메뉴 건너뛰기




Volumn 397, Issue 5, 2010, Pages 1199-1208

Structural and biochemical bases for the redox sensitivity of mycobacterium tuberculosis RslA

Author keywords

Anti factor; Extracytoplasmic function factor; Redox sensitivity; Zinc binding

Indexed keywords

BACTERIAL PROTEIN; CYSTEINE; DNA POLYMERASE; POLYKETIDE SYNTHASE; PROTEIN RSIA; RNA POLYMERASE; UNCLASSIFIED DRUG; ZINC ION;

EID: 77950517981     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.026     Document Type: Article
Times cited : (42)

References (46)
  • 2
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic function (ECF) sigma factors
    • Helmann J.D. The extracytoplasmic function (ECF) sigma factors. Adv. Microb. Physiol. 2002, 46:47-110.
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 3
    • 34548252292 scopus 로고    scopus 로고
    • A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria
    • Campbell E.A., Greenwell R., Anthony J.R., Wang S., Lim L., Das K., et al. A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria. Mol. Cell 2007, 27:793-805.
    • (2007) Mol. Cell , vol.27 , pp. 793-805
    • Campbell, E.A.1    Greenwell, R.2    Anthony, J.R.3    Wang, S.4    Lim, L.5    Das, K.6
  • 4
    • 0012837562 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA
    • Campbell E.A., Tupy J.L., Gruber T.M., Wang S., Sharp M.M., Gross C.A., Darst S.A. Crystal structure of Escherichia coli sigmaE with the cytoplasmic domain of its anti-sigma RseA. Mol. Cell 2003, 11:1067-1078.
    • (2003) Mol. Cell , vol.11 , pp. 1067-1078
    • Campbell, E.A.1    Tupy, J.L.2    Gruber, T.M.3    Wang, S.4    Sharp, M.M.5    Gross, C.A.6    Darst, S.A.7
  • 5
    • 0036203066 scopus 로고    scopus 로고
    • Structure of the bacterial RNA polymerase promoter specificity sigma subunit
    • Campbell E.A., Muzzin O., Chlenov M., Sun J.L., Olson C.A., Weinman O., et al. Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Mol. Cell 2002, 9:527-539.
    • (2002) Mol. Cell , vol.9 , pp. 527-539
    • Campbell, E.A.1    Muzzin, O.2    Chlenov, M.3    Sun, J.L.4    Olson, C.A.5    Weinman, O.6
  • 6
    • 33947506850 scopus 로고    scopus 로고
    • Structural and biophysical studies on two promoter recognition domains of the extra-cytoplasmic function sigma factor sigma(C) from Mycobacterium tuberculosis
    • Thakur K.G., Joshi A.M., Gopal B. Structural and biophysical studies on two promoter recognition domains of the extra-cytoplasmic function sigma factor sigma(C) from Mycobacterium tuberculosis. J. Biol. Chem. 2007, 282:4711-4718.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4711-4718
    • Thakur, K.G.1    Joshi, A.M.2    Gopal, B.3
  • 8
    • 0038784717 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis pathogenesis and molecular determinants of virulence
    • Smith I. Mycobacterium tuberculosis pathogenesis and molecular determinants of virulence. Clin. Microbiol. Rev. 2003, 16:463-496.
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 463-496
    • Smith, I.1
  • 9
    • 33745865202 scopus 로고    scopus 로고
    • Zinc center as redox switch-new function for an old motif
    • Ilbert M., Graf P.C., Jakob U. Zinc center as redox switch-new function for an old motif. Antioxid. Redox Signal. 2006, 8:835-846.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 835-846
    • Ilbert, M.1    Graf, P.C.2    Jakob, U.3
  • 10
    • 0034623949 scopus 로고    scopus 로고
    • Redox switch of hsp33 has a novel zinc-binding motif
    • Jakob U., Eser M., Bardwell J.C. Redox switch of hsp33 has a novel zinc-binding motif. J. Biol. Chem. 2000, 275:38302-38310.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38302-38310
    • Jakob, U.1    Eser, M.2    Bardwell, J.C.3
  • 12
    • 0346996698 scopus 로고    scopus 로고
    • Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: zinc release and disulfide bond formation
