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Volumn 150, Issue 2, 2004, Pages 497-512

Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; METHIONINE; PEROXIDE; PROTEOME; REACTIVE OXYGEN METABOLITE; SULFATE; SUPEROXIDE;

EID: 1242318677     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26665-0     Document Type: Article
Times cited : (208)

References (68)
  • 1
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C. & Spizizen, J. (1961). Requirements for transformation in Bacillus subtilis. J Bacteriol 81, 741-746.
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 2
    • 0030800698 scopus 로고    scopus 로고
    • First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis
    • Antelmann, H., Bernhardt, J., Schmid, R., Mach, H., Völker, U. & Hecker, M. (1997). First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis. Electrophoresis 18, 1451-1463.
    • (1997) Electrophoresis , vol.18 , pp. 1451-1463
    • Antelmann, H.1    Bernhardt, J.2    Schmid, R.3    Mach, H.4    Völker, U.5    Hecker, M.6
  • 3
    • 0019475137 scopus 로고
    • Manganese and defenses against oxygen toxicity in Lactobacillus plantarum
    • Archibald, F. S. & Fridovich, I. (1981). Manganese and defenses against oxygen toxicity in Lactobacillus plantarum. J Bacteriol 145, 442-451.
    • (1981) J. Bacteriol. , vol.145 , pp. 442-451
    • Archibald, F.S.1    Fridovich, I.2
  • 4
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes in vitro
    • Archibald, F. S. & Fridovich, I. (1982). The scavenging of superoxide radical by manganous complexes in vitro. Arch Biochem Biophys 214, 452-463.
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 5
    • 0036724254 scopus 로고    scopus 로고
    • Global expression profile of Bacillus subtilis grown in the presence of sulfate or methionine
    • Auger, S., Danchin, A. & Martin-Verstraete, I. (2002). Global expression profile of Bacillus subtilis grown in the presence of sulfate or methionine. J Bacteriol 184, 5179-5186.
    • (2002) J. Bacteriol. , vol.184 , pp. 5179-5186
    • Auger, S.1    Danchin, A.2    Martin-Verstraete, I.3
  • 6
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon
    • Baichoo, N., Wang, T., Ye, R. & Helmann, J. D. (2002). Global analysis of the Bacillus subtilis Fur regulon and the iron starvation stimulon. Mol Microbiol 45, 1613-1629.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 7
    • 0033548265 scopus 로고    scopus 로고
    • Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli. The transketolase connection
    • Benov, L. & Fridovich, I. (1999). Why superoxide imposes an aromatic amino acid auxotrophy on Escherichia coli. The transketolase connection. J Biol Chem 274, 4202-4206.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4202-4206
    • Benov, L.1    Fridovich, I.2
  • 8
    • 0036406739 scopus 로고    scopus 로고
    • Induction of the SoxRS regulon of Escherichia coli by glycolaldehyde
    • Benov, L. & Fridovich, I. (2002). Induction of the SoxRS regulon of Escherichia coli by glycolaldehyde. Arch Biochem Biophys 407, 45-48.
    • (2002) Arch. Biochem. Biophys. , vol.407 , pp. 45-48
    • Benov, L.1    Fridovich, I.2
  • 9
    • 0029787379 scopus 로고    scopus 로고
    • The mechanism of the auxotrophy for sulfur-containing amino acids imposed upon Escherichia coli by superoxide
    • Benov, L., Kredich, N. M. & Fridovich, I. (1996). The mechanism of the auxotrophy for sulfur-containing amino acids imposed upon Escherichia coli by superoxide. J Biol Chem 271, 21037-21040.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21037-21040
    • Benov, L.1    Kredich, N.M.2    Fridovich, I.3
  • 10
    • 0344329881 scopus 로고    scopus 로고
    • Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis
    • Bernhardt, J., Buttner, K., Scharf, C. & Hecker, M. (1999). Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis. Electrophoresis 20, 2225-2240.
