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Volumn 11, Issue 4, 2003, Pages 1067-1078

Crystal structure of Escherichia coli σE with the cytoplasmic domain of its anti-σ RseA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HOLOENZYME; PROTEIN RSEA; RNA POLYMERASE; SIGMA FACTOR; UNCLASSIFIED DRUG;

EID: 0012837562     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(03)00148-5     Document Type: Article
Times cited : (207)

References (70)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement
    • Adams P.D., Pannu N.S., Read R.J., Brunger A.T. Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA. 94:1997;5018-5023.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 2
    • 0033568606 scopus 로고    scopus 로고
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor
    • E-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Genes Dev. 13:1999;2449-2461.
    • (1999) Genes Dev. , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 5
    • 0029070395 scopus 로고
    • The role of anti-sigma factors in gene regulation
    • Brown K.L., Hughes K.T. The role of anti-sigma factors in gene regulation. Mol. Microbiol. 16:1995;397-404.
    • (1995) Mol. Microbiol. , vol.16 , pp. 397-404
    • Brown, K.L.1    Hughes, K.T.2
  • 6
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • Brown M.S., Ye J., Rawson R.B., Goldstein J.L. Regulated intramembrane proteolysis. a control mechanism conserved from bacteria to humans Cell. 100:2000;391-398.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 7
  • 8
    • 0034733377 scopus 로고    scopus 로고
    • F, contacting multiple conserved cegions of the σ factor
    • F, contacting multiple conserved cegions of the σ factor. J. Mol. Biol. 300:2000;17-28.
    • (2000) J. Mol. Biol. , vol.300 , pp. 17-28
    • Campbell, E.A.1    Darst, S.A.2
  • 12
    • 0031893965 scopus 로고    scopus 로고
    • The bacteriophage T4 AsiA protein: A molecular switch for sigma 70-dependent promoters
    • Coland F., Orsini G., Brody E., Buc H., Kolb A. The bacteriophage T4 AsiA protein. a molecular switch for sigma 70-dependent promoters Mol. Microbiol. 27:1998;819-829.
    • (1998) Mol. Microbiol. , vol.27 , pp. 819-829
    • Coland, F.1    Orsini, G.2    Brody, E.3    Buc, H.4    Kolb, A.5
  • 14
    • 0030763077 scopus 로고    scopus 로고
    • The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways
    • Connolly L., De Las Penas A., Alba B.M., Gross C.A. The response to extracytoplasmic stress in Escherichia coli is controlled by partially overlapping pathways. Genes Dev. 11:1997;2012-2021.
    • (1997) Genes Dev. , vol.11 , pp. 2012-2021
    • Connolly, L.1    De Las Penas, A.2    Alba, B.M.3    Gross, C.A.4
  • 15
    • 0002583957 scopus 로고
    • Dm-density modification package
    • Cowtan, K. (1994). Dm-density modification package, ESF/CCP4 Newsletter 31, 34-38.
    • (1994) ESF/CCP4 Newsletter , vol.31 , pp. 34-38
    • Cowtan, K.1
  • 16
    • 0030998321 scopus 로고    scopus 로고
    • The sigma (E) and the Cpx signal transductin systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli
    • Danese P.N., Silhavy T.J. The sigma (E) and the Cpx signal transductin systems control the synthesis of periplasmic protein-folding enzymes in Escherichia coli. Genes Dev. 11:1997;1183-1193.
    • (1997) Genes Dev. , vol.11 , pp. 1183-1193
    • Danese, P.N.1    Silhavy, T.J.2
  • 18
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28
    • Daughdrill G.W., Chadsey M.S., Karlinsey J.E., Hughes K.T., Dahlquist F.W. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28. Nat. Struct. Biol. 4:1997;285-291.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 21
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276:1997;523-530.