    • Bae J.B., Park J.H., Hahn M.Y., Kim M.S., Roe J.H. Redox-dependent changes in RsrA, an anti-sigma factor in Streptomyces coelicolor: zinc release and disulfide bond formation. J. Mol. Biol. 2004, 335:425-435.
    • (2004) J. Mol. Biol. , vol.335 , pp. 425-435
    • Bae, J.B.1    Park, J.H.2    Hahn, M.Y.3    Kim, M.S.4    Roe, J.H.5
  • 14
    • 0036065206 scopus 로고    scopus 로고
    • Role of the extracytoplasmic-function sigma factor sigma(H) in Mycobacterium tuberculosis global gene expression
    • Manganelli R., Voskuil M.I., Schoolnik G.K., Dubnau E., Gomez M., Smith I. Role of the extracytoplasmic-function sigma factor sigma(H) in Mycobacterium tuberculosis global gene expression. Mol. Microbiol. 2002, 45:365-374.
    • (2002) Mol. Microbiol. , vol.45 , pp. 365-374
    • Manganelli, R.1    Voskuil, M.I.2    Schoolnik, G.K.3    Dubnau, E.4    Gomez, M.5    Smith, I.6
  • 15
    • 0034903883 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global gene expression and survival in macrophages
    • Manganelli R., Voskuil M.I., Schoolnik G.K., Smith I. The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global gene expression and survival in macrophages. Mol. Microbiol. 2001, 41:423-437.
    • (2001) Mol. Microbiol. , vol.41 , pp. 423-437
    • Manganelli, R.1    Voskuil, M.I.2    Schoolnik, G.K.3    Smith, I.4
  • 16
    • 33645532080 scopus 로고    scopus 로고
    • Posttranslational regulation of Mycobacterium tuberculosis extracytoplasmic-function sigma factor sigma L and roles in virulence and in global regulation of gene expression
    • Dainese E., Rodrigue S., Delogu G., Provvedi R., Laflamme L., Brzezinski R., et al. Posttranslational regulation of Mycobacterium tuberculosis extracytoplasmic-function sigma factor sigma L and roles in virulence and in global regulation of gene expression. Infect. Immun. 2006, 74:2457-2461.
    • (2006) Infect. Immun. , vol.74 , pp. 2457-2461
    • Dainese, E.1    Rodrigue, S.2    Delogu, G.3    Provvedi, R.4    Laflamme, L.5    Brzezinski, R.6
  • 17
    • 26444518218 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence
    • Hahn M.Y., Raman S., Anaya M., Husson R.N. The Mycobacterium tuberculosis extracytoplasmic-function sigma factor SigL regulates polyketide synthases and secreted or membrane proteins and is required for virulence. J. Bacteriol. 2005, 187:7062-7071.
    • (2005) J. Bacteriol. , vol.187 , pp. 7062-7071
    • Hahn, M.Y.1    Raman, S.2    Anaya, M.3    Husson, R.N.4
  • 18
    • 4143133402 scopus 로고    scopus 로고
    • T4 AsiA blocks DNA recognition by remodeling sigma70 region 4
    • Lambert L.J., Wei Y., Schirf V., Demeler B., Werner M.H. T4 AsiA blocks DNA recognition by remodeling sigma70 region 4. EMBO J. 2004, 23:2952-2962.
    • (2004) EMBO J. , vol.23 , pp. 2952-2962
    • Lambert, L.J.1    Wei, Y.2    Schirf, V.3    Demeler, B.4    Werner, M.H.5
  • 19
    • 3342950406 scopus 로고    scopus 로고
    • Interactions between the Rhodobacter sphaeroides ECF sigma factor, sigma(E), and its anti-sigma factor, ChrR
    • Anthony J.R., Newman J.D., Donohue T.J. Interactions between the Rhodobacter sphaeroides ECF sigma factor, sigma(E), and its anti-sigma factor, ChrR. J. Mol. Biol. 2004, 341:345-360.
    • (2004) J. Mol. Biol. , vol.341 , pp. 345-360
    • Anthony, J.R.1    Newman, J.D.2    Donohue, T.J.3
  • 20
    • 33748625150 scopus 로고    scopus 로고
    • The structural basis for promoter -35 element recognition by the group IV sigma factors
    • Lane W.J., Darst S.A. The structural basis for promoter -35 element recognition by the group IV sigma factors. PLoS Biol. 2006, 4:e269.
    • (2006) PLoS Biol. , vol.4
    • Lane, W.J.1    Darst, S.A.2
  • 21
