메뉴 건너뛰기




Volumn 324, Issue 1, 2002, Pages 17-34

Protein-protein and protein-DNA interactions of σ70 region 4 involved in transcription activation by λcI

Author keywords

E. coli RNA polymerase; Lambda cI; Sigma 70; Thermus aquaticus; Transcription activation

Indexed keywords

BACTERIAL PROTEIN; PROTEIN LAMBDA CI; PROTEIN SIGMA 70; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 0036435823     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01043-4     Document Type: Article
Times cited : (64)

References (45)
  • 2
    • 0026612797 scopus 로고
    • 70 family - Sequence conservation and evolutionary relationships
    • 70 family - Sequence conservation and evolutionary relationships. J. Bacteriol. 174, 3843-3849.
    • (1992) J. Bacteriol. , vol.174 , pp. 3843-3849
    • Lonetto, M.1    Gribskov, M.2    Gross, C.A.3
  • 4
    • 0036203066 scopus 로고    scopus 로고
    • Structure of the bacterial RNA polymerase promoter specificity σ subunit
    • Campbell, E. A., Muzzin, O., Chlenov, M., Sun, J. L., Olson, C. A., Weinman, O. et al. (2002). Structure of the bacterial RNA polymerase promoter specificity σ subunit. Mol. Cell, 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
    • 0018868527 scopus 로고
    • R) of bacteriophage lambda. III. Lambda repressor directly activates gene transcription
    • R) of bacteriophage lambda. III. Lambda repressor directly activates gene transcription. J. Mol. Biol. 139, 195-205.
    • (1980) J. Mol. Biol. , vol.139 , pp. 195-205
    • Meyer, B.J.1    Ptashne, M.2
  • 7
    • 0019977222 scopus 로고
    • The operator-binding domain of λ repressor: Structure and DNA recognition
    • Pabo, C. O. & Lewis, M. (1982). The operator-binding domain of λ repressor: Structure and DNA recognition. Nature, 298, 443-447.
    • (1982) Nature , vol.298 , pp. 443-447
    • Pabo, C.O.1    Lewis, M.2
  • 8
    • 0024462398 scopus 로고
    • A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor
    • Bushman, F. D., Shang, C. & Ptashne, M. (1989). A single glutamic acid residue plays a key role in the transcriptional activation function of lambda repressor. Cell, 58, 1163-1171.
    • (1989) Cell , vol.58 , pp. 1163-1171
    • Bushman, F.D.1    Shang, C.2    Ptashne, M.3
  • 9
    • 0020713848 scopus 로고
    • Repressor structure and the mechanism of positive control
    • Hochschild, A., Irwin, N. & Ptashne, M. (1983). Repressor structure and the mechanism of positive control. Cell, 32, 319-325.
    • (1983) Cell , vol.32 , pp. 319-325
    • Hochschild, A.1    Irwin, N.2    Ptashne, M.3
  • 10
    • 0028287795 scopus 로고
    • 70 that result in defects in phage λ repressor-stimulated transcription
    • 70 that result in defects in phage λ repressor-stimulated transcription. J. Bacteriol. 176, 2991-2998.
    • (1994) J. Bacteriol. , vol.176 , pp. 2991-2998
    • Kuldell, N.1    Hochschild, A.2
  • 11
    • 0028197624 scopus 로고
    • Target of the transcriptional activation function of phage λ cI protein
    • Li, M., Moyle, H. & Susskind, M. M. (1994). Target of the transcriptional activation function of phage λ cI protein. Science, 263, 75-77.
    • (1994) Science , vol.263 , pp. 75-77
    • Li, M.1    Moyle, H.2    Susskind, M.M.3
  • 12
    • 0034700165 scopus 로고    scopus 로고
    • Mechanism for a transcriptional activator that works at the isomerization step
    • Dove, S. L., Huang, F. W. & Hochschild, A. (2000). Mechanism for a transcriptional activator that works at the isomerization step. Proc. Natl. Acad. Sci. USA, 97, 13215-13220.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13215-13220
    • Dove, S.L.1    Huang, F.W.2    Hochschild, A.3
  • 13
    • 0024355282 scopus 로고
    • 70 subunit of RNA polymerase with altered promoter specificity
    • 70 subunit of RNA polymerase with altered promoter specificity. J. Mol. Biol. 206, 579-590.
    • (1989) J. Mol. Biol. , vol.206 , pp. 579-590
    • Gardella, T.1    Moyle, H.2    Susskind, M.M.3
  • 14
    • 0032032533 scopus 로고    scopus 로고
    • Conversion of the ω subunit of Escherichia coli RNA polymerase into a transcriptional activator or an activation target
