메뉴 건너뛰기




Volumn 79, Issue , 2005, Pages 339-369

The Second Paradigm for Activation of Transcription

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; DNA DIRECTED RNA POLYMERASE; SIGMA FACTOR; SIGMA FACTOR RPON; TRANSACTIVATOR PROTEIN;

EID: 23944492419     PISSN: 00796603     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-6603(04)79007-8     Document Type: Review
Times cited : (34)

References (149)
  • 2
    • 0034671288 scopus 로고    scopus 로고
    • RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II
    • Ebright R.H. RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II. J. Mol. Biol. 304 (2000) 687-698
    • (2000) J. Mol. Biol. , vol.304 , pp. 687-698
    • Ebright, R.H.1
  • 3
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby S., and Ebright R.H. Transcription activation by catabolite activator protein (CAP). J. Mol. Biol. 293 (1999) 199-213
    • (1999) J. Mol. Biol. , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 4
    • 0032035329 scopus 로고    scopus 로고
    • Positive activation of gene expression
    • Rhodius V.A., and Busby S.J. Positive activation of gene expression. Curr. Opin. Microbiol. 1 (1998) 152-159
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 152-159
    • Rhodius, V.A.1    Busby, S.J.2
  • 6
    • 0030960672 scopus 로고    scopus 로고
    • Transcriptional activation by recruitment
    • Ptashne M., and Gann A. Transcriptional activation by recruitment. Nature 386 (1997) 569-577
    • (1997) Nature , vol.386 , pp. 569-577
    • Ptashne, M.1    Gann, A.2
  • 7
    • 0014663102 scopus 로고
    • Factor stimulating transcription by RNA polymerase
    • Burgess R.R., Travers A.A., Dunn J.J., and Bautz E.K. Factor stimulating transcription by RNA polymerase. Nature 221 (1969) 43-46
    • (1969) Nature , vol.221 , pp. 43-46
    • Burgess, R.R.1    Travers, A.A.2    Dunn, J.J.3    Bautz, E.K.4
  • 8
    • 0023918675 scopus 로고
    • Structure and function of bacterial sigma factors
    • Helmann J.D., and 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
  • 9
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • Gruber T.M., and Gross C.A. Multiple sigma subunits and the partitioning of bacterial transcription space. Annu. Rev. Microbiol. 57 (2003) 441-466
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 10
    • 0037261948 scopus 로고    scopus 로고
    • The sigma70 family of sigma factors
    • Paget M.S., and Helmann J.D. The sigma70 family of sigma factors. Genome Biol. 4 (2003) 203
    • (2003) Genome Biol. , vol.4 , pp. 203
    • Paget, M.S.1    Helmann, J.D.2
  • 11
    • 0033912262 scopus 로고    scopus 로고
    • The bacterial enhancer-dependent sigma(54) (sigma(N)) transcription factor
    • Buck M., Gallegos M.T., Studholme D.J., Guo Y., and Gralla J.D. The bacterial enhancer-dependent sigma(54) (sigma(N)) transcription factor. J. Bacteriol. 182 (2000) 4129-4136
    • (2000) J. Bacteriol. , vol.182 , pp. 4129-4136
    • Buck, M.1    Gallegos, M.T.2    Studholme, D.J.3    Guo, Y.4    Gralla, J.D.5
  • 12
    • 0027770723 scopus 로고
    • In a class of its own: The RNA polymerase sigma factor sigma 54 (sigma N)
    • Merrick M.J. In a class of its own: The RNA polymerase sigma factor sigma 54 (sigma N). Mol. Microbiol. 10 (1993) 903-909
    • (1993) Mol. Microbiol. , vol.10 , pp. 903-909
    • Merrick, M.J.1
  • 13
    • 1842591130 scopus 로고    scopus 로고
    • The regulation of bacterial transcription initiation
    • Browning D.F., and Busby S.J. The regulation of bacterial transcription initiation. Nature Rev. Microbiol. 2 (2004) 57-65
    • (2004) Nature Rev. Microbiol. , vol.2 , pp. 57-65
    • Browning, D.F.1    Busby, S.J.2
  • 14
    • 0035066617 scopus 로고    scopus 로고
    • Transcriptional regulation at a distance in bacteria
    • Xu H., and Hoover T.R. Transcriptional regulation at a distance in bacteria. Curr. Opin. Microbiol. 4 (2001) 138-144
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 138-144
    • Xu, H.1    Hoover, T.R.2
  • 16
    • 2142707172 scopus 로고    scopus 로고
    • ATP-dependent transcriptional activation by bacterial PspF AAA+ protein
    • Schumacher J., Zhang X., Jones S., Bordes P., and Buck M. ATP-dependent transcriptional activation by bacterial PspF AAA+ protein. J. Mol. Biol. 338 (2004) 863-875
    • (2004) J. Mol. Biol. , vol.338 , pp. 863-875
    • Schumacher, J.1    Zhang, X.2    Jones, S.3    Bordes, P.4    Buck, M.5
  • 17
    • 0032164070 scopus 로고    scopus 로고
    • Active recruitment of sigma54-RNA polymerase to the Pu promoter of Pseudomonas putida: Role of IHF and alphaCTD
    • Bertoni G., Fujita N., Ishihama A., and de Lorenzo V. Active recruitment of sigma54-RNA polymerase to the Pu promoter of Pseudomonas putida: Role of IHF and alphaCTD. EMBO J. 17 (1998) 5120-5128
    • (1998) EMBO J. , vol.17 , pp. 5120-5128
    • Bertoni, G.1    Fujita, N.2    Ishihama, A.3    de Lorenzo, V.4
  • 18
    • 0022545682 scopus 로고
    • Upstream activator sequences are present in the promoters of nitrogen fixation genes
    • Buck M., Miller S., Drummond M., and Dixon R. Upstream activator sequences are present in the promoters of nitrogen fixation genes. Nature 320 (1986) 374-378
    • (1986) Nature , vol.320 , pp. 374-378
    • Buck, M.1    Miller, S.2    Drummond, M.3    Dixon, R.4
  • 19
    • 0022446209 scopus 로고
    • Transcription of glnA in E. coli is stimulated by activator bound to sites far from the promoter
    • Reitzer L.J., and Magasanik B. Transcription of glnA in E. coli is stimulated by activator bound to sites far from the promoter. Cell 45 (1986) 785-792
    • (1986) Cell , vol.45 , pp. 785-792
    • Reitzer, L.J.1    Magasanik, B.2
  • 20
    • 0036777449 scopus 로고    scopus 로고
    • FleQ, the major flagellar gene regulator in Pseudomonas aeruginosa, binds to enhancer sites located either upstream or atypically downstream of the RpoN binding site
    • Jyot J., Dasgupta N., and Ramphal R. FleQ, the major flagellar gene regulator in Pseudomonas aeruginosa, binds to enhancer sites located either upstream or atypically downstream of the RpoN binding site. J. Bacteriol. 184 (2002) 5251-5260
    • (2002) J. Bacteriol. , vol.184 , pp. 5251-5260
    • Jyot, J.1    Dasgupta, N.2    Ramphal, R.3
  • 21
    • 0025035371 scopus 로고
    • DNA-looping and enhancer activity: Association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter
    • Su W., Porter S., Kustu S., and Echols H. DNA-looping and enhancer activity: Association between DNA-bound NtrC activator and RNA polymerase at the bacterial glnA promoter. Proc. Natl. Acad. Sci. USA 87 (1990) 5504-5508
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5504-5508
    • Su, W.1    Porter, S.2    Kustu, S.3    Echols, H.4
  • 22
    • 0025012093 scopus 로고
    • The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons
    • Hoover T.R., Santero E., Porter S., and Kustu S. The integration host factor stimulates interaction of RNA polymerase with NIFA, the transcriptional activator for nitrogen fixation operons. Cell 63 (1990) 11-22