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 23
    • 0033985080 scopus 로고    scopus 로고
    • GHKL, an emergent ATPase/kinase superfamily
    • Dutta R., Inouye M. GHKL, an emergent ATPase/kinase superfamily. Trends Biochem. Sci. 25:2000;24-28.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 24-28
    • Dutta, R.1    Inouye, M.2
  • 24
    • 0024727149 scopus 로고
    • E subunit of Escherichia coli RNA polymerase: A second alternate s factor involved in high-temperature gene expression
    • E subunit of Escherichia coli RNA polymerase. a second alternate s factor involved in high-temperature gene expression Genes Dev. 3:1989;1462-1471.
    • (1989) Genes Dev. , vol.3 , pp. 1462-1471
    • Erickson, J.W.1    Gross, C.A.2
  • 25
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn J.M., Kim Y.-I., Sauer R.T., Baker T.A. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol Cell. 11:2003;671-678.
    • (2003) Mol Cell , vol.11 , pp. 671-678
    • Flynn, J.M.1    Kim, Y.-I.2    Sauer, R.T.3    Baker, T.A.4
  • 26
    • 0023057529 scopus 로고
    • Sigma factors from E. coli, B. subtilis, phase SPO1, and phage T4 are homologous proteins
    • Gribskov M., Burgess R.R. Sigma factors from E. coli, B. subtilis, phase SPO1, and phage T4 are homologous proteins. Nucleic Acids Res. 14:1986;6745-6763.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 6745-6763
    • Gribskov, M.1    Burgess, R.R.2
  • 27
    • 0000776061 scopus 로고
    • Bacterial sigma factors
    • K. Yamamoto, & S. McKnight. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Gross C.A., Lonetto M., Losick R. Bacterial sigma factors. Yamamoto K., McKnight S. Transcriptional Regulation. 1992;129-176 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1992) Transcriptional Regulation , pp. 129-176
    • Gross, C.A.1    Lonetto, M.2    Losick, R.3
  • 30
    • 0031050795 scopus 로고    scopus 로고
    • Molecular systematic studies of eubacteria, using sigma70-type sigma factors of group 1 and group 2
    • Gruber T.M., Bryant D.A. Molecular systematic studies of eubacteria, using sigma70-type sigma factors of group 1 and group 2. J. Bacteriol. 179:1997;1734-1747.
    • (1997) J. Bacteriol. , vol.179 , pp. 1734-1747
    • Gruber, T.M.1    Bryant, D.A.2
  • 31
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic funciton (ECF) sigma factors
    • Helmann J.D. The extracytoplasmic funciton (ECF) sigma factors. Adv. Microb. Physiol. 46:2002;47-110.
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 32
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • Helmann J.D., Chamberlin M.J. Structure and function of bacterial sigma factors. Annu. Rev. Biochem. 57:1988;839-872.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 839-872
    • Helmann, J.D.1    Chamberlin, M.J.2
  • 33
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synchrotron radiation
    • Hendrickson W.A. Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science. 254:1991;51-58.
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 34
    • 0029785147 scopus 로고    scopus 로고
    • Mapping the protein universe
    • Holm L., Sander C. Mapping the protein universe. Science. 273:1996;595-602.
    • (1996) Science , vol.273 , pp. 595-602
    • Holm, L.1    Sander, C.2
  • 36
    • 84889120137 scopus 로고
    • Imrpoved methods for building protein models in electron denstiy maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S., Kjeldgaard M. Imrpoved methods for building protein models in electron denstiy maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 41
    • 0026612797 scopus 로고
    • 70 family: Sequence conservation and evolutionary relationships
    • 70 family. sequence conservation and evolutionary relationships J. Bacteriol. 174:1992;3843-3849.