    • (1999) Electrophoresis , vol.20 , pp. 2225-2240
    • Bernhardt, J.1    Buttner, K.2    Scharf, C.3    Hecker, M.4
  • 11
    • 0029010808 scopus 로고
    • Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: Effects of intracellular superoxide dismutase on its inactivation by oxidant stress
    • Brown, O. R., Smyk-Randall, E., Draczynska-Lusiak, B. & Fee, J. A. (1995). Dihydroxy-acid dehydratase, a [4Fe-4S] cluster-containing enzyme in Escherichia coli: effects of intracellular superoxide dismutase on its inactivation by oxidant stress. Arch Biochem Biophys 319, 10-22.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 10-22
    • Brown, O.R.1    Smyk-Randall, E.2    Draczynska-Lusiak, B.3    Fee, J.A.4
  • 12
    • 0029854169 scopus 로고    scopus 로고
    • Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes
    • Bsat, N., Chen, L. & Helmann, J. D. (1996). Mutation of the Bacillus subtilis alkyl hydroperoxide reductase (ahpCF) operon reveals compensatory interactions among hydrogen peroxide stress genes. J Bacteriol 178, 6579-6586.
    • (1996) J. Bacteriol. , vol.178 , pp. 6579-6586
    • Bsat, N.1    Chen, L.2    Helmann, J.D.3
  • 13
    • 0031850630 scopus 로고    scopus 로고
    • 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, J. D. (1998). Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol Microbiol 29, 189-198.
    • (1998) Mol. Microbiol. , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 14
    • 0034837018 scopus 로고    scopus 로고
    • A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis
    • 7 other authors
    • Büttner, K., Bernhardt, J., Scharf, C. & 7 other authors (2001). A comprehensive two-dimensional map of cytosolic proteins of Bacillus subtilis. Electrophoresis 22, 2908-2935.
    • (2001) Electrophoresis , vol.22 , pp. 2908-2935
    • Büttner, K.1    Bernhardt, J.2    Scharf, C.3
  • 15
    • 0022683672 scopus 로고
    • Isolation of superoxide dismutase mutants in Escherichia coli: Is superoxide dismutase necessary for aerobic life?
    • Carlioz, A. & Touati, D. (1986). Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J 5, 623-630.
    • (1986) EMBO J. , vol.5 , pp. 623-630
    • Carlioz, A.1    Touati, D.2
  • 16
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae, H. Z., Chung, S. J. & Rhee, S. G. (1994). Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269, 27670-27678.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 17
    • 0029152774 scopus 로고
    • Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions
    • Chen, L., Keramati, L. & Helmann, J. D. (1995). Coordinate regulation of Bacillus subtilis peroxide stress genes by hydrogen peroxide and metal ions. Proc Natl Acad Sci U S A 92, 8190-8194.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8190-8194
    • Chen, L.1    Keramati, L.2    Helmann, J.D.3
  • 18
    • 0342333739 scopus 로고
    • OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins
    • Christman, M. F., Storz, G. & Ames, B. N. (1989). OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci U S A 86, 3484-3488.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 3484-3488
    • Christman, M.F.1    Storz, G.2    Ames, B.N.3
  • 20
    • 0023490127 scopus 로고
    • Relationship among oxidative stress, growth cycle, and sporulation in Bacillus subtilis
    • Dowds, B. C., Murphy, P., McConnell, D. J. & Devine, K. M. (1987). Relationship among oxidative stress, growth cycle, and sporulation in Bacillus subtilis. J Bacteriol 169, 5771-5775.
    • (1987) J. Bacteriol. , vol.169 , pp. 5771-5775
    • Dowds, B.C.1    Murphy, P.2    McConnell, D.J.3    Devine, K.M.4
  • 21
    • 0036223585 scopus 로고    scopus 로고
    • Bacillus subtilis functional genomics: Global characterization of the stringent response by proteome and transcriptome analysis
    • Eymann, C., Homuth, G., Scharf, C. & Hecker, M. (2002). Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis. J Bacteriol 184, 2500-2520.