    • (1990) Cell , vol.63 , pp. 11-22
    • Hoover, T.R.1    Santero, E.2    Porter, S.3    Kustu, S.4
  • 23
    • 0032992369 scopus 로고    scopus 로고
    • Role of ArgR in activation of the ast operon, encoding enzymes of the arginine succinyl transferase pathway in Salmonella typhimurium
    • Lu C.D., and Abdelal A.T. Role of ArgR in activation of the ast operon, encoding enzymes of the arginine succinyl transferase pathway in Salmonella typhimurium. J. Bacteriol. 181 (1999) 1934-1938
    • (1999) J. Bacteriol. , vol.181 , pp. 1934-1938
    • Lu, C.D.1    Abdelal, A.T.2
  • 24
    • 0030931164 scopus 로고    scopus 로고
    • DNA bending and the initiation of transcription at sigma54-dependent bacterial promoters
    • Carmona M., Claverie-Martin F., and Magasanik B. DNA bending and the initiation of transcription at sigma54-dependent bacterial promoters. Proc. Natl. Acad. Sci. USA 94 (1997) 9568-9572
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9568-9572
    • Carmona, M.1    Claverie-Martin, F.2    Magasanik, B.3
  • 25
    • 0033857305 scopus 로고    scopus 로고
    • Promoter opening by sigma(54) and sigma(70) RNA polymerases: Sigma factor-directed alterations in the mechanism and tightness of control
    • Guo Y., Lew C.M., and Gralla J.D. Promoter opening by sigma(54) and sigma(70) RNA polymerases: Sigma factor-directed alterations in the mechanism and tightness of control. Genes Dev. 14 (2000) 2242-2255
    • (2000) Genes Dev. , vol.14 , pp. 2242-2255
    • Guo, Y.1    Lew, C.M.2    Gralla, J.D.3
  • 26
    • 0035793716 scopus 로고    scopus 로고
    • Regulatory sequences in sigma 54 localise near the start of DNA melting
    • Wigneshweraraj S.R., Chaney M.K., Ishihama A., and Buck M. Regulatory sequences in sigma 54 localise near the start of DNA melting. J. Mol. Biol. 306 (2001) 681-701
    • (2001) J. Mol. Biol. , vol.306 , pp. 681-701
    • Wigneshweraraj, S.R.1    Chaney, M.K.2    Ishihama, A.3    Buck, M.4
  • 27
    • 4844230879 scopus 로고    scopus 로고
    • Reorganisation of an RNA polymerase-promoter DNA complex for DNA melting
    • Burrows P.C., Severinov K., Buck M., and Wigneshweraraj S.R. Reorganisation of an RNA polymerase-promoter DNA complex for DNA melting. EMBO J 23 (2004) 4253-4263
    • (2004) EMBO J , vol.23 , pp. 4253-4263
    • Burrows, P.C.1    Severinov, K.2    Buck, M.3    Wigneshweraraj, S.R.4
  • 28
    • 0011064770 scopus 로고
    • Products of nitrogen regulatory genes ntrA and ntrC of enteric bacteria activate glnA transcription in vitro: Evidence that the ntrA product is a sigma factor
    • Hirschman J., Wong P.K., Sei K., Keener J., and Kustu S. Products of nitrogen regulatory genes ntrA and ntrC of enteric bacteria activate glnA transcription in vitro: Evidence that the ntrA product is a sigma factor. Proc. Natl. Acad. Sci. USA 82 (1985) 7525-7529
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7525-7529
    • Hirschman, J.1    Wong, P.K.2    Sei, K.3    Keener, J.4    Kustu, S.5
  • 29
    • 0345758482 scopus 로고
    • Transcription of glnA by purified Escherichia coli components: Core RNA polymerase and the products of glnF, glnG, and glnL
    • Hunt T.P., and Magasanik B. Transcription of glnA by purified Escherichia coli components: Core RNA polymerase and the products of glnF, glnG, and glnL. Proc. Natl. Acad. Sci. USA 82 (1985) 8453-8457
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8453-8457
    • Hunt, T.P.1    Magasanik, B.2
  • 30
    • 0024830930 scopus 로고
    • Mutations in genes downstream of the rpoN gene (encoding sigma 54) of Klebsiella pneumoniae affect expression from sigma 54-dependent promoters
    • Merrick M.J., and Coppard J.R. Mutations in genes downstream of the rpoN gene (encoding sigma 54) of Klebsiella pneumoniae affect expression from sigma 54-dependent promoters. Mol. Microbiol. 3 (1989) 1765-1775
    • (1989) Mol. Microbiol. , vol.3 , pp. 1765-1775
    • Merrick, M.J.1    Coppard, J.R.2
  • 31
    • 0034822014 scopus 로고    scopus 로고
    • Metabolic context and possible physiological themes of sigma(54)-dependent genes in Escherichia coli
    • Reitzer L., and Schneider B.L. Metabolic context and possible physiological themes of sigma(54)-dependent genes in Escherichia coli. Microbiol. Mol. Biol. Rev. 65 (2001) 422-444
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 422-444
    • Reitzer, L.1    Schneider, B.L.2
  • 32
    • 0034192966 scopus 로고    scopus 로고
    • The biology of enhancer-dependent transcriptional regulation in bacteria: Insights from genome sequences
    • Studholme D.J., and Buck M. The biology of enhancer-dependent transcriptional regulation in bacteria: Insights from genome sequences. FEMS Microbiol. Lett. 186 (2000) 1-9
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 1-9
    • Studholme, D.J.1    Buck, M.2
  • 33
    • 0034666279 scopus 로고    scopus 로고
    • Competition among seven Escherichia coli sigma subunits: Relative binding affinities to the core RNA polymerase
    • Maeda H., Fujita N., and Ishihama A. Competition among seven Escherichia coli sigma subunits: Relative binding affinities to the core RNA polymerase. Nucleic Acids Res. 28 (2000) 3497-3503
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3497-3503
    • Maeda, H.1    Fujita, N.2    Ishihama, A.3
  • 34
    • 0029029993 scopus 로고
    • Core RNA polymerase and promoter DNA interactions of purified domains of sigma N: bipartite functions
    • Cannon W., Missailidis S., Smith C., Cottier A., Austin S., Moore M., and Buck M. Core RNA polymerase and promoter DNA interactions of purified domains of sigma N: bipartite functions. J. Mol. Biol. 248 (1995) 781-803
    • (1995) J. Mol. Biol. , vol.248 , pp. 781-803
    • Cannon, W.1    Missailidis, S.2    Smith, C.3    Cottier, A.4    Austin, S.5    Moore, M.6    Buck, M.7
  • 35
    • 0032588981 scopus 로고    scopus 로고
    • Sequences in sigmaN determining holoenzyme formation and properties
    • Gallegos M.T., and Buck M. Sequences in sigmaN determining holoenzyme formation and properties. J. Mol. Biol. 288 (1999) 539-553
    • (1999) J. Mol. Biol. , vol.288 , pp. 539-553
    • Gallegos, M.T.1    Buck, M.2
  • 36
    • 0023496357 scopus 로고
    • The nucleotide sequence of the sigma factor gene ntrA (rpoN) of Azotobacter vinelandii: Analysis of conserved sequences in NtrA proteins
    • Merrick M., Gibbins J., and Toukdarian A. The nucleotide sequence of the sigma factor gene ntrA (rpoN) of Azotobacter vinelandii: Analysis of conserved sequences in NtrA proteins. Mol. Gen. Genet. 210 (1987) 323-330
    • (1987) Mol. Gen. Genet. , vol.210 , pp. 323-330
    • Merrick, M.1    Gibbins, J.2    Toukdarian, A.3
  • 37
    • 0025180626 scopus 로고
    • Role of eukaryotic-type functional domains found in the prokaryotic enhancer receptor factor sigma 54
    • Sasse-Dwight S., and Gralla J.D. Role of eukaryotic-type functional domains found in the prokaryotic enhancer receptor factor sigma 54. Cell 62 (1990) 945-954
    • (1990) Cell , vol.62 , pp. 945-954
