메뉴 건너뛰기




Volumn 55, Issue 2, 2005, Pages 498-510

Redox-sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; CYSTEINE; DISULFIDE; PROTEIN SPX; REGULATOR PROTEIN; RNA POLYMERASE; THIOL; THIOREDOXIN; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 13144257719     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04395.x     Document Type: Article
Times cited : (122)

References (41)
  • 1
    • 0033582933 scopus 로고    scopus 로고
    • Bridge over troubled waters: Sensing stress by disulfide bond formation
    • Åslund, F., and Beckwith, J. (1999) Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96: 751-753.
    • (1999) Cell , vol.96 , pp. 751-753
    • Åslund, F.1    Beckwith, J.2
  • 2
    • 1842506160 scopus 로고    scopus 로고
    • Regulation at complex bacterial promoters: How bacteria use different promoter organizations to produce different regulatory outcomes
    • Barnard, A., Wolfe, A., and Busby, S. (2004) Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes. Curr Opin Microbiol 7: 102-108.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 102-108
    • Barnard, A.1    Wolfe, A.2    Busby, S.3
  • 4
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby, S., and Ebright, R.H. (1999) Transcription activation by catabolite activator protein (CAP). J Mol Biol 293: 199-213.
    • (1999) J Mol Biol , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 5
    • 0037756788 scopus 로고    scopus 로고
    • Functional interaction between RNA polymerase alpha subunit C-terminal domain and sigma70 in UP-element- and activator-dependent transcription
    • Chen, H., Tang, H., and Ebright, R.H. (2003) Functional interaction between RNA polymerase alpha subunit C-terminal domain and sigma70 in UP-element- and activator-dependent transcription. Mol Cell 11: 1621-1633.
    • (2003) Mol Cell , vol.11 , pp. 1621-1633
    • Chen, H.1    Tang, H.2    Ebright, R.H.3
  • 6
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi, H., Kim, S., Mukhopadhyay, P., Cho, S., Woo, J., Storz, G., and Ryu, S. (2001) Structural basis of the redox switch in the OxyR transcription factor. Cell 105: 103-113.
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.7
  • 7
    • 0030448704 scopus 로고    scopus 로고
    • The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor
    • Ding, H., Hidalgo, E., and Demple, B. (1996) The redox state of the [2Fe-2S] clusters in SoxR protein regulates its activity as a transcription factor. J Biol Chem 271: 33173-33175.
    • (1996) J Biol Chem , vol.271 , pp. 33173-33175
    • Ding, H.1    Hidalgo, E.2    Demple, B.3
  • 8
    • 0033567215 scopus 로고    scopus 로고
    • Bacterial promoter architecture: Subsite structure of UP elements and interactions with the carboxy-terminal domain of the RNA polymerase alpha subunit
    • Estrem, S.T., Ross, W., Gaal, T., Chen, Z.W., Niu, W., Ebright, R.H., and Course, R.L. (1999) Bacterial promoter architecture: subsite structure of UP elements and interactions with the carboxy-terminal domain of the RNA polymerase alpha subunit. Genes Dev 13: 2134-2147.
    • (1999) Genes Dev , vol.13 , pp. 2134-2147
    • Estrem, S.T.1    Ross, W.2    Gaal, T.3    Chen, Z.W.4    Niu, W.5    Ebright, R.H.6    Course, R.L.7
  • 9
    • 0025014845 scopus 로고
    • A target for carbon source-dependent negative regulation of the citB promoter of Bacillus subtilis
    • Fouet, A., and Sonenshein, A.L. (1990) A target for carbon source-dependent negative regulation of the citB promoter of Bacillus subtilis. J Bacteriol 172: 835-844.
    • (1990) J Bacteriol , vol.172 , pp. 835-844
    • Fouet, A.1    Sonenshein, A.L.2
  • 10
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M., and Helmann, J.D. (2002) The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc Natl Acad Sci USA 99: 6690-6695.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 11
    • 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., and 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
  • 12
    • 0029790760 scopus 로고    scopus 로고
    • SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form
    • Gaudu, P., and Weiss, B. (1996) SoxR, a [2Fe-2S] transcription factor, is active only in its oxidized form. Proc Natl Acad Sci USA 93: 10094-10098.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 10094-10098
    • Gaudu, P.1    Weiss, B.2
  • 16
    • 0025089521 scopus 로고
    • Cloning and analysis of the Bacillus subtilis rpsD gene, encoding ribosomal protein S4
    • Grundy, F.J., and Henkin, T.M. (1990) Cloning and analysis of the Bacillus subtilis rpsD gene, encoding ribosomal protein S4. J Bacteriol 172: 6372-6379.
    • (1990) J Bacteriol , vol.172 , pp. 6372-6379
    • Grundy, F.J.1    Henkin, T.M.2
  • 17
    • 0030597337 scopus 로고    scopus 로고
    • Plasmids for ectopic integration in Bacillus subtilis
    • Guerout-Fleury, A.M., Frandsen, N., and Stragier, P. (1996) Plasmids for ectopic integration in Bacillus subtilis. Gene 180: 57-61.