    • (1992) J. Bacteriol. , vol.174 , pp. 3843-3849
    • Lonetto, M.1    Gribskov, M.2    Gross, C.A.3
  • 42
    • 0028018104 scopus 로고
    • Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase σ factors involved in the regulation of extracytoplasmic functions
    • Lonetto M.A., Brown K.L., Rudd K.E., Buttner M.J. Analysis of the Streptomyces coelicolor sigE gene reveals the existence of a subfamily of eubacterial RNA polymerase σ factors involved in the regulation of extracytoplasmic functions. Proc. Natl. Acad. Sci. USA. 91:1994;7573-7577.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7573-7577
    • Lonetto, M.A.1    Brown, K.L.2    Rudd, K.E.3    Buttner, M.J.4
  • 43
    • 0030271890 scopus 로고    scopus 로고
    • 70 subunit fragment from Escherichia coli RNA polymerase
    • 70 subunit fragment from Escherichia coli RNA polymerase. Cell. 87:1996;127-136.
    • (1996) Cell , vol.87 , pp. 127-136
    • Malhotra, A.1    Severinova, E.2    Darst, S.A.3
  • 44
    • 0027328345 scopus 로고
    • ΣF, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-Σ factor that is also a protein kinase
    • Min K.T., Hilditch C.M., Diederich B., Errington J., Yudkin M.D. ΣF, the first compartment-specific transcription factor of B. subtilis, is regulated by an anti-Σ factor that is also a protein kinase. Cell. 74:1993;735-742.
    • (1993) Cell , vol.74 , pp. 735-742
    • Min, K.T.1    Hilditch, C.M.2    Diederich, B.3    Errington, J.4    Yudkin, M.D.5
  • 45
    • 0031745718 scopus 로고    scopus 로고
    • The extracytoplasmic function sigma factors: Role and regulation
    • Missiakas, D., and Raina, S. (1998). The extracytoplasmic function sigma factors: role and regulation, Mol. Microbiol. 28.
    • (1998) Mol. Microbiol. , vol.28
    • Missiakas, D.1    Raina, S.2
  • 46
    • 0030907038 scopus 로고    scopus 로고
    • Modulation of the Escherichia coli sE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins
    • Missiakas D., Mayer M.P., Lemaire M., Georgopoulos C., Raina S. Modulation of the Escherichia coli sE (RpoE) heat-shock transcription-factor activity by the RseA, RseB and RseC proteins. Mol. Microbiol. 24:1997;355-371.
    • (1997) Mol. Microbiol. , vol.24 , pp. 355-371
    • Missiakas, D.1    Mayer, M.P.2    Lemaire, M.3    Georgopoulos, C.4    Raina, S.5
  • 47
    • 0037937689 scopus 로고    scopus 로고
    • Insights into transcription initiation from structural studies of bacterial RNA polymerase holoenzyme
    • Murakami K., Darst S.A. Insights into transcription initiation from structural studies of bacterial RNA polymerase holoenzyme. Curr. Opin. Struct. Biol. 13:2003;131-139.
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 131-139
    • Murakami, K.1    Darst, S.A.2
  • 48
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • a
    • Murakami K., Masuda S., Darst S.A. Structural basis of transcription initiation. RNA polymerase holoenzyme at 4 Å resolution Science. 269:2002;1280-1284. a.
    • (2002) Science , vol.269 , pp. 1280-1284
    • Murakami, K.1    Masuda, S.2    Darst, S.A.3
  • 49
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • b
    • Murakami K., Masuda S., E.A C., Muzzin O., Darst S.A. Structural basis of transcription initiation. an RNA polymerase holoenzyme-DNA complex Science. 296:2002;1285-1290. b.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.1    Masuda S.E.A, C.2    Muzzin, O.3    Darst, S.A.4
  • 50
    • 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. D. 53:1997;240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 51
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association. insights from the interfacial and thermodynamic properties of hydrocarbons Proteins: Structure, Function and Genetics. 11:1991;281-296.