    • Sasse-Dwight, S.1    Gralla, J.D.2
  • 38
    • 0028316752 scopus 로고
    • The domain structure of sigma 54 as determined by analysis of a set of deletion mutants
    • Wong C., Tintut Y., and Gralla J.D. The domain structure of sigma 54 as determined by analysis of a set of deletion mutants. J. Mol. Biol. 236 (1994) 81-90
    • (1994) J. Mol. Biol. , vol.236 , pp. 81-90
    • Wong, C.1    Tintut, Y.2    Gralla, J.D.3
  • 39
    • 0035937702 scopus 로고    scopus 로고
    • Roles for the C-terminal region of sigma 54 in transcriptional silencing and DNA binding
    • Wang L., and Gralla J.D. Roles for the C-terminal region of sigma 54 in transcriptional silencing and DNA binding. J. Biol. Chem. 276 (2001) 8979-8986
    • (2001) J. Biol. Chem. , vol.276 , pp. 8979-8986
    • Wang, L.1    Gralla, J.D.2
  • 40
    • 0033764355 scopus 로고    scopus 로고
    • Transcription initiation-defective forms of sigma(54) that differ in ability to function with a heteroduplex DNA template
    • Kelly M.T., Ferguson III J.A., and Hoover T.R. Transcription initiation-defective forms of sigma(54) that differ in ability to function with a heteroduplex DNA template. J. Bacteriol. 182 (2000) 6503-6508
    • (2000) J. Bacteriol. , vol.182 , pp. 6503-6508
    • Kelly, M.T.1    Ferguson III, J.A.2    Hoover, T.R.3
  • 41
    • 0026464921 scopus 로고
    • A role for the acidic trimer repeat region of transcription factor sigma 54 in setting the rate and temperature dependence of promoter melting in vivo
    • Wong C., and Gralla J.D. A role for the acidic trimer repeat region of transcription factor sigma 54 in setting the rate and temperature dependence of promoter melting in vivo. J. Biol. Chem. 267 (1992) 24762-24768
    • (1992) J. Biol. Chem. , vol.267 , pp. 24762-24768
    • Wong, C.1    Gralla, J.D.2
  • 42
    • 0034234457 scopus 로고    scopus 로고
    • The role of region II in the RNA polymerase sigma factor sigma(N) (sigma(54))
    • Southern E., and Merrick M. The role of region II in the RNA polymerase sigma factor sigma(N) (sigma(54)). Nucleic Acids Res. 28 (2000) 2563-2570
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2563-2570
    • Southern, E.1    Merrick, M.2
  • 44
    • 0034635484 scopus 로고    scopus 로고
    • Low resolution structure of the sigma54 transcription factor revealed by X-ray solution scattering
    • Svergun D.I., Malfois M., Koch M.H., Wigneshweraraj S.R., and Buck M. Low resolution structure of the sigma54 transcription factor revealed by X-ray solution scattering. J. Biol. Chem. 275 (2000) 4210-4214
    • (2000) J. Biol. Chem. , vol.275 , pp. 4210-4214
    • Svergun, D.I.1    Malfois, M.2    Koch, M.H.3    Wigneshweraraj, S.R.4    Buck, M.5
  • 45
    • 0033619725 scopus 로고    scopus 로고
    • Targeted protein footprinting: Where different transcription factors bind to RNA polymerase
    • Traviglia S.L., Datwyler S.A., Yan D., Ishihama A., and Meares C.F. Targeted protein footprinting: Where different transcription factors bind to RNA polymerase. Biochemistry 38 (1999) 15774-15778
    • (1999) Biochemistry , vol.38 , pp. 15774-15778
    • Traviglia, S.L.1    Datwyler, S.A.2    Yan, D.3    Ishihama, A.4    Meares, C.F.5
  • 46
    • 0034660249 scopus 로고    scopus 로고
    • Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes
    • Wigneshweraraj S.R., Fujita N., Ishihama A., and Buck M. Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes. EMBO J. 19 (2000) 3038-3048
    • (2000) EMBO J. , vol.19 , pp. 3038-3048
    • Wigneshweraraj, S.R.1    Fujita, N.2    Ishihama, A.3    Buck, M.4
  • 47
    • 0033555643 scopus 로고    scopus 로고
    • Region I modifies DNA-binding domain conformation of sigma 54 within the holoenzyme
    • Casaz P., and Buck M. Region I modifies DNA-binding domain conformation of sigma 54 within the holoenzyme. J. Mol. Biol. 285 (1999) 507-514
    • (1999) J. Mol. Biol. , vol.285 , pp. 507-514
    • Casaz, P.1    Buck, M.2
  • 48
    • 0034535611 scopus 로고    scopus 로고
    • Interaction of sigma factor sigmaN with Escherichia coli RNA polymerase core enzyme
    • Scott D.J., Ferguson A.L., Gallegos M.T., Pitt M., Buck M., and Hoggett J.G. Interaction of sigma factor sigmaN with Escherichia coli RNA polymerase core enzyme. Biochem. J. 352 (2000) 539-547
    • (2000) Biochem. J. , vol.352 , pp. 539-547
    • Scott, D.J.1    Ferguson, A.L.2    Gallegos, M.T.3    Pitt, M.4    Buck, M.5    Hoggett, J.G.6
  • 49
    • 0028789094 scopus 로고
    • Converting Escherichia coli RNA polymerase into an enhancer-responsive enzyme: Role of an NH2-terminal leucine patch in sigma 54
    • Wang J.T., Syed A., Hsieh M., and Gralla J.D. Converting Escherichia coli RNA polymerase into an enhancer-responsive enzyme: Role of an NH2-terminal leucine patch in sigma 54. Science 270 (1995) 992-994
    • (1995) Science , vol.270 , pp. 992-994
    • Wang, J.T.1    Syed, A.2    Hsieh, M.3    Gralla, J.D.4
  • 50
    • 0034615697 scopus 로고    scopus 로고
    • Sequences in sigma(54) region I required for binding to early melted DNA and their involvement in sigma-DNA isomerisation
    • Gallegos M.T., and Buck M. Sequences in sigma(54) region I required for binding to early melted DNA and their involvement in sigma-DNA isomerisation. J. Mol. Biol. 297 (2000) 849-859
    • (2000) J. Mol. Biol. , vol.297 , pp. 849-859
    • Gallegos, M.T.1    Buck, M.2
  • 51
    • 0031028731 scopus 로고    scopus 로고
    • Isolation and properties of enhancer-bypass mutants of sigma 54
    • Syed A., and Gralla J.D. Isolation and properties of enhancer-bypass mutants of sigma 54. Mol. Microbiol. 23 (1997) 987-995
    • (1997) Mol. Microbiol. , vol.23 , pp. 987-995
    • Syed, A.1    Gralla, J.D.2
  • 52
    • 0033578493 scopus 로고    scopus 로고
    • Systematic analysis of sigma54 N-terminal sequences identifies regions involved in positive and negative regulation of transcription
    • Casaz P., Gallegos M.T., and Buck M. Systematic analysis of sigma54 N-terminal sequences identifies regions involved in positive and negative regulation of transcription. J. Mol. Biol. 292 (1999) 229-239
    • (1999) J. Mol. Biol. , vol.292 , pp. 229-239
    • Casaz, P.1    Gallegos, M.T.2    Buck, M.3
  • 53
    • 0033520123 scopus 로고    scopus 로고
    • Functions of the sigma(54) region I in trans and implications for transcription activation
    • Gallegos M.T., Cannon W.V., and Buck M. Functions of the sigma(54) region I in trans and implications for transcription activation. J. Biol. Chem. 274 (1999) 25285-25290
    • (1999) J. Biol. Chem. , vol.274 , pp. 25285-25290
    • Gallegos, M.T.1    Cannon, W.V.2    Buck, M.3
  • 54
    • 0033083794 scopus 로고    scopus 로고
    • Amino-terminal sequences of sigmaN (sigma54) inhibit RNA polymerase isomerization
    • Cannon W., Gallegos M.T., Casaz P., and Buck M. Amino-terminal sequences of sigmaN (sigma54) inhibit RNA polymerase isomerization. Genes Dev. 13 (1999) 357-370
    • (1999) Genes Dev. , vol.13 , pp. 357-370
    • Cannon, W.1    Gallegos, M.T.2    Casaz, P.3    Buck, M.4