    • (2002) J. Bacteriol. , vol.184 , pp. 2500-2520
    • Eymann, C.1    Homuth, G.2    Scharf, C.3    Hecker, M.4
  • 22
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr, S. B. & 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
  • 23
    • 0026497715 scopus 로고
    • Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells
    • Fernando, M. R., Nanri, H., Yoshitake, S., Nagata-Kuno, K. & Minakami, S. (1992). Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells. Eur J Biochem 209, 917-922.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 917-922
    • Fernando, M.R.1    Nanri, H.2    Yoshitake, S.3    Nagata-Kuno, K.4    Minakami, S.5
  • 24
    • 0038820069 scopus 로고    scopus 로고
    • Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response
    • Fitzpatrick, T. B., Amrhein, N. & Macheroux, P. (2003). Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response. J Biol Chem 278, 19891-19897.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19891-19897
    • Fitzpatrick, T.B.1    Amrhein, N.2    Macheroux, P.3
  • 25
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich, I. (1995). Superoxide radical and superoxide dismutases. Annu Rev Biochem 64, 97-112.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 26
    • 0030806863 scopus 로고    scopus 로고
    • -), superoxide dismutases, and related matters
    • -), superoxide dismutases, and related matters. J Biol Chem 272, 18515-18517.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 27
    • 0034971954 scopus 로고    scopus 로고
    • OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis
    • Fuangthong, M., Atichartpongkul, S., Mongkolsuk, S. & Helmann, J. D. (2001). OhrR is a repressor of ohrA, a key organic hydroperoxide resistance determinant in Bacillus subtilis. J Bacteriol 183, 4134-4141.
    • (2001) J. Bacteriol. , vol.183 , pp. 4134-4141
    • Fuangthong, M.1    Atichartpongkul, S.2    Mongkolsuk, S.3    Helmann, J.D.4
  • 28
    • 0036267391 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis fur and perR genes by PerR: Not all members of the PerR regulon are peroxide inducible
    • Fuangthong, M., Herbig, A. F., Bsat, N. & Helmann, J. D. (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.
    • (2002) J. Bacteriol. , vol.184 , pp. 3276-3286
    • Fuangthong, M.1    Herbig, A.F.2    Bsat, N.3    Helmann, J.D.4
  • 29
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli aconitase
    • Gardner, P. R. & Fridovich, I. (1991). Superoxide sensitivity of the Escherichia coli aconitase. J Biol Chem 266, 19328-19333.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 30
    • 0031048106 scopus 로고    scopus 로고
    • Regulation of the SoxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo
    • Gaudu, P., Moon, N. & Weiss, B. (1997). Regulation of the SoxRS oxidative stress regulon. Reversible oxidation of the Fe-S centers of SoxR in vivo. J Biol Chem 272, 5082-5086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5082-5086
    • Gaudu, P.1    Moon, N.2    Weiss, B.3
  • 31
    • 0024343602 scopus 로고
    • A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress
    • Greenberg, J. T. & Demple, B. (1989). A global response induced in Escherichia coli by redox-cycling agents overlaps with that induced by peroxide stress. J Bacteriol 171, 3933-3939.
    • (1989) J. Bacteriol. , vol.171 , pp. 3933-3939
    • Greenberg, J.T.1    Demple, B.2
  • 32
    • 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. & Demple, B. (1990). Positive control of a global antioxidant defense regulon activated by superoxide- generating agents in Escherichia coli. Proc Natl Acad Sci U S A 87, 6181-6185.
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 6181-6185
    • Greenberg, J.T.1    Monach, P.2    Chou, J.H.3    Josephy, P.D.4    Demple, B.5
  • 33
    • 0031735563 scopus 로고    scopus 로고
    • The S box regulon: A new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria
    • Grundy, F. J. & Henkin, T. M. (1998). The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria. Mol Microbiol 30, 737-749.
    • (1998) Mol. Microbiol. , vol.30 , pp. 737-749
    • Grundy, F.J.1    Henkin, T.M.2
  • 34
    • 0034987011 scopus 로고    scopus 로고
    • General stress response of Bacillus subtilis and other bacteria
    • Hecker, M. & Völker, U. (2001). General stress response of Bacillus subtilis and other bacteria. Adv Microb Physiol 44, 35-91.
    • (2001) Adv. Microb. Physiol. , vol.44 , pp. 35-91
    • Hecker, M.1    Völker, U.2
  • 35
    • 0037215627 scopus 로고    scopus 로고
    • The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors
    • Helmann, J. D., Wu, M. F., Gaballa, A., Kobel, P. A., Morshedi, M. M., Fawcett, P. & Paddon, C. (2003). The global transcriptional response of Bacillus subtilis to peroxide stress is coordinated by three transcription factors. J Bacteriol 185, 243-253.