    • (1991) Proteins: Structure, Function and Genetics , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 52
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy-atom parameters in isomorphous replacement and anomalous scattering
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington, United Kingdom: SERC Daresbury Laboratory. 80-86.pp
    • Otwinowski Z. Maximum likelihood refinement of heavy-atom parameters in isomorphous replacement and anomalous scattering. Wolf W., Evans P.R., Leslie A.G.W. Proceedings of the CCP4 Study Weekend. 1991;SERC Daresbury Laboratory, Warrington, United Kingdom. 80-86.pp.
    • (1991) Proceedings of the CCP4 Study Weekend
    • Otwinowski, Z.1
  • 53
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 54
    • 0028925747 scopus 로고
    • Bacteriophage T4 MotA and AsiA proteins suffice to direct Escherichia coli RNA polymerase to initiate transcription at T4 middle promoters
    • Ouhammouch M., Adelman K., Harvey S.R., Orsini G., Brody E.N. Bacteriophage T4 MotA and AsiA proteins suffice to direct Escherichia coli RNA polymerase to initiate transcription at T4 middle promoters. Proc. Natl. Acad. Sci. USA. 92:1995;1451-1455.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1451-1455
    • Ouhammouch, M.1    Adelman, K.2    Harvey, S.R.3    Orsini, G.4    Brody, E.N.5
  • 55
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:1999;458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 57
    • 0034780493 scopus 로고    scopus 로고
    • Periplasmic stress and ECF sigma factors
    • Raivio T.L., Silhavy T.J. Periplasmic stress and ECF sigma factors. Annu. Rev. Microbiol. 55:2001;591-624.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 591-624
    • Raivio, T.L.1    Silhavy, T.J.2
  • 59
    • 0033593022 scopus 로고    scopus 로고
    • A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors
    • Rudner D.Z., Fawcett P., Losick R. A family of membrane-embedded metalloproteases involved in regulated proteolysis of membrane-associated transcription factors. Proc. Natl. Acad. Sci. USA. 96:1999;14765-14770.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14765-14770
    • Rudner, D.Z.1    Fawcett, P.2    Losick, R.3
  • 60
    • 0032577371 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli RNA polymerase by bacteriophage T4 AsiA
    • Severinova E., Severinov K., Darst S.A. Inhibition of Escherichia coli RNA polymerase by bacteriophage T4 AsiA. J. Mol. Biol. 279:1998;9-18.
    • (1998) J. Mol. Biol. , vol.279 , pp. 9-18
    • Severinova, E.1    Severinov, K.2    Darst, S.A.3
  • 62
    • 0014007813 scopus 로고
    • Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of slufite and hydroxylamine reductases
    • Siegel L.M., Monty K.J. Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of slufite and hydroxylamine reductases. Biochim. Biophys. Acta. 112:1966;346-362.
    • (1966) Biochim. Biophys. Acta , vol.112 , pp. 346-362
    • Siegel, L.M.1    Monty, K.J.2
  • 63
    • 0017595440 scopus 로고
    • Inhibition of DNA-enzyme binding by an RNA polymerase inhibitor from T4 phage-infected Escherichia coli
    • Stevens A. Inhibition of DNA-enzyme binding by an RNA polymerase inhibitor from T4 phage-infected Escherichia coli. Biochim. Biophys. Acta. 475:1977;193-196.
    • (1977) Biochim. Biophys. Acta , vol.475 , pp. 193-196
    • Stevens, A.1
  • 64
    • 0022253253 scopus 로고
    • Two functional domains conserved in major and alternate bacterial sigma factors
    • Stragier P., Parsot C., Bouvier J. Two functional domains conserved in major and alternate bacterial sigma factors. FEBS Lett. 187:1985;11-15.
    • (1985) FEBS Lett. , vol.187 , pp. 11-15
    • Stragier, P.1    Parsot, C.2    Bouvier, J.3
  • 68
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks C.M., Miller R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32:1999;120-124.
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 69
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn M.D., Isupov M.N., Murshudov G.N. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D. 57:2001;122-123.
    • (2001) Acta Crystallogr. D , vol.57 , pp. 122-123
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 70


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