  • 56
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • Murakami K.S., Masuda S., and Darst S.A. Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science 296 (2002) 1280-1284
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 58
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang G., Campbell E.A., Minakhin L., Richter C., Severinov K., and Darst S.A. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell 98 (1999) 811-824
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 60
    • 0029822092 scopus 로고    scopus 로고
    • The RpoN-box motif of the RNA polymerase sigma factor sigma N plays a role in promoter recognition
    • Taylor M., Butler R., Chambers S., Casimiro M., Badii F., and Merrick M. The RpoN-box motif of the RNA polymerase sigma factor sigma N plays a role in promoter recognition. Mol. Microbiol. 22 (1996) 1045-1054
    • (1996) Mol. Microbiol. , vol.22 , pp. 1045-1054
    • Taylor, M.1    Butler, R.2    Chambers, S.3    Casimiro, M.4    Badii, F.5    Merrick, M.6
  • 61
    • 0026592145 scopus 로고
    • The helix-turn-helix motif of sigma 54 is involved in recognition of the -13 promoter region
    • Merrick M., and Chambers S. The helix-turn-helix motif of sigma 54 is involved in recognition of the -13 promoter region. J. Bacteriol. 174 (1992) 7221-7226
    • (1992) J. Bacteriol. , vol.174 , pp. 7221-7226
    • Merrick, M.1    Chambers, S.2
  • 62
    • 0025771543 scopus 로고
    • Cassette mutagenesis implicates a helix-turn-helix motif in promoter recognition by the novel RNA polymerase sigma factor sigma 54
    • Coppard J.R., and Merrick M.J. Cassette mutagenesis implicates a helix-turn-helix motif in promoter recognition by the novel RNA polymerase sigma factor sigma 54. Mol. Microbiol. 5 (1991) 1309-1317
    • (1991) Mol. Microbiol. , vol.5 , pp. 1309-1317
    • Coppard, J.R.1    Merrick, M.J.2
  • 63
    • 0043032654 scopus 로고    scopus 로고
    • Mapping sigma 54-RNA polymerase interactions at the -24 consensus promoter element
    • Burrows P.C., Severinov K., Ishihama A., Buck M., and Wigneshweraraj S.R. Mapping sigma 54-RNA polymerase interactions at the -24 consensus promoter element. J. Biol. Chem. 278 (2003) 29728-29743
    • (2003) J. Biol. Chem. , vol.278 , pp. 29728-29743
    • Burrows, P.C.1    Severinov, K.2    Ishihama, A.3    Buck, M.4    Wigneshweraraj, S.R.5
  • 64
    • 0028335281 scopus 로고
    • Identification of a DNA-contacting surface in the transcription factor sigma-54
    • Cannon W., Claverie-Martin F., Austin S., and Buck M. Identification of a DNA-contacting surface in the transcription factor sigma-54. Mol. Microbiol. 11 (1994) 227-236
    • (1994) Mol. Microbiol. , vol.11 , pp. 227-236
    • Cannon, W.1    Claverie-Martin, F.2    Austin, S.3    Buck, M.4
  • 65
    • 0033988987 scopus 로고    scopus 로고
    • The amino terminus of Salmonella enterica serovar Typhimurium sigma(54) is required for interactions with an enhancer-binding protein and binding to fork junction DNA
    • Kelly M.T., and Hoover T.R. The amino terminus of Salmonella enterica serovar Typhimurium sigma(54) is required for interactions with an enhancer-binding protein and binding to fork junction DNA. J. Bacteriol. 182 (2000) 513-517
    • (2000) J. Bacteriol. , vol.182 , pp. 513-517
    • Kelly, M.T.1    Hoover, T.R.2
  • 66
    • 0033168678 scopus 로고    scopus 로고
    • A fork junction DNA-protein switch that controls promoter melting by the bacterial enhancer-dependent sigma factor
    • Guo Y., Wang L., and Gralla J.D. A fork junction DNA-protein switch that controls promoter melting by the bacterial enhancer-dependent sigma factor. EMBO J. 18 (1999) 3736-3745
    • (1999) EMBO J. , vol.18 , pp. 3736-3745
    • Guo, Y.1    Wang, L.2    Gralla, J.D.3
  • 67
    • 0030984217 scopus 로고    scopus 로고
    • Multiple pathways to bypass the enhancer requirement of sigma 54 RNA polymerase: Roles for DNA and protein determinants
    • Wang J.T., Syed A., and Gralla J.D. Multiple pathways to bypass the enhancer requirement of sigma 54 RNA polymerase: Roles for DNA and protein determinants. Proc. Natl. Acad. Sci. USA 94 (1997) 9538-9543
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9538-9543
    • Wang, J.T.1    Syed, A.2    Gralla, J.D.3
  • 68
  • 69
    • 0033570908 scopus 로고    scopus 로고
    • Compilation and analysis of sigma(54)-dependent promoter sequences
    • Barrios H., Valderrama B., and Morett E. Compilation and analysis of sigma(54)-dependent promoter sequences. Nucleic Acids Res. 27 (1999) 4305-4313
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4305-4313
    • Barrios, H.1    Valderrama, B.2    Morett, E.3
  • 70
    • 0029123818 scopus 로고
    • An early A-signal-dependent gene in Myxococcus xanthus has a sigma 54-like promoter
    • Keseler I.M., and Kaiser D. An early A-signal-dependent gene in Myxococcus xanthus has a sigma 54-like promoter. J. Bacteriol. 177 (1995) 4638-4644
    • (1995) J. Bacteriol. , vol.177 , pp. 4638-4644
    • Keseler, I.M.1    Kaiser, D.2
  • 71
    • 0022580666 scopus 로고
    • Deletion analysis of the Klebsiella pneumoniae nitrogenase promoter: importance of spacing between conserved sequences around positions -12 and -24 for activation by the nifA and ntrC (glnG) products
    • Buck M. Deletion analysis of the Klebsiella pneumoniae nitrogenase promoter: importance of spacing between conserved sequences around positions -12 and -24 for activation by the nifA and ntrC (glnG) products. J. Bacteriol. 166 (1986) 545-551
    • (1986) J. Bacteriol. , vol.166 , pp. 545-551
    • Buck, M.1
  • 72
    • 0024495733 scopus 로고
    • Escherichia coli sigma 54 RNA polymerase recognizes Caulobacter crescentus flbG and flaN flagellar gene promoters in vitro
    • Ninfa A.J., Mullin D.A., Ramakrishnan G., and Newton A. Escherichia coli sigma 54 RNA polymerase recognizes Caulobacter crescentus flbG and flaN flagellar gene promoters in vitro. J. Bacteriol. 171 (1989) 383-391
    • (1989) J. Bacteriol. , vol.171 , pp. 383-391
    • Ninfa, A.J.1    Mullin, D.A.2    Ramakrishnan, G.3    Newton, A.4
  • 73
    • 0028301602 scopus 로고
    • DNA distortion and nucleation of local DNA unwinding within sigma-54 (sigma N) holoenzyme closed promoter complexes
    • Morris L., Cannon W., Claverie-Martin F., Austin S., and Buck M. DNA distortion and nucleation of local DNA unwinding within sigma-54 (sigma N) holoenzyme closed promoter complexes. J. Biol. Chem. 269 (1994) 11563-11571
    • (1994) J. Biol. Chem. , vol.269 , pp. 11563-11571
    • Morris, L.1    Cannon, W.2    Claverie-Martin, F.3    Austin, S.4    Buck, M.5
  • 74
    • 0032785893 scopus 로고    scopus 로고
    • Regulation of sigma 54-dependent transcription by core promoter sequences: Role of -12 region nucleotides
    • Wang L., Guo Y., and Gralla J.D. Regulation of sigma 54-dependent transcription by core promoter sequences: Role of -12 region nucleotides. J. Bacteriol. 181 (1999) 7558-7565
    • (1999) J. Bacteriol. , vol.181 , pp. 7558-7565