    • (2003) J. Bacteriol. , vol.185 , pp. 243-253
    • Helmann, J.D.1    Wu, M.F.2    Gaballa, A.3    Kobel, P.A.4    Morshedi, M.M.5    Fawcett, P.6    Paddon, C.7
  • 36
    • 0030797051 scopus 로고    scopus 로고
    • Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide
    • Henle, E. S. & Linn, S. (1997). Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide. J Biol Chem 272, 19095-19098.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19095-19098
    • Henle, E.S.1    Linn, S.2
  • 37
    • 0035723780 scopus 로고    scopus 로고
    • Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA
    • Herbig, A. F. & Helmann, J. D. (2001). Roles of metal ions and hydrogen peroxide in modulating the interaction of the Bacillus subtilis PerR peroxide regulon repressor with operator DNA. Mol Microbiol 41, 849-859.
    • (2001) Mol. Microbiol. , vol.41 , pp. 849-859
    • Herbig, A.F.1    Helmann, J.D.2
  • 38
    • 0003003066 scopus 로고    scopus 로고
    • Metal ion uptake and oxidative stress
    • Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology
    • Herbig, A. & Helmann, J. D. (2002). Metal ion uptake and oxidative stress. In Bacillus and its Closest Relatives, pp. 405-414. Edited by A. L. Sonenshein, J. A. Hoch & R. Losick. Washington, DC: American Society for Microbiology.
    • (2002) Bacillus and Its Closest Relatives , pp. 405-414
    • Herbig, A.1    Helmann, J.D.2
  • 39
    • 0030936964 scopus 로고    scopus 로고
    • Redox signal transduction: Mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form
    • Hidalgo, E., Ding, H. & Demple, B. (1997). Redox signal transduction: mutations shifting [2Fe-2S] centers of the SoxR sensor-regulator to the oxidized form. Cell 88, 121-129.
    • (1997) Cell , vol.88 , pp. 121-129
    • Hidalgo, E.1    Ding, H.2    Demple, B.3
  • 40
    • 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
  • 41
    • 0025800392 scopus 로고
    • Assay of metabolic superoxide production in Escherichia coli
    • Imlay, J. A. & Fridovich, I. (1991). Assay of metabolic superoxide production in Escherichia coli. J Biol Chem 266, 6957-6965.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6957-6965
    • Imlay, J.A.1    Fridovich, I.2
  • 42
    • 0032464905 scopus 로고    scopus 로고
    • Molecular cloning and nucleoticle sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis
    • Inaoka, T., Matsumura, Y. & Tsuchido, T. (1998). Molecular cloning and nucleoticle sequence of the superoxide dismutase gene and characterization of its product from Bacillus subtilis. J Bacteriol 180, 3697-3703.
    • (1998) J. Bacteriol. , vol.180 , pp. 3697-3703
    • Inaoka, T.1    Matsumura, Y.2    Tsuchido, T.3
  • 43
    • 0033037716 scopus 로고    scopus 로고
    • SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of Bacillus subtilis
    • Inaoka, T., Matsumura, Y. & Tsuchido, T. (1999). SodA and manganese are essential for resistance to oxidative stress in growing and sporulating cells of Bacillus subtilis. J Bacteriol 181, 1939-1943.
    • (1999) J. Bacteriol. , vol.181 , pp. 1939-1943
    • Inaoka, T.1    Matsumura, Y.2    Tsuchido, T.3
  • 44
    • 0037326508 scopus 로고    scopus 로고
    • Identification of a protein, YneA, responsible for cell division suppression during the SOS response in Bacillus subtilis
    • Kawai, Y., Moriya, S. & Ogasawara, N. (2003). Identification of a protein, YneA, responsible for cell division suppression during the SOS response in Bacillus subtilis. Mol Microbiol 47, 1113-1122.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1113-1122
    • Kawai, Y.1    Moriya, S.2    Ogasawara, N.3
  • 45
    • 0035951874 scopus 로고    scopus 로고
    • Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: Alteration of pyridine nucleotide binding by a single amino acid substitution
    • Kobori, T., Sasaki, H., Lee, W. C., Zenno, S., Saigo, K., Murphy, M. E. & Tanokura, M. (2001). Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution. J Biol Chem 276, 2816-2823.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2816-2823
    • Kobori, T.1    Sasaki, H.2    Lee, W.C.3    Zenno, S.4    Saigo, K.5    Murphy, M.E.6    Tanokura, M.7
  • 46
    • 0032431906 scopus 로고    scopus 로고
    • The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes
    • Krüger, E. & Hecker, M. (1998). The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes. J Bacteriol 180, 6681-6688.