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • Murakami K.S., Masuda S., Darst S.A. Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science 2002, 296:1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 23
    • 0141645618 scopus 로고    scopus 로고
    • The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor
    • Li W., Bottrill A.R., Bibb M.J., Buttner M.J., Paget M.S., Kleanthous C. The role of zinc in the disulphide stress-regulated anti-sigma factor RsrA from Streptomyces coelicolor. J. Mol. Biol. 2003, 333:461-472.
    • (2003) J. Mol. Biol. , vol.333 , pp. 461-472
    • Li, W.1    Bottrill, A.R.2    Bibb, M.J.3    Buttner, M.J.4    Paget, M.S.5    Kleanthous, C.6
  • 24
    • 0035798615 scopus 로고    scopus 로고
    • Conserved regions 4.1 and 4.2 of sigma(70) constitute the recognition sites for the anti-sigma factor AsiA, and AsiA is a dimer free in solution
    • Urbauer J.L., Adelman K., Urbauer R.J., Simeonov M.F., Gilmore J.M., Zolkiewski M., Brody E.N. Conserved regions 4.1 and 4.2 of sigma(70) constitute the recognition sites for the anti-sigma factor AsiA, and AsiA is a dimer free in solution. J. Biol. Chem. 2001, 276:41128-41132.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41128-41132
    • Urbauer, J.L.1    Adelman, K.2    Urbauer, R.J.3    Simeonov, M.F.4    Gilmore, J.M.5    Zolkiewski, M.6    Brody, E.N.7
  • 25
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • Gruber T.M., Gross C.A. Multiple sigma subunits and the partitioning of bacterial transcription space. Annu. Rev. Microbiol. 2003, 57:441-466.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 26
    • 0033950956 scopus 로고    scopus 로고
    • Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34
    • Tibazarwa C., Wuertz S., Mergeay M., Wyns L., van Der Lelie D. Regulation of the cnr cobalt and nickel resistance determinant of Ralstonia eutropha (Alcaligenes eutrophus) CH34. J. Bacteriol. 2000, 182:1399-1409.
    • (2000) J. Bacteriol. , vol.182 , pp. 1399-1409
    • Tibazarwa, C.1    Wuertz, S.2    Mergeay, M.3    Wyns, L.4    van Der Lelie, D.5
  • 27
    • 0038354921 scopus 로고    scopus 로고
    • Region 4 of sigma as a target for transcription regulation
    • Dove S.L., Darst S.A., Hochschild A. Region 4 of sigma as a target for transcription regulation. Mol. Microbiol. 2003, 48:863-874.
    • (2003) Mol. Microbiol. , vol.48 , pp. 863-874
    • Dove, S.L.1    Darst, S.A.2    Hochschild, A.3
  • 28
    • 42049122814 scopus 로고    scopus 로고
    • Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective
    • Campbell E.A., Westblade L.F., Darst S.A. Regulation of bacterial RNA polymerase sigma factor activity: a structural perspective. Curr. Opin. Microbiol. 2008, 11:121-127.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 121-127
    • Campbell, E.A.1    Westblade, L.F.2    Darst, S.A.3
  • 29
    • 34548153206 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4
    • Patikoglou G.A., Westblade L.F., Campbell E.A., Lamour V., Lane W.J., Darst S.A. Crystal structure of the Escherichia coli regulator of sigma70, Rsd, in complex with sigma70 domain 4. J. Mol. Biol. 2007, 372:649-659.
    • (2007) J. Mol. Biol. , vol.372 , pp. 649-659
    • Patikoglou, G.A.1    Westblade, L.F.2    Campbell, E.A.3    Lamour, V.4    Lane, W.J.5    Darst, S.A.6
  • 30
    • 1842766125 scopus 로고    scopus 로고
    • Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    • Sorenson M.K., Ray S.S., Darst S.A. Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation. Mol. Cell 2004, 14:127-138.
    • (2004) Mol. Cell , vol.14 , pp. 127-138
    • Sorenson, M.K.1    Ray, S.S.2    Darst, S.A.3
  • 31
    • 0036280086 scopus 로고    scopus 로고
    • Functional interaction of region 4 of the extracytoplasmic function sigma factor FecI with the cytoplasmic portion of the FecR transmembrane protein of the Escherichia coli ferric citrate transport system