    • Wang, L.1    Guo, Y.2    Gralla, J.D.3
  • 75
    • 0031740289 scopus 로고    scopus 로고
    • Multiple in vivo roles for the -12-region elements of sigma 54 promoters
    • Wang L., and Gralla J.D. Multiple in vivo roles for the -12-region elements of sigma 54 promoters. J. Bacteriol. 180 (1998) 5626-5631
    • (1998) J. Bacteriol. , vol.180 , pp. 5626-5631
    • Wang, L.1    Gralla, J.D.2
  • 76
    • 0037082415 scopus 로고    scopus 로고
    • Correlating protein footprinting with mutational analysis in the bacterial transcription factor sigma54 (sigmaN)
    • Wigneshweraraj S.R., Casaz P., and Buck M. Correlating protein footprinting with mutational analysis in the bacterial transcription factor sigma54 (sigmaN). Nucleic Acids Res. 30 (2002) 1016-1028
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1016-1028
    • Wigneshweraraj, S.R.1    Casaz, P.2    Buck, M.3
  • 77
    • 0035282873 scopus 로고    scopus 로고
    • In vitro roles of invariant helix-turn-helix motif residue R383 in sigma(54) (sigma(N))
    • Wigneshweraraj S.R., Ishihama A., and Buck M. In vitro roles of invariant helix-turn-helix motif residue R383 in sigma(54) (sigma(N)). Nucleic Acids Res. 29 (2001) 1163-1174
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1163-1174
    • Wigneshweraraj, S.R.1    Ishihama, A.2    Buck, M.3
  • 78
    • 0032854067 scopus 로고    scopus 로고
    • The sigma 54 DNA-binding domain includes a determinant of enhancer responsiveness
    • Chaney M., and Buck M. The sigma 54 DNA-binding domain includes a determinant of enhancer responsiveness. Mol. Microbiol. 33 (1999) 1200-1209
    • (1999) Mol. Microbiol. , vol.33 , pp. 1200-1209
    • Chaney, M.1    Buck, M.2
  • 79
    • 0032578471 scopus 로고    scopus 로고
    • Promoter opening via a DNA fork junction binding activity
    • Guo Y., and Gralla J.D. Promoter opening via a DNA fork junction binding activity. Proc. Natl. Acad. Sci. USA 95 (1998) 11655-11660
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11655-11660
    • Guo, Y.1    Gralla, J.D.2
  • 80
    • 0033938884 scopus 로고    scopus 로고
    • Isomerization of a binary sigma-promoter DNA complex by transcription activators
    • Cannon W.V., Gallegos M.T., and Buck M. Isomerization of a binary sigma-promoter DNA complex by transcription activators. Nature Struct. Biol. 7 (2000) 594-601
    • (2000) Nature Struct. Biol. , vol.7 , pp. 594-601
    • Cannon, W.V.1    Gallegos, M.T.2    Buck, M.3
  • 81
    • 0037474295 scopus 로고    scopus 로고
    • Multiple roles of the RNA polymerase beta subunit flap domain in sigma 54-dependent transcription
    • Wigneshweraraj S.R., Kuznedelov K., Severinov K., and Buck M. Multiple roles of the RNA polymerase beta subunit flap domain in sigma 54-dependent transcription. J. Biol. Chem. 278 (2003) 3455-3465
    • (2003) J. Biol. Chem. , vol.278 , pp. 3455-3465
    • Wigneshweraraj, S.R.1    Kuznedelov, K.2    Severinov, K.3    Buck, M.4
  • 82
    • 0037490143 scopus 로고    scopus 로고
    • Nucleotide-dependent triggering of RNA polymerase-DNA interactions by an AAA regulator of transcription
    • Cannon W., Bordes P., Wigneshweraraj S.R., and Buck M. Nucleotide-dependent triggering of RNA polymerase-DNA interactions by an AAA regulator of transcription. J. Biol. Chem. 278 (2003) 19815-19825
    • (2003) J. Biol. Chem. , vol.278 , pp. 19815-19825
    • Cannon, W.1    Bordes, P.2    Wigneshweraraj, S.R.3    Buck, M.4
  • 85
    • 0033607619 scopus 로고    scopus 로고
    • Suppression analysis of positive control mutants of NifA reveals two overlapping promoters for Klebsiella pneumoniae rpoN
    • Grande R.A., Valderrama B., and Morett E. Suppression analysis of positive control mutants of NifA reveals two overlapping promoters for Klebsiella pneumoniae rpoN. J. Mol. Biol. 294 (1999) 291-298
    • (1999) J. Mol. Biol. , vol.294 , pp. 291-298
    • Grande, R.A.1    Valderrama, B.2    Morett, E.3
  • 86
    • 0037332383 scopus 로고    scopus 로고
    • Domain architectures of sigma54-dependent transcriptional activators
    • Studholme D.J., and Dixon R. Domain architectures of sigma54-dependent transcriptional activators. J. Bacteriol. 185 (2003) 1757-1767
    • (2003) J. Bacteriol. , vol.185 , pp. 1757-1767
    • Studholme, D.J.1    Dixon, R.2
  • 87
    • 0033536573 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of NtrC with three alanine substitutions
    • Pelton J.G., Kustu S., and Wemmer D.E. Solution structure of the DNA-binding domain of NtrC with three alanine substitutions. J. Mol. Biol. 292 (1999) 1095-1110
    • (1999) J. Mol. Biol. , vol.292 , pp. 1095-1110
    • Pelton, J.G.1    Kustu, S.2    Wemmer, D.E.3
  • 88
    • 0037106322 scopus 로고    scopus 로고
    • Secondary structure and DNA binding by the C-terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae
    • Ray P., Smith K.J., Parslow R.A., Dixon R., and Hyde E.I. Secondary structure and DNA binding by the C-terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae. Nucleic Acids Res. 30 (2002) 3972-3980
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3972-3980
    • Ray, P.1    Smith, K.J.2    Parslow, R.A.3    Dixon, R.4    Hyde, E.I.5
  • 89
    • 0028122355 scopus 로고
    • The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain
    • Klose K.E., North A.K., Stedman K.M., and Kustu S. The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain. J. Mol. Biol. 241 (1994) 233-245
    • (1994) J. Mol. Biol. , vol.241 , pp. 233-245
    • Klose, K.E.1    North, A.K.2    Stedman, K.M.3    Kustu, S.4
  • 90
    • 0027391968 scopus 로고
    • Effects of insertions and deletions in glnG (ntrC) of Escherichia coli on nitrogen regulator I-dependent DNA binding and transcriptional activation
    • Shiau S.P., Chen P., and Reitzer L.J. Effects of insertions and deletions in glnG (ntrC) of Escherichia coli on nitrogen regulator I-dependent DNA binding and transcriptional activation. J. Bacteriol. 175 (1993) 190-199
    • (1993) J. Bacteriol. , vol.175 , pp. 190-199
    • Shiau, S.P.1    Chen, P.2    Reitzer, L.J.3
  • 91
    • 4344578623 scopus 로고    scopus 로고
    • Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: A third function for the C-terminal domain
    • Yang X.F., Ji Y., Schneider B.L., and Reitzer L. Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: A third function for the C-terminal domain. J. Biol. Chem. 279 (2004) 36708-36714
    • (2004) J. Biol. Chem. , vol.279 , pp. 36708-36714
    • Yang, X.F.1    Ji, Y.2    Schneider, B.L.3    Reitzer, L.4
  • 92
    • 0033555834 scopus 로고    scopus 로고
    • In vivo and in vitro activities of the Escherichia coli sigma54 transcription activator, PspF, and its DNA-binding mutant, PspFΔHTH
    • Jovanovic G., Rakonjac J., and Model P. In vivo and in vitro activities of the Escherichia coli sigma54 transcription activator, PspF, and its DNA-binding mutant, PspFΔHTH. J. Mol. Biol. 285 (1999) 469-483
    • (1999) J. Mol. Biol. , vol.285 , pp. 469-483
    • Jovanovic, G.1    Rakonjac, J.2    Model, P.3
  • 93
    • 0030894489 scopus 로고    scopus 로고
    • Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein
    • Wyman C., Rombel I., North A.K., Bustamante C., and Kustu S. Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein. Science 275 (1997) 1658-1661
    • (1997) Science , vol.275 , pp. 1658-1661
    • Wyman, C.1    Rombel, I.2    North, A.K.3    Bustamante, C.4    Kustu, S.5
  • 94
    • 3042733355 scopus 로고    scopus 로고
    • Helicobacter pylori FlgR is an enhancer-independent activator of sigma54-RNA polymerase holoenzyme
    • Brahmachary P., Dashti M.G., Olson J.W., and Hoover T.R. Helicobacter pylori FlgR is an enhancer-independent activator of sigma54-RNA polymerase holoenzyme. J. Bacteriol. 186 (2004) 4535-4542
    • (2004) J. Bacteriol. , vol.186 , pp. 4535-4542
    • Brahmachary, P.1    Dashti, M.G.2    Olson, J.W.3    Hoover, T.R.4
  • 95
    • 0033821317 scopus 로고    scopus 로고
    • Phosphorylation-induced signal propagation in the response regulator ntrC
    • Lee J., Owens J.T., Hwang I., Meares C., and Kustu S. Phosphorylation-induced signal propagation in the response regulator ntrC. J. Bacteriol. 182 (2000) 5188-5195
    • (2000) J. Bacteriol. , vol.182 , pp. 5188-5195
    • Lee, J.1    Owens, J.T.2    Hwang, I.3    Meares, C.4    Kustu, S.5
  • 96
    • 0029002441 scopus 로고
    • Active contribution of two domains to cooperative DNA binding of the enhancer-binding protein nitrogen regulator I (NtrC) of Escherichia coli: Stimulation by phosphorylation and the binding of ATP
    • Chen P., and Reitzer L.J. Active contribution of two domains to cooperative DNA binding of the enhancer-binding protein nitrogen regulator I (NtrC) of Escherichia coli: Stimulation by phosphorylation and the binding of ATP. J. Bacteriol. 177 (1995) 2490-2496
    • (1995) J. Bacteriol. , vol.177 , pp. 2490-2496
    • Chen, P.1    Reitzer, L.J.2
  • 97
    • 0142091549 scopus 로고    scopus 로고
    • Regulation of the transcriptional activator NtrC1: Structural studies of the regulatory and AAA+ ATPase domains
    • Lee S.Y., De La Torre A., Yan D., Kustu S., Nixon B.T., and Wemmer D.E. Regulation of the transcriptional activator NtrC1: Structural studies of the regulatory and AAA+ ATPase domains. Genes Dev. 17 (2003) 2552-2563
    • (2003) Genes Dev. , vol.17 , pp. 2552-2563
    • Lee, S.Y.1    De La Torre, A.2    Yan, D.3    Kustu, S.4    Nixon, B.T.5    Wemmer, D.E.6
  • 98
    • 0035695915 scopus 로고    scopus 로고
    • Structural insights into the regulation of bacterial signalling proteins containing PRDs
    • van Tilbeurgh H., and Declerck N. Structural insights into the regulation of bacterial signalling proteins containing PRDs. Curr. Opin. Struct. Biol. 11 (2001) 685-693
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 685-693
    • van Tilbeurgh, H.1    Declerck, N.2
  • 99
  • 100
    • 0031262875 scopus 로고    scopus 로고
    • PAS: A multifunctional domain family comes to light
    • Ponting C.P., and Aravind L. PAS: A multifunctional domain family comes to light. Curr. Biol. 7 (1997) R674-R677
    • (1997) Curr. Biol. , vol.7
    • Ponting, C.P.1    Aravind, L.2
  • 101
    • 0028208257 scopus 로고
    • RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators
    • Calogero S., Gardan R., Glaser P., Schweizer J., Rapoport G., and Debarbouille M. RocR, a novel regulatory protein controlling arginine utilization in Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional activators. J. Bacteriol. 176 (1994) 1234-1241
    • (1994) J. Bacteriol. , vol.176 , pp. 1234-1241
    • Calogero, S.1    Gardan, R.2    Glaser, P.3    Schweizer, J.4    Rapoport, G.5    Debarbouille, M.6
  • 102
    • 0035853296 scopus 로고    scopus 로고
    • Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains
    • Anantharaman V., Koonin E.V., and Aravind L. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 307 (2001) 1271-1292
    • (2001) J. Mol. Biol. , vol.307 , pp. 1271-1292
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 103
    • 0029073435 scopus 로고
    • The amino-terminal domain of the prokaryotic enhancer-binding protein XylR is a specific intramolecular repressor
    • Perez-Martin J., and De Lorenzo V. The amino-terminal domain of the prokaryotic enhancer-binding protein XylR is a specific intramolecular repressor. Proc. Natl. Acad. Sci. USA 92 (1995) 9392-9396
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9392-9396
    • Perez-Martin, J.1    De Lorenzo, V.2
  • 104
    • 0031945812 scopus 로고    scopus 로고
    • Aromatic ligand binding and intramolecular signalling of the phenol-responsive sigma54-dependent regulator DmpR
    • O'Neill E., Ng L.C., Sze C.C., and Shingler V. Aromatic ligand binding and intramolecular signalling of the phenol-responsive sigma54-dependent regulator DmpR. Mol. Microbiol. 28 (1998) 131-141
    • (1998) Mol. Microbiol. , vol.28 , pp. 131-141
    • O'Neill, E.1    Ng, L.C.2    Sze, C.C.3    Shingler, V.4
  • 105
    • 4544275675 scopus 로고    scopus 로고
    • Bacterial transcriptional regulators for degradation pathways of aromatic compounds
    • Tropel D., and Van Der Meer J.R. Bacterial transcriptional regulators for degradation pathways of aromatic compounds. Microbiol. Mol. Biol. Rev. 68 (2004) 474-500
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 474-500
    • Tropel, D.1    Van Der Meer, J.R.2
  • 106
    • 0036009684 scopus 로고    scopus 로고
    • Deciphering the action of aromatic effectors on the prokaryotic enhancer-binding protein XylR: A structural model of its N-terminal domain
    • Devos D., Garmendia J., de Lorenzo V., and Valencia A. Deciphering the action of aromatic effectors on the prokaryotic enhancer-binding protein XylR: A structural model of its N-terminal domain. Environ. Microbiol. 4 (2002) 29-41
    • (2002) Environ. Microbiol. , vol.4 , pp. 29-41
    • Devos, D.1    Garmendia, J.2    de Lorenzo, V.3    Valencia, A.4
  • 107
    • 0034981053 scopus 로고    scopus 로고
    • New insights into the activation of o-xylene biodegradation in Pseudomonas stutzeri OX1 by pathway substrates
    • Arenghi F.L., Barbieri P., Bertoni G., and de Lorenzo V. New insights into the activation of o-xylene biodegradation in Pseudomonas stutzeri OX1 by pathway substrates. EMBO Rep. 2 (2001) 409-414
    • (2001) EMBO Rep. , vol.2 , pp. 409-414
    • Arenghi, F.L.1    Barbieri, P.2    Bertoni, G.3    de Lorenzo, V.4
  • 108
    • 0029132191 scopus 로고
    • Direct regulation of the ATPase activity of the transcriptional activator DmpR by aromatic compounds
    • Shingler V., and Pavel H. Direct regulation of the ATPase activity of the transcriptional activator DmpR by aromatic compounds. Mol. Microbiol. 17 (1995) 505-513
    • (1995) Mol. Microbiol. , vol.17 , pp. 505-513
    • Shingler, V.1    Pavel, H.2
  • 109
    • 0030712081 scopus 로고    scopus 로고
    • The GAF domain: An evolutionary link between diverse phototransducing proteins
    • Aravind L., and Ponting C.P. The GAF domain: An evolutionary link between diverse phototransducing proteins. Trends Biochem. Sci. 22 (1997) 458-459