    • (1998) J. Bacteriol. , vol.180 , pp. 6681-6688
    • Krüger, E.1    Hecker, M.2
  • 47
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the gram-positive bacterium Bacillus subtilis
    • 148 other authors
    • Kunst, F., Ogasawara, N., Moszer, I. & 148 other authors (1997). The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, F.1    Ogasawara, N.2    Moszer, I.3
  • 48
    • 0037334843 scopus 로고    scopus 로고
    • Global characterization of disulfide stress in Bacillus subtilis
    • Leichert, L. I., Scharf, C. & Hecker, M. (2003). Global characterization of disulfide stress in Bacillus subtilis. J Bacteriol 185, 1967-1975.
    • (2003) J. Bacteriol. , vol.185 , pp. 1967-1975
    • Leichert, L.I.1    Scharf, C.2    Hecker, M.3
  • 49
    • 0345192734 scopus 로고
    • DNA-damage-inducible (din) loci are transcriptionally activated in competent Bacillus subtilis
    • Love, P. E., Lyle, M. J. & Yasbin, R. E. (1985). DNA-damage-inducible (din) loci are transcriptionally activated in competent Bacillus subtilis. Proc Natl Acad Sci U S A 82, 6201-6205.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 6201-6205
    • Love, P.E.1    Lyle, M.J.2    Yasbin, R.E.3
  • 50
    • 0038210214 scopus 로고    scopus 로고
    • Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria
    • Mandal, M., Boese, B., Barrick, J. E., Winkler, W. C. & Breaker, R. R. (2003). Riboswitches control fundamental biochemical pathways in Bacillus subtilis and other bacteria. Cell 113, 577-586.
    • (2003) Cell , vol.113 , pp. 577-586
    • Mandal, M.1    Boese, B.2    Barrick, J.E.3    Winkler, W.C.4    Breaker, R.R.5
  • 51
    • 0037453069 scopus 로고    scopus 로고
    • Transcription termination control of the S box system: Direct measurement of S-adenosylmethionine by the leader RNA
    • McDaniel, B. A., Grundy, F. J., Artsimovitch, I. & Henkin, T. M. (2003). Transcription termination control of the S box system: direct measurement of S-adenosylmethionine by the leader RNA. Proc Natl Acad Sci U S A 100, 3083-3088.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 3083-3088
    • McDaniel, B.A.1    Grundy, F.J.2    Artsimovitch, I.3    Henkin, T.M.4
  • 52
    • 0033538048 scopus 로고    scopus 로고
    • The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli
    • Messner, K. R. & Imlay, J. A. (1999). The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J Biol Chem 274, 10119-10128.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10119-10128
    • Messner, K.R.1    Imlay, J.A.2
  • 53
    • 0030479502 scopus 로고    scopus 로고
    • The Bacillus subtilis dinR gene codes for the analogue of Escherichia coli LexA. Purification and characterization of the DinR protein
    • Miller, M. C., Resnick, J. B., Smith, B. T. & Lovett, C. M., Jr (1996). The Bacillus subtilis dinR gene codes for the analogue of Escherichia coli LexA. Purification and characterization of the DinR protein. J Biol Chem 271, 33502-33508.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33502-33508
    • Miller, M.C.1    Resnick, J.B.2    Smith, B.T.3    Lovett Jr., C.M.4
  • 54
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: Regulation of expression and role in protecting against oxidative damage
    • Moskovitz, J., Rahman, M. A., Strassman, J., Yancey, S. O., Kushner, S. R., Brot, N. & Weissbach, H. (1995). Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J Bacteriol 177, 502-507.
    • (1995) J. Bacteriol. , vol.177 , pp. 502-507
    • Moskovitz, J.1    Rahman, M.A.2    Strassman, J.3    Yancey, S.O.4    Kushner, S.R.5    Brot, N.6    Weissbach, H.7
  • 55
    • 0023491512 scopus 로고
    • Oxidative stress and growth temperature in Bacillus subtilis
    • Murphy, P., Dowds, B. C., McConnell, D. J. & Devine, K. M. (1987). Oxidative stress and growth temperature in Bacillus subtilis. J Bacteriol 169, 5766-5770.