    • Dove, S. L. & Hochschild, A. (1998). Conversion of the ω subunit of Escherichia coli RNA polymerase into a transcriptional activator or an activation target. Genes Dev. 12, 745-754.
    • (1998) Genes Dev. , vol.12 , pp. 745-754
    • Dove, S.L.1    Hochschild, A.2
  • 15
    • 0030907304 scopus 로고    scopus 로고
    • Activation of prokaryotic transcription through arbitrary protein-protein contacts
    • Dove, S. L., Joung, J. K. & Hochschild, A. (1997). Activation of prokaryotic transcription through arbitrary protein-protein contacts. Nature, 386, 627-630.
    • (1997) Nature , vol.386 , pp. 627-630
    • Dove, S.L.1    Joung, J.K.2    Hochschild, A.3
  • 17
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby, S. & Ebright, R. H. (1999). Transcription activation by catabolite activator protein (CAP). J. Mol. Biol. 293, 199-213.
    • (1999) J. Mol. Biol. , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 19
    • 0026657433 scopus 로고
    • Refined 1.8 Å crystal structure of the λ repressor-operator complex
    • Beamer, L. J. & Pabo, C. O. (1992). Refined 1.8 Å crystal structure of the λ repressor-operator complex. J. Mol. Biol. 227, 177-196.
    • (1992) J. Mol. Biol. , vol.227 , pp. 177-196
    • Beamer, L.J.1    Pabo, C.O.2
  • 20
    • 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. & Darst, S. A. (2002). Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex. Science, 296, 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
  • 21
    • 0018817388 scopus 로고
    • R3: Their roles in mediating the effects of repressor and cro
    • R3: Their roles in mediating the effects of repressor and cro. J. Mol. Biol. 139, 163-194.
    • (1980) J. Mol. Biol. , vol.139 , pp. 163-194
    • Meyer, B.J.1    Maurer, R.2    Ptashne, M.3
  • 22
    • 0031046671 scopus 로고    scopus 로고
    • The activation defect of a λcI positive control mutant
    • Whipple, F. W., Ptashne, M. & Hochschild, A. (1997). The activation defect of a λcI positive control mutant. J. Mol. Biol. 265, 261-265.
    • (1997) J. Mol. Biol. , vol.265 , pp. 261-265
    • Whipple, F.W.1    Ptashne, M.2    Hochschild, A.3
  • 23
    • 0031015563 scopus 로고    scopus 로고
    • Molecular anatomy of a transcription activation patch: FIS-RNA polymerase interactions at the Escherichia coli rrnB P1 promoter
    • Bokal, A. J., Ross, W., Gaal, T., Johnson, R. C. & Gourse, R. L. (1997). Molecular anatomy of a transcription activation patch: FIS-RNA polymerase interactions at the Escherichia coli rrnB P1 promoter. EMBO J. 16, 154-162.
    • (1997) EMBO J. , vol.16 , pp. 154-162
    • Bokal, A.J.1    Ross, W.2    Gaal, T.3    Johnson, R.C.4    Gourse, R.L.5
  • 24
    • 0033901463 scopus 로고    scopus 로고
    • Genetic evidence that transcription activation by RhaS involves specific amino acid contacts with sigma 70
    • Bhende, P. M. & Egan, S. M. (2000). Genetic evidence that transcription activation by RhaS involves specific amino acid contacts with sigma 70. J. Bacteriol. 182, 4959-4969.
    • (2000) J. Bacteriol. , vol.182 , pp. 4959-4969
    • Bhende, P.M.1    Egan, S.M.2
  • 25
    • 0033058086 scopus 로고    scopus 로고
    • 70 subunit of RNA polymerase according to promoter architecture: Identification of the target of Ada activation at the alkA promoter
    • Landini, P. & Busby, S. J. W. (1999). The Escherichia coli Ada protein can interact with two distinct determinants in the s(70)subunit of RNA polymerase according to promoter architecture: Identification of the target of Ada activation at the alkA promoter. J. Bacteriol. 181, 1524-1529.
    • (1999) J. Bacteriol. , vol.181 , pp. 1524-1529
    • Landini, P.1    Busby, S.J.W.2
  • 26
    • 0032699605 scopus 로고    scopus 로고
    • 70 subunits participate in transcription of the Escherichia coli uhpT promoter
    • 70 subunits participate in transcription of the Escherichia coli uhpT promoter. J. Bacteriol. 181, 7266-7273.
    • (1999) J. Bacteriol. , vol.181 , pp. 7266-7273
    • Olekhnovich, I.N.1    Kadner, R.J.2
  • 27
    • 0034595498 scopus 로고    scopus 로고