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 458-459
    • Aravind, L.1    Ponting, C.P.2
  • 110
    • 3042640724 scopus 로고    scopus 로고
    • Role of the amino-terminal GAF domain of the NifA activator in controlling the response to the antiactivator protein NifL
    • Martinez-Argudo I., Little R., and Dixon R. Role of the amino-terminal GAF domain of the NifA activator in controlling the response to the antiactivator protein NifL. Mol. Microbiol. 52 (2004) 1731-1744
    • (2004) Mol. Microbiol. , vol.52 , pp. 1731-1744
    • Martinez-Argudo, I.1    Little, R.2    Dixon, R.3
  • 111
    • 0029874910 scopus 로고    scopus 로고
    • Identification, nucleotide sequence, and characterization of PspF, the transcriptional activator of the Escherichia coli stress-induced psp operon
    • Jovanovic G., Weiner L., and Model P. Identification, nucleotide sequence, and characterization of PspF, the transcriptional activator of the Escherichia coli stress-induced psp operon. J. Bacteriol. 178 (1996) 1936-1945
    • (1996) J. Bacteriol. , vol.178 , pp. 1936-1945
    • Jovanovic, G.1    Weiner, L.2    Model, P.3
  • 112
    • 0242575006 scopus 로고    scopus 로고
    • Secretion defects that activate the phage shock response of Escherichia coli
    • Jones S.E., Lloyd L.J., Tan K.K., and Buck M. Secretion defects that activate the phage shock response of Escherichia coli. J. Bacteriol. 185 (2003) 6707-6711
    • (2003) J. Bacteriol. , vol.185 , pp. 6707-6711
    • Jones, S.E.1    Lloyd, L.J.2    Tan, K.K.3    Buck, M.4
  • 113
    • 0035154988 scopus 로고    scopus 로고
    • The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced
    • Darwin A.J., and Miller V.L. The psp locus of Yersinia enterocolitica is required for virulence and for growth in vitro when the Ysc type III secretion system is produced. Mol. Microbiol. 39 (2001) 429-444
    • (2001) Mol. Microbiol. , vol.39 , pp. 429-444
    • Darwin, A.J.1    Miller, V.L.2
  • 114
    • 0036293607 scopus 로고    scopus 로고
    • Mechanism of action of the Escherichia coli phage shock protein PspA in repression of the AAA family transcription factor PspF
    • Elderkin S., Jones S., Schumacher J., Studholme D., and Buck M. Mechanism of action of the Escherichia coli phage shock protein PspA in repression of the AAA family transcription factor PspF. J. Mol. Biol. 320 (2002) 23-37
    • (2002) J. Mol. Biol. , vol.320 , pp. 23-37
    • Elderkin, S.1    Jones, S.2    Schumacher, J.3    Studholme, D.4    Buck, M.5
  • 115
    • 0033986477 scopus 로고    scopus 로고
    • The PspA protein of Escherichia coli is a negative regulator of sigma(54)-dependent transcription
    • Dworkin J., Jovanovic G., and Model P. The PspA protein of Escherichia coli is a negative regulator of sigma(54)-dependent transcription. J. Bacteriol. 182 (2000) 311-319
    • (2000) J. Bacteriol. , vol.182 , pp. 311-319
    • Dworkin, J.1    Jovanovic, G.2    Model, P.3
  • 116
    • 1542275423 scopus 로고    scopus 로고
    • Organization of the AAA(+) adaptor protein PspA is an oligomeric ring
    • Hankamer B.D., Elderkin S.L., Buck M., and Nield J. Organization of the AAA(+) adaptor protein PspA is an oligomeric ring. J. Biol. Chem. 279 (2004) 8862-8866
    • (2004) J. Biol. Chem. , vol.279 , pp. 8862-8866
    • Hankamer, B.D.1    Elderkin, S.L.2    Buck, M.3    Nield, J.4
  • 117
    • 2442690436 scopus 로고    scopus 로고
    • Purification and characterization of the AAA+ domain of Sinorhizobium meliloti DctD, a sigma54-dependent transcriptional activator
    • Xu H., Gu B., Nixon B.T., and Hoover T.R. Purification and characterization of the AAA+ domain of Sinorhizobium meliloti DctD, a sigma54-dependent transcriptional activator. J. Bacteriol. 186 (2004) 3499-3507
    • (2004) J. Bacteriol. , vol.186 , pp. 3499-3507
    • Xu, H.1    Gu, B.2    Nixon, B.T.3    Hoover, T.R.4
  • 118
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald A.F., Aravind L., Spouge J.L., and Koonin E.V. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9 (1999) 27-43
    • (1999) Genome Res. , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 119
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T., and Wilkinson A.J. AAA+ superfamily ATPases: Common structure-diverse function. Genes Cells 6 (2001) 575-597
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 120
    • 0032557498 scopus 로고    scopus 로고
    • Association states of the transcription activator protein NtrC from E. coli determined by analytical ultracentrifugation
    • Rippe K., Mucke N., and Schulz A. Association states of the transcription activator protein NtrC from E. coli determined by analytical ultracentrifugation. J. Mol. Biol. 278 (1998) 915-933
    • (1998) J. Mol. Biol. , vol.278 , pp. 915-933
    • Rippe, K.1    Mucke, N.2    Schulz, A.3
  • 122
    • 0027340543 scopus 로고
    • The sigma 54 bacterial enhancer-binding protein family: Mechanism of action and phylogenetic relationship of their functional domains
    • Morett E., and Segovia L. The sigma 54 bacterial enhancer-binding protein family: Mechanism of action and phylogenetic relationship of their functional domains. J. Bacteriol. 175 (1993) 6067-6074
    • (1993) J. Bacteriol. , vol.175 , pp. 6067-6074
    • Morett, E.1    Segovia, L.2
  • 123
    • 0036830121 scopus 로고    scopus 로고
    • New roles for conserved regions within a sigma 54-dependent enhancer-binding protein
    • Lew C.M., and Gralla J.D. New roles for conserved regions within a sigma 54-dependent enhancer-binding protein. J. Biol. Chem. 277 (2002) 41517-41524
    • (2002) J. Biol. Chem. , vol.277 , pp. 41517-41524
    • Lew, C.M.1    Gralla, J.D.2
  • 124
    • 0037418230 scopus 로고    scopus 로고
    • The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: Identifying a surface that binds sigma 54
    • Bordes P., Wigneshweraraj S.R., Schumacher J., Zhang X., Chaney M., and Buck M. The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: Identifying a surface that binds sigma 54. Proc. Natl. Acad. Sci. USA 100 (2003) 2278-2283
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2278-2283
    • Bordes, P.1    Wigneshweraraj, S.R.2    Schumacher, J.3    Zhang, X.4    Chaney, M.5    Buck, M.6
  • 125
    • 0028839628 scopus 로고
    • Protein crosslinking studies suggest that Rhizobium meliloti C4-dicarboxylic acid transport protein D, a sigma 54-dependent transcriptional activator, interacts with sigma 54 and the beta subunit of RNA polymerase
    • Lee J.H., and Hoover T.R. Protein crosslinking studies suggest that Rhizobium meliloti C4-dicarboxylic acid transport protein D, a sigma 54-dependent transcriptional activator, interacts with sigma 54 and the beta subunit of RNA polymerase. Proc. Natl. Acad. Sci. USA 92 (1995) 9702-9706
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9702-9706
    • Lee, J.H.1    Hoover, T.R.2
  • 126
    • 0030609128 scopus 로고    scopus 로고
    • A conserved region in the sigma54-dependent activator DctD is involved in both binding to RNA polymerase and coupling ATP hydrolysis to activation