    • (1987) J. Bacteriol. , vol.169 , pp. 5766-5770
    • Murphy, P.1    Dowds, B.C.2    McConnell, D.J.3    Devine, K.M.4
  • 56
    • 9244225687 scopus 로고    scopus 로고
    • Distribution of thiols in microorganisms: Mycothiol is a major thiol in most actinomycetes
    • 7 other authors
    • Newton, G. L., Arnold, K., Price, M. S. & 7 other authors (1996). Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J Bacteriol 178, 1990-1995.
    • (1996) J. Bacteriol. , vol.178 , pp. 1990-1995
    • Newton, G.L.1    Arnold, K.2    Price, M.S.3
  • 58
    • 0035985625 scopus 로고    scopus 로고
    • Global adjustment of microbial physiology during free radical stress
    • Pomposiello, P. J. & 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
  • 60
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman, E. R. (1993). Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem 62, 797-821.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 61
    • 0002463721 scopus 로고    scopus 로고
    • Oxidative stress
    • Edited by G. Storz & R. Hengge-Aronis. Washington, DC: American Society for Microbiology
    • Storz, G. & Zheng, M. (2000). Oxidative stress. In Bacterial Stress Responses, pp. 47-60. Edited by G. Storz & R. Hengge-Aronis. Washington, DC: American Society for Microbiology.
    • (2000) Bacterial Stress Responses , pp. 47-60
    • Storz, G.1    Zheng, M.2
  • 62
    • 0027524789 scopus 로고
    • Temporal activation of betaglucanase synthesis in Bacillus subtilis is mediated by the GTP pool
    • Stülke, J., Hanschke, R. & Hecker, M. (1993). Temporal activation of betaglucanase synthesis in Bacillus subtilis is mediated by the GTP pool. J Gen Microbiol 139, 2041-2045.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2041-2045
    • Stülke, J.1    Hanschke, R.2    Hecker, M.3
  • 63
    • 0023129314 scopus 로고
    • Differential induction of heat shock, SOS, and oxidation stress regulons and accumulation of nucleotides in Escherichia coli
    • VanBogelen, R. A., Kelley, P. M. & Neidhardt, F. C. (1987). Differential induction of heat shock, SOS, and oxidation stress regulons and accumulation of nucleotides in Escherichia coli. J Bacteriol 169, 26-32.
    • (1987) J. Bacteriol. , vol.169 , pp. 26-32
    • VanBogelen, R.A.1    Kelley, P.M.2    Neidhardt, F.C.3
  • 64
    • 0031665131 scopus 로고    scopus 로고
    • Bacillus subtilis genes for the utilization of sulfur from aliphatic sulfonates
    • van der Ploeg, J. R., Cummings, N. J., Leisinger, T. & Connerton, I. F. (1998). Bacillus subtilis genes for the utilization of sulfur from aliphatic sulfonates. Microbiology 144, 2555-2561.
    • (1998) Microbiology , vol.144 , pp. 2555-2561
    • van der Ploeg, J.R.1    Cummings, N.J.2    Leisinger, T.3    Connerton, I.F.4
  • 65
    • 0024554109 scopus 로고
    • Escherichia coli proteins inducible by oxidative stress mediated by the superoxide radical
    • Walkup, L. K. & Kogoma, T. (1989). Escherichia coli proteins inducible by oxidative stress mediated by the superoxide radical. J Bacteriol 171, 1476-1484.
    • (1989) J. Bacteriol. , vol.171 , pp. 1476-1484
    • Walkup, L.K.1    Kogoma, T.2
  • 66
    • 0032174885 scopus 로고    scopus 로고
    • Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase
    • Zenno, S., Kobori, T., Tanokura, M. & Saigo, K. (1998). Purification and characterization of NfrA1, a Bacillus subtilis nitro/flavin reductase capable of interacting with the bacterial luciferase. Biosci Biotechnol Biochem 62, 1978-1987.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1978-1987
    • Zenno, S.1    Kobori, T.2    Tanokura, M.3    Saigo, K.4
  • 67
    • 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


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