., Zou, C., Fujita, N., and Ishihama, A. (1995) Mapping of the OxyR protein contact site in the C-terminal region of RNA polymerase alpha subunit. J Bacteriol 177: 6740-6744.
    • (1995) J Bacteriol , vol.177 , pp. 6740-6744
    • Tao, K.1    Zou, C.2    Fujita, N.3    Ishihama, A.4
  • 37
    • 0028023175 scopus 로고
    • Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: A mechanism for differential promoter selection
    • Toledano, M.B., Kullik, I., Trinh, F., Baird, P.T., Schneider, T.D., and Storz, G. (1994) Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 78: 897-909.
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, M.B.1    Kullik, I.2    Trinh, F.3    Baird, P.T.4    Schneider, T.D.5    Storz, G.6
  • 38
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F., and 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
  • 40
    • 0034932337 scopus 로고    scopus 로고
    • DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide
    • Zheng, M., Wang, X., Templeton, L.J., Smulski, D.R., Larossa, R.A., and Storz, G. (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    Wang, X.2    Templeton, L.J.3    Smulski, D.R.4    Larossa, R.A.5    Storz, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.