    • 70 subunit: Application of suppression genetics
    • 70 subunit: Application of suppression genetics. J. Mol. Biol. 299, 311-324.
    • (2000) J. Mol. Biol. , vol.299 , pp. 311-324
    • Rhodius, V.A.1    Busby, S.J.W.2
  • 28
    • 0030595337 scopus 로고    scopus 로고
    • Structural classification of HTH DNA-binding domains and protein-DNA interaction modes
    • Wintjens, R. & Rooman, M. (1996). Structural classification of HTH DNA-binding domains and protein-DNA interaction modes. J. Mol. Biol. 262, 294-313.
    • (1996) J. Mol. Biol. , vol.262 , pp. 294-313
    • Wintjens, R.1    Rooman, M.2
  • 30
    • 0035688875 scopus 로고    scopus 로고
    • 70 subunit of RNA polymerase and the transcriptional regulators Rsd from Escherichia coli and AlgQ from Pseudomonas aeruginosa
    • 70 subunit of RNA polymerase and the transcriptional regulators Rsd from Escherichia coli and AlgQ from Pseudomonas aeruginosa. J. Bacteriol. 183, 6413-6421.
    • (2001) J. Bacteriol. , vol.183 , pp. 6413-6421
    • Dove, S.L.1    Hochschild, A.2
  • 31
    • 0036469062 scopus 로고    scopus 로고
    • A role for interaction of the RNA polymerase flap domain with the sigma subunit in promoter recognition
    • Kuznedelov, K., Minakhin, L., Niedziela-Majka, A., Dove, S. L., Rogulja, D., Nickels, B. E. et al. (2002). A role for interaction of the RNA polymerase flap domain with the sigma subunit in promoter recognition. Science, 295, 855-857.
    • (2002) Science , vol.295 , pp. 855-857
    • Kuznedelov, K.1    Minakhin, L.2    Niedziela-Majka, A.3    Dove, S.L.4    Rogulja, D.5    Nickels, B.E.6
  • 35
    • 0032529668 scopus 로고    scopus 로고
    • Genetic analysis of prokaryotic and eukaryotic DNA-binding proteins in Escherichia coli
    • Whipple, F. W. (1998). Genetic analysis of prokaryotic and eukaryotic DNA-binding proteins in Escherichia coli. Nucl. Acids Res. 26, 3700-3706.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 3700-3706
    • Whipple, F.W.1
  • 36
    • 0028051844 scopus 로고
    • Synergistic activation of transcription by bacteriophage λ cI protein and E. coli cAMP receptor protein
    • Joung, J. K., Koepp, D. M. & Hochschild, A. (1994). Synergistic activation of transcription by bacteriophage λ cI protein and E. coli cAMP receptor protein. Science, 265, 1863-1866.
    • (1994) Science , vol.265 , pp. 1863-1866
    • Joung, J.K.1    Koepp, D.M.2    Hochschild, A.3
  • 37
    • 0030796260 scopus 로고    scopus 로고
    • Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: Application to open reading frame characterization
    • Link, A. J., Phillips, D. & Church, G. M. (1997). Methods for generating precise deletions and insertions in the genome of wild-type Escherichia coli: Application to open reading frame characterization. J. Bacteriol. 179, 6228-6237.
    • (1997) J. Bacteriol. , vol.179 , pp. 6228-6237
    • Link, A.J.1    Phillips, D.2    Church, G.M.3
  • 38
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (1972). Experiments in Molecular Genetics, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 41
    • 0035827332 scopus 로고    scopus 로고
    • Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution
    • Gnatt, A. L., Cramer, P., Fu, J., Bushnell, D. A. & Kornberg, R. D. (2001). Structural basis of transcription: An RNA polymerase II elongation complex at 3.3 Å resolution. Science, 292, 1876-1882.
    • (2001) Science , vol.292 , pp. 1876-1882
    • Gnatt, A.L.1    Cramer, P.2    Fu, J.3    Bushnell, D.A.4    Kornberg, R.D.5
  • 42
    • 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. (1997). Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement. Proc. Natl. Acad. Sci. USA, 94, 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
  • 43
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: T. aquaticus RNA polymerase holoenzyme at 4 Å resolution
    • Murakami, K. S., Masuda, S. & Darst, S. A. (2002). Structural basis of transcription initiation: T. aquaticus RNA polymerase holoenzyme at 4 Å resolution. Science, 296, 1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 44
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.