    • (1996) Gene , vol.180 , pp. 57-61
    • Guerout-Fleury, A.M.1    Frandsen, N.2    Stragier, P.3
  • 18
    • 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., and 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
  • 19
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob, U., Muse, W., Eser, M., and Bardwell, J.C. (1999) Chaperone activity with a redox switch. Cell 96: 341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 20
  • 22
    • 0037334843 scopus 로고    scopus 로고
    • Global characterization of disulfide stress in Bacillus subtilis
    • Leichert, L.I., Scharf, C., and 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
  • 23
    • 0036407638 scopus 로고    scopus 로고
    • Identification and structure of the anti-sigma factor-binding domain of the disulphide-stress regulated sigma factor sigma(R) from Streptomyces coelicolor
    • Li, W., Stevenson, C.E., Burton, N., Jakimowicz, P., Paget, M.S., Buttner, M.J., et al. (2002) Identification and structure of the anti-sigma factor-binding domain of the disulphide-stress regulated sigma factor sigma(R) from Streptomyces coelicolor. J Mol Biol 323: 225-236.
    • (2002) J Mol Biol , vol.323 , pp. 225-236
    • Li, W.1    Stevenson, C.E.2    Burton, N.3    Jakimowicz, P.4    Paget, M.S.5    Buttner, M.J.6
  • 24
    • 0033866677 scopus 로고    scopus 로고
    • The ClpX protein of Bacillus subtilis indirectly influences RNA polymerase holoenzyme composition and directly stimulates sigma-dependent transcription
    • Liu, J., and Zuber, P. (2000) The ClpX protein of Bacillus subtilis indirectly influences RNA polymerase holoenzyme composition and directly stimulates sigma-dependent transcription. Mol Microbiol 37: 885-897.
    • (2000) Mol Microbiol , vol.37 , pp. 885-897
    • Liu, J.1    Zuber, P.2
  • 25
    • 0035190119 scopus 로고    scopus 로고
    • Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme
    • Martin, P., DeMel, S., Shi, J., Gladysheva, T., Gatti, D.L., Rosen, B.P., and Edwards, B.F. (2001) Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure (Camb) 9: 1071-1081.
    • (2001) Structure (Camb) , vol.9 , pp. 1071-1081
    • Martin, P.1    DeMel, S.2    Shi, J.3    Gladysheva, T.4    Gatti, D.L.5    Rosen, B.P.6    Edwards, B.F.7
  • 26
    • 0033865389 scopus 로고    scopus 로고
    • Mutations conferring amino acid residue substitutions in the carboxy-terminal domain of RNA polymerase alpha can suppress clpX and clpP with respect to developmentally regulated transcription in Bacillus subtilis
    • Nakano, M.M., Zhu, Y., Liu, J., Reyes, D.Y., Yoshikawa, H., and Zuber, P. (2000) Mutations conferring amino acid residue substitutions in the carboxy-terminal domain of RNA polymerase alpha can suppress clpX and clpP with respect to developmentally regulated transcription in Bacillus subtilis. Mol Microbiol 37: 869-884.
    • (2000) Mol Microbiol , vol.37 , pp. 869-884
    • Nakano, M.M.1    Zhu, Y.2    Liu, J.3    Reyes, D.Y.4    Yoshikawa, H.5    Zuber, P.6
  • 27
    • 0034757626 scopus 로고    scopus 로고
    • Loss-of-function mutations in yjbD result in ClpX- and ClpP-independent competence development of Bacillus subtilis
    • Nakano, M.M., Hajarizadeh, F., Zhu, Y., and Zuber, P. (2001) Loss-of-function mutations in yjbD result in ClpX- and ClpP-independent competence development of Bacillus subtilis. Mol Microbiol 42: 383-394.
    • (2001) Mol Microbiol , vol.42 , pp. 383-394
    • Nakano, M.M.1    Hajarizadeh, F.2    Zhu, Y.3    Zuber, P.4
  • 28
    • 0036015647 scopus 로고    scopus 로고
    • Spx (YjbD), a negative effector of competence in Bacillus subtilis, enhances ClpC-MecA-ComK interaction
    • Nakano, M.M., Nakano, S., and Zuber, P. (2002) Spx (YjbD), a negative effector of competence in Bacillus subtilis, enhances ClpC-MecA-ComK interaction. Mol Microbiol 44: 1341-1349.
    • (2002) Mol Microbiol , vol.44 , pp. 1341-1349
    • Nakano, M.M.1    Nakano, S.2    Zuber, P.3
  • 29
    • 0036283489 scopus 로고    scopus 로고
    • Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis
    • Nakano, S., Zheng, G., Nakano, M.M., and Zuber, P. (2002) Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis. J Bacteriol 184: 3664-3670.