    • Mahren S., Enz S., Braun V. Functional interaction of region 4 of the extracytoplasmic function sigma factor FecI with the cytoplasmic portion of the FecR transmembrane protein of the Escherichia coli ferric citrate transport system. J. Bacteriol. 2002, 184:3704-3711.
    • (2002) J. Bacteriol. , vol.184 , pp. 3704-3711
    • Mahren, S.1    Enz, S.2    Braun, V.3
  • 32
    • 47049102125 scopus 로고    scopus 로고
    • Differential mechanisms of binding of anti-sigma factors Escherichia coli Rsd and bacteriophage T4 AsiA to E. coli RNA polymerase lead to diverse physiological consequences
    • Sharma U.K., Chatterji D. Differential mechanisms of binding of anti-sigma factors Escherichia coli Rsd and bacteriophage T4 AsiA to E. coli RNA polymerase lead to diverse physiological consequences. J. Bacteriol. 2008, 190:3434-3443.
    • (2008) J. Bacteriol. , vol.190 , pp. 3434-3443
    • Sharma, U.K.1    Chatterji, D.2
  • 33
    • 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. 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. 2002, 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
  • 34
    • 0242521392 scopus 로고    scopus 로고
    • RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH
    • Song T., Dove S.L., Lee K.H., Husson R.N. RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH. Mol. Microbiol. 2003, 50:949-959.
    • (2003) Mol. Microbiol. , vol.50 , pp. 949-959
    • Song, T.1    Dove, S.L.2    Lee, K.H.3    Husson, R.N.4
  • 36
    • 49649088871 scopus 로고    scopus 로고
    • Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA
    • Lewin A., Crow A., Hodson C.T., Hederstedt L., Le Brun N.E. Effects of substitutions in the CXXC active-site motif of the extracytoplasmic thioredoxin ResA. Biochem. J. 2008, 414:81-91.
    • (2008) Biochem. J. , vol.414 , pp. 81-91
    • Lewin, A.1    Crow, A.2    Hodson, C.T.3    Hederstedt, L.4    Le Brun, N.E.5
  • 37
    • 13144257719 scopus 로고    scopus 로고
    • Redox-sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx
    • Nakano S., Erwin K.N., Ralle M., Zuber P. Redox-sensitive transcriptional control by a thiol/disulphide switch in the global regulator, Spx. Mol. Microbiol. 2005, 55:498-510.
    • (2005) Mol. Microbiol. , vol.55 , pp. 498-510
    • Nakano, S.1    Erwin, K.N.2    Ralle, M.3    Zuber, P.4
  • 38
    • 0029934516 scopus 로고    scopus 로고
    • The CXXC motif: imperatives for the formation of native disulfide bonds in the cell
    • Chivers P.T., Laboissiere M.C., Raines R.T. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 1996, 15:2659-2667.
    • (1996) EMBO J. , vol.15 , pp. 2659-2667
    • Chivers, P.T.1    Laboissiere, M.C.2    Raines, R.T.3
  • 40
    • 0038167027 scopus 로고    scopus 로고
    • Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA
    • Shenoy A.R., Visweswariah S.S. Site-directed mutagenesis using a single mutagenic oligonucleotide and DpnI digestion of template DNA. Anal. Biochem. 2003, 319:335-336.
    • (2003) Anal. Biochem. , vol.319 , pp. 335-336
    • Shenoy, A.R.1    Visweswariah, S.S.2
  • 41
    • 0003076963 scopus 로고
    • Recent changes to the mosflm package for processing film and image plate data
    • Leslie A.G.W. Recent changes to the mosflm package for processing film and image plate data. Jt. CCP4+ ESF-EAMCB Newsl. Protein Crystallogr. 1992, 26.
    • (1992) Jt. CCP4+ ESF-EAMCB Newsl. Protein Crystallogr. , vol.26
    • Leslie, A.G.W.1
  • 42
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 1994, 50:760-763. CCP4.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 44
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 1997, 53:240-255.
    • (1997) Acta Crystallogr. Sect. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 45
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 2004, 60:2126-2132.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.