    • Wang Y.K., Lee J.H., Brewer J.M., and Hoover T.R. A conserved region in the sigma54-dependent activator DctD is involved in both binding to RNA polymerase and coupling ATP hydrolysis to activation. Mol. Microbiol. 26 (1997) 373-386
    • (1997) Mol. Microbiol. , vol.26 , pp. 373-386
    • Wang, Y.K.1    Lee, J.H.2    Brewer, J.M.3    Hoover, T.R.4
  • 127
    • 0025740385 scopus 로고
    • TyrR protein of Escherichia coli and its role as repressor and activator
    • Pittard A.J., and Davidson B.E. TyrR protein of Escherichia coli and its role as repressor and activator. Mol. Microbiol. 5 (1991) 1585-1592
    • (1991) Mol. Microbiol. , vol.5 , pp. 1585-1592
    • Pittard, A.J.1    Davidson, B.E.2
  • 128
    • 0041355268 scopus 로고    scopus 로고
    • RNA polymerase subunit requirements for activation by the enhancer-binding protein Rhodobacter capsulatus NtrC
    • Richard C.L., Tandon A., Sloan N.R., and Kranz R.G. RNA polymerase subunit requirements for activation by the enhancer-binding protein Rhodobacter capsulatus NtrC. J. Biol. Chem. 278 (2003) 31701-31708
    • (2003) J. Biol. Chem. , vol.278 , pp. 31701-31708
    • Richard, C.L.1    Tandon, A.2    Sloan, N.R.3    Kranz, R.G.4
  • 130
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami K.S., Masuda S., Campbell E.A., Muzzin O., and Darst S.A. Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex. Science 296 (2002) 1285-1290
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5
  • 134
    • 0344413496 scopus 로고    scopus 로고
    • The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination
    • Toulokhonov I., and Landick R. The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination. Mol. Cell 12 (2003) 1125-1136
    • (2003) Mol. Cell , vol.12 , pp. 1125-1136
    • Toulokhonov, I.1    Landick, R.2
  • 135
    • 0031456021 scopus 로고    scopus 로고
    • A mutant RNA polymerase that forms unusual open promoter complexes
    • Severinov K., and Darst S.A. A mutant RNA polymerase that forms unusual open promoter complexes. Proc. Natl. Acad. Sci. USA 94 (1997) 13481-13486
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13481-13486
    • Severinov, K.1    Darst, S.A.2
  • 136
    • 0034682813 scopus 로고    scopus 로고
    • Dissection of two hallmarks of the open promoter complex by mutation in an RNA polymerase core subunit
    • Nechaev S., Chlenov M., and Severinov K. Dissection of two hallmarks of the open promoter complex by mutation in an RNA polymerase core subunit. J. Biol. Chem. 275 (2000) 25516-25522
    • (2000) J. Biol. Chem. , vol.275 , pp. 25516-25522
    • Nechaev, S.1    Chlenov, M.2    Severinov, K.3
  • 138
    • 0037020252 scopus 로고    scopus 로고
    • The downstream DNA jaw of bacterial RNA polymerase facilitates both transcriptional initiation and pausing
    • Ederth J., Artsimovitch I., Isaksson L.A., and Landick R. The downstream DNA jaw of bacterial RNA polymerase facilitates both transcriptional initiation and pausing. J. Biol. Chem. 277 (2002) 37456-37463
    • (2002) J. Biol. Chem. , vol.277 , pp. 37456-37463
    • Ederth, J.1    Artsimovitch, I.2    Isaksson, L.A.3    Landick, R.4
  • 139
    • 0033022148 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli RNA polymerase by bacteriophage T7 gene 2 protein
    • Nechaev S., and Severinov K. Inhibition of Escherichia coli RNA polymerase by bacteriophage T7 gene 2 protein. J. Mol. Biol. 289 (1999) 815-826
    • (1999) J. Mol. Biol. , vol.289 , pp. 815-826
    • Nechaev, S.1    Severinov, K.2
  • 140
    • 0036300776 scopus 로고    scopus 로고
    • Beta subunit residues 186-433 and 436-445 are commonly used by Esigma54 and Esigma70 RNA polymerase for open promoter complex formation
    • Wigneshweraraj S.R., Nechaev S., Severinov K., and Buck M. Beta subunit residues 186-433 and 436-445 are commonly used by Esigma54 and Esigma70 RNA polymerase for open promoter complex formation. J. Mol. Biol. 319 (2002) 1067-1083
    • (2002) J. Mol. Biol. , vol.319 , pp. 1067-1083
    • Wigneshweraraj, S.R.1    Nechaev, S.2    Severinov, K.3    Buck, M.4
  • 141
    • 9144244886 scopus 로고    scopus 로고
    • Regulated communication between the upstream face of RNA polymerase and the beta' subunit jaw domain
    • Wigneshweraraj S.R., Burrows P.C., Necheav S., Zenkin N., Severinov K., and Buck M. Regulated communication between the upstream face of RNA polymerase and the beta' subunit jaw domain. EMBO J 23 (2004) 4264-4274
    • (2004) EMBO J , vol.23 , pp. 4264-4274
    • Wigneshweraraj, S.R.1    Burrows, P.C.2    Necheav, S.3    Zenkin, N.4    Severinov, K.5    Buck, M.6
  • 142
    • 33645871158 scopus 로고    scopus 로고
    • Wigneshweraraj, S. R., Burrows, P. C., Zakeyeva, I., Severinov, K., and Buck, M. In press. Contribution of the beta' Jaw domain to sigma54-RNA polymerase dependent transcription.
  • 143
    • 0242693109 scopus 로고    scopus 로고
    • Bacteriophage-induced modifications of host RNA polymerase
    • Nechaev S., and Severinov K. Bacteriophage-induced modifications of host RNA polymerase. Annu. Rev. Microbiol. 57 (2003) 301-322
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 301-322
    • Nechaev, S.1    Severinov, K.2
  • 144
    • 0029166594 scopus 로고
    • The bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation
    • Wedel A., and Kustu S. The bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation. Genes Dev. 9 (1995) 2042-2052
    • (1995) Genes Dev. , vol.9 , pp. 2042-2052
    • Wedel, A.1    Kustu, S.2
  • 145
    • 4344602493 scopus 로고    scopus 로고
    • Nucleotide-dependent interactions between a fork junction-RNA polymerase complex and an AAA+ transcriptional activator protein
    • Cannon W.V., Schumacher J., and Buck M. Nucleotide-dependent interactions between a fork junction-RNA polymerase complex and an AAA+ transcriptional activator protein. Nucleic Acids Res. 32 (2004) 4596-4608
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4596-4608
    • Cannon, W.V.1    Schumacher, J.2    Buck, M.3
  • 147
    • 0032897503 scopus 로고    scopus 로고
    • Involvement of the FtsH (HflB) protease in the activity of sigma 54 promoters
    • Carmona M., and de Lorenzo V. Involvement of the FtsH (HflB) protease in the activity of sigma 54 promoters. Mol. Microbiol. 31 (1999) 261-270
    • (1999) Mol. Microbiol. , vol.31 , pp. 261-270
    • Carmona, M.1    de Lorenzo, V.2
  • 148
    • 33645895752 scopus 로고    scopus 로고
    • Shingler, V., personal communication.
  • 149
    • 0037155137 scopus 로고    scopus 로고
    • Transcriptional activation of a heat-shock gene, lonD, of Myxococcus xanthus by a two component histidine-aspartate phosphorelay system
    • Ueki T., and Inouye S. Transcriptional activation of a heat-shock gene, lonD, of Myxococcus xanthus by a two component histidine-aspartate phosphorelay system. J. Biol. Chem. 277 (2002) 6170-6177
    • (2002) J. Biol. Chem. , vol.277 , pp. 6170-6177
    • Ueki, T.1    Inouye, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.