    • (2002) J Bacteriol , vol.184 , pp. 3664-3670
    • Nakano, S.1    Zheng, G.2    Nakano, M.M.3    Zuber, P.4
  • 30
    • 0344392193 scopus 로고    scopus 로고
    • Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis
    • Nakano, S., Kuster-Schock, E., Grossman, A.D., and Zuber, P. (2003a) Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis. Proc Natl Acad Sci USA 100: 13603-13608.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 13603-13608
    • Nakano, S.1    Kuster-Schock, E.2    Grossman, A.D.3    Zuber, P.4
  • 31
    • 0037386620 scopus 로고    scopus 로고
    • A regulatory protein that interferes with activator-stimulated transcription in bacteria
    • Nakano, S., Nakano, M.M., Zhang, Y., Leelakriangsak, M., and Zuber, P. (2003b) A regulatory protein that interferes with activator-stimulated transcription in bacteria. Proc Natl Acad Sci USA 100: 4233-4238.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4233-4238
    • Nakano, S.1    Nakano, M.M.2    Zhang, Y.3    Leelakriangsak, M.4    Zuber, P.5
  • 32
    • 0141492988 scopus 로고    scopus 로고
    • Thiol-based regulatory switches
    • Paget, M.S., and Buttner, M.J. (2003) Thiol-based regulatory switches. Annu Rev Genet 37: 91-121.
    • (2003) Annu Rev Genet , vol.37 , pp. 91-121
    • Paget, M.S.1    Buttner, M.J.2
  • 33
    • 0031746383 scopus 로고    scopus 로고
    • PhoP-P and RNA polymerase sigmaA holoenzyme are sufficient for transcription of Pho regulon promoters in Bacillus subtilis: PhoP-P activator sites within the coding region stimulate transcription in vitro
    • Qi, Y., and Hulett, F.M. (1998) PhoP-P and RNA polymerase sigmaA holoenzyme are sufficient for transcription of Pho regulon promoters in Bacillus subtilis: PhoP-P activator sites within the coding region stimulate transcription in vitro. Mol Microbiol 28: 1187-1197.
    • (1998) Mol Microbiol , vol.28 , pp. 1187-1197
    • Qi, Y.1    Hulett, F.M.2
  • 34
    • 0027761839 scopus 로고
    • A third recognition element in bacterial promoters: DNA binding by the alpha subunit of RNA polymerase
    • Ross, W., Gosink, K.K., Salomon, J., Igarashi, K., Zou, C., Ishihama, A., et al. (1993) A third recognition element in bacterial promoters: DNA binding by the alpha subunit of RNA polymerase. Science 262: 1407-1413.
    • (1993) Science , vol.262 , pp. 1407-1413
    • Ross, W.1    Gosink, K.K.2    Salomon, J.3    Igarashi, K.4    Zou, C.5    Ishihama, A.6
  • 35
    • 0038522852 scopus 로고    scopus 로고
    • An intersubunit contact stimulating transcription initiation by E. coli RNA polymerase: Interaction of the alpha C-terminal domain and sigma region 4
    • Ross, W., Schneider, D.A., Paul, B.J., Mertens, A., and Course, R.L. (2003) An intersubunit contact stimulating transcription initiation by E. coli RNA polymerase: interaction of the alpha C-terminal domain and sigma region 4. Genes Dev 17: 1293-1307.
    • (2003) Genes Dev , vol.17 , pp. 1293-1307
    • Ross, W.1    Schneider, D.A.2    Paul, B.J.3    Mertens, A.4    Course, R.L.5
  • 36
    • 0033520115 scopus 로고    scopus 로고
    • Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773
    • Stevens, S.Y., Hu, W., Gladysheva, T., Rosen, B.P., Zuiderweg, E.R., and Lee, L. (1999) Secondary structure and fold homology of the ArsC protein from the Escherichia coli arsenic resistance plasmid R773. Biochemistry 38: 10178-10186.
    • (1999) Biochemistry , vol.38 , pp. 10178-10186
    • Stevens, S.Y.1    Hu, W.2    Gladysheva, T.3    Rosen, B.P.4    Zuiderweg, E.R.5    Lee, L.6
  • 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
    • 0034990115 scopus 로고    scopus 로고
    • The 2.2 A crystal structure of Hsp33: A heat shock protein with redox-regulated chaperone activity
    • Vijayalakshmi, J., Mukhergee, M.K., Graumann, J., Jakob, U., and Saper, M.A. (2001) The 2.2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity. Structure (Camb) 9: 367-375.
    • (2001) Structure (Camb) , vol.9 , pp. 367-375
    • Vijayalakshmi, J.1    Mukhergee, M.K.2    Graumann, J.3    Jakob, U.4    Saper, M.A.5
  • 39
    • 0033991496 scopus 로고    scopus 로고
    • Redox sensing by prokaryotic transcription factors
    • Zheng, M., and Storz, G. (2000) Redox sensing by prokaryotic transcription factors. Biochem Pharmacol 59: 1-6.
    • (2000) Biochem Pharmacol , vol.59 , pp. 1-6
    • Zheng, M.1    Storz, G.2
  • 40
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Åslund, 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    Åslund, F.2    Storz, G.3
  • 41
    • 1642352469 scopus 로고    scopus 로고
    • Spx-RNA polymerase interaction and global transcriptional control during oxidative stress
    • Zuber, P. (2004) Spx-RNA polymerase interaction and global transcriptional control during oxidative stress. J Bacteriol 186: 1911-1918.
    • (2004) J Bacteriol , vol.186 , pp. 1911-1918
    • Zuber, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.