메뉴 건너뛰기




Volumn 11, Issue 12, 2004, Pages 1179-1185

Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; OXIDIZING AGENT; OXYR PROTEIN, E COLI; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRYPTOPHAN; UREA;

EID: 16544369973     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb856     Document Type: Article
Times cited : (218)

References (25)
  • 2
    • 0031036917 scopus 로고    scopus 로고
    • An essential role for free radicals and derived species in signal transduction
    • Lander, H.M. An essential role for free radicals and derived species in signal transduction. FASEB J. 11, 118-124 (1997).
    • (1997) FASEB J , vol.11 , pp. 118-124
    • Lander, H.M.1
  • 3
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress- inducible genes: Direct activation by oxidation
    • Storz, G., Tartaglia, L.A. & Ames, B.N. Transcriptional regulator of oxidative stress- inducible genes: direct activation by oxidation. Science 248, 189-194 (1990).
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 4
    • 0032513362 scopus 로고    scopus 로고
    • Activation of the OxyR transcription factor by reversible disulfide bond formation
    • Zheng, M., Aslund, F. & Storz, G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279, 1718-1721 (1998).
    • (1998) Science , vol.279 , pp. 1718-1721
    • Zheng, M.1    Aslund, F.2    Storz, G.3
  • 5
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • Hausladen, A. et al. Nitrosative stress: activation of the transcription factor OxyR. Cell 86, 719-729 (1996).
    • (1996) Cell , vol.86 , pp. 719-729
    • Hausladen, A.1
  • 6
    • 0028965108 scopus 로고
    • Mutational analysis of the redox- sensitive transcriptional regulator OxyR: Regions important for oxidation and transcrip- tional activation
    • Kullik, I., Toledano, M.B., Tartaglia, L.A. & Storz, G. Mutational analysis of the redox- sensitive transcriptional regulator OxyR: regions important for oxidation and transcrip- tional activation. J. Bacteriol. 177, 1275-1284 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 1275-1284
    • Kullik, I.1    Toledano, M.B.2    Tartaglia, L.A.3    Storz, G.4
  • 7
    • 0027416847 scopus 로고
    • Involvement of the RNA polymerase alpha subunit C-terminal region in co-operative interaction and transcriptional activation with OxyR protein
    • Tao, K., Fujita, N. & Ishihama, A. Involvement of the RNA polymerase alpha subunit C-terminal region in co-operative interaction and transcriptional activation with OxyR protein. Mol. Microbiol. 7, 859-864 (1993).
    • (1993) Mol. Microbiol. , vol.7 , pp. 859-864
    • Tao, K.1    Fujita, N.2    Ishihama, A.3
  • 8
    • 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. et al. Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 78, 897-909 (1994).
    • (1994) Cell , vol.78 , pp. 897-909
    • Toledano, M.B.1
  • 9
    • 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. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc. Natl. Acad. Sci. USA 96, 6161-6165 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6161-6165
    • Aslund, F.1    Zheng, M.2    Beckwith, J.3    Storz, G.4
  • 10
    • 0032792514 scopus 로고    scopus 로고
    • In vivo oxidation-reduction kinetics of OxyR, the transcriptional activator for an oxidative stress-inducible regulon in Escherichia coli
    • Tao, K. In vivo oxidation-reduction kinetics of OxyR, the transcriptional activator for an oxidative stress-inducible regulon in Escherichia coli. FEBS Lett. 457, 90-92 (1999).
    • (1999) FEBS Lett , vol.457 , pp. 90-92
    • Tao, K.1
  • 11
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi, H. et al. Structural basis of the redox switch in the OxyR transcription factor. Cell 105, 103-113 (2001).
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1
  • 12
    • 0037013155 scopus 로고    scopus 로고
    • OxyR: A molecular code for redox-related signaling
    • Kim, S.O. et al. OxyR: a molecular code for redox-related signaling. Cell 109, 383-396 (2002).
    • (2002) Cell , vol.109 , pp. 383-396
    • Kim, S.O.1
  • 13
    • 0037336620 scopus 로고    scopus 로고
    • The structure of full-length LysR-type transcriptional regulators. Modeling of the full-length OxyR transcription factor dimer
    • Zaim, J. & Kierzek, A.M. The structure of full-length LysR-type transcriptional regulators. Modeling of the full-length OxyR transcription factor dimer. Nucleic Acids Res. 31, 1444-1454 (2003).
    • (2003) Nucleic Acids Res , vol.31 , pp. 1444-1454
    • Zaim, J.1    Kierzek, A.M.2
  • 14
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reduc- tase
    • Ellis, H.R. & Poole, L.B. Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reduc- tase. Biochemistry 36, 15013-15018 (1997).
    • (1997) Biochemistry , vol.36 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 15
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne, A. et al. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38, 15407-15416 (1999).
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1
  • 16
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y., & Barkley, M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry 37, 9976-9982 (1998).
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 17
    • 0037135590 scopus 로고    scopus 로고
    • Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator
    • Li, S., Rosen, B.P., Borges-Walmsley, M.I., & Walmsley, A.R. Evidence for cooperativity between the four binding sites of dimeric ArsD, an As(III)-responsive transcriptional regulator. J. Biol. Chem. 277, 25992-26002 (2003).
    • (2003) J. Biol. Chem. , vol.277 , pp. 25992-26002
    • Li, S.1    Rosen, B.P.2    Borges-Walmsley, M.I.3    Walmsley, A.R.4
  • 18
    • 0037470555 scopus 로고    scopus 로고
    • Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1
    • Kafri, G. & Horovitz, A. Transient kinetic analysis of ATP-induced allosteric transitions in the eukaryotic chaperonin containing TCP-1. J. Mol. Biol. 326, 981-987 (2003).
    • (2003) J. Mol. Biol. , vol.326 , pp. 981-987
    • Kafri, G.1    Horovitz, A.2
  • 20
    • 0037184525 scopus 로고    scopus 로고
    • How to flip the (Redox) switch
    • Georgiou, G. How to flip the (redox) switch. Cell 111, 607-610 (2002).
    • (2002) Cell , vol.111 , pp. 607-610
    • Georgiou, G.1
  • 21
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O.B. Molten globule and protein folding. Adv. Protein Chem. 47, 83-229 (1995).
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 22
    • 0038691618 scopus 로고    scopus 로고
    • Detection of an intermediate during unfolding of bacterial cell division protein FtsZ
    • Santra, M.K. and Panda, D. Detection of an intermediate during unfolding of bacterial cell division protein FtsZ. J. Biol. Chem. 278, 21336-21343 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 21336-21343
    • Santra, M.K.1    Panda, D.2
  • 23
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C.M. & Kim, P.S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832 (1993).
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 24
    • 0034608856 scopus 로고    scopus 로고
    • Regulation of protein function by native metastability
    • Lee, C., Park, S.H., Lee, M.Y. & Yu, M.H. Regulation of protein function by native metastability. Proc. Natl. Acad. Sci. USA 97, 7727-7731 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7727-7731
    • Lee, C.1    Park, S.H.2    Lee, M.Y.3    Yu, M.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.