메뉴 건너뛰기




Volumn 25, Issue 9, 2000, Pages 408-414

Protein-protein interactions mapped by artificial proteases: Where σ factors bind to RNA polymerase

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; PROTEINASE; RNA POLYMERASE; SIGMA FACTOR;

EID: 0034284365     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01652-2     Document Type: Review
Times cited : (43)

References (44)
  • 1
    • 0027442911 scopus 로고
    • Cross-linking of Escherichia coli RNA polymerase subunits: Identification of β' as the binding site of ω
    • 1 Gentry, D.R. and Burgess, R.R. (1993) Cross-linking of Escherichia coli RNA polymerase subunits: identification of β' as the binding site of ω. Biochemistry 32, 11224-11227
    • (1993) Biochemistry , vol.32 , pp. 11224-11227
    • Gentry, D.R.1    Burgess, R.R.2
  • 2
    • 0033083036 scopus 로고    scopus 로고
    • Core RNA polymerase from E. coli induces a major change in the domain arrangement of the σ70 subunit
    • 2 Callaci, S. et al. (1999) Core RNA polymerase from E. coli induces a major change in the domain arrangement of the σ70 subunit. Mol. Cell 3, 229-238
    • (1999) Mol. Cell , vol.3 , pp. 229-238
    • Callaci, S.1
  • 3
    • 0032735991 scopus 로고    scopus 로고
    • The interface of σ with core RNA polymerase is extensive, conserved, and functionally specialized
    • 3 Sharp, M.M. et al. (1999) The interface of σ with core RNA polymerase is extensive, conserved, and functionally specialized. Genes Dev. 13, 3015-3026
    • (1999) Genes Dev. , vol.13 , pp. 3015-3026
    • Sharp, M.M.1
  • 4
    • 0032545186 scopus 로고    scopus 로고
    • Identification of a contact site for different transcription activators in region 4 of the Escherichia coli RNA polymerase σ70 subunit
    • 4 Lonetto, M.A. et al. (1998) Identification of a contact site for different transcription activators in region 4 of the Escherichia coli RNA polymerase σ70 subunit. J. Mol. Biol. 284, 1353-1365
    • (1998) J. Mol. Biol. , vol.284 , pp. 1353-1365
    • Lonetto, M.A.1
  • 5
    • 0032719343 scopus 로고    scopus 로고
    • Genetic analysis of nif regulatory genes by utilizing the yeast two-hybrid system detected formation of a NifL-NifA complex that is implicated in regulated expression of nif genes
    • 5 Lei, S. et al. (1999) Genetic analysis of nif regulatory genes by utilizing the yeast two-hybrid system detected formation of a NifL-NifA complex that is implicated in regulated expression of nif genes. J. Bacteriol. 181, 6535-6539
    • (1999) J. Bacteriol. , vol.181 , pp. 6535-6539
    • Lei, S.1
  • 6
    • 0025208245 scopus 로고
    • Specific cleavage of a protein by an attached iron chelate
    • 6 Rana, T.M. and Meares, C.F. (1990) Specific cleavage of a protein by an attached iron chelate. J. Am. Chem. Soc. 112, 2457-2458
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2457-2458
    • Rana, T.M.1    Meares, C.F.2
  • 7
    • 0025074680 scopus 로고
    • Site-specific cleavage of the protein calmodulin using a trifluoperazine-based affinity reagent
    • 7 Schepartz, A. and Cuenoud, B. (1990) Site-specific cleavage of the protein calmodulin using a trifluoperazine-based affinity reagent. J. Am. Chem. Soc. 112, 3247-3249
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3247-3249
    • Schepartz, A.1    Cuenoud, B.2
  • 8
    • 0025042473 scopus 로고
    • A new strategy for selective protein cleavage
    • 8 Hoyer, D. et al. (1990) A new strategy for selective protein cleavage. J. Am. Chem. Soc. 112, 3249-3250
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3249-3250
    • Hoyer, D.1
  • 9
    • 0029115087 scopus 로고
    • Proximity mapping the surface of a membrane protein using an artificial protease: Demonstration that the quinone-binding domain of subunit I is near the N-terminal region of subunit II of cytochrome bd
    • 9 Ghaim, J.B. et al. (1995) Proximity mapping the surface of a membrane protein using an artificial protease: demonstration that the quinone-binding domain of subunit I is near the N-terminal region of subunit II of cytochrome bd. Biochemistry 34, 11311-11315
    • (1995) Biochemistry , vol.34 , pp. 11311-11315
    • Ghaim, J.B.1
  • 10
    • 0026489715 scopus 로고
    • Incorporation of an EDTA-metal complex at a rationally selected site within a protein: Application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro
    • 10 Ebright, Y.W. et al. (1992) Incorporation of an EDTA-metal complex at a rationally selected site within a protein: application to EDTA-iron DNA affinity cleaving with catabolite gene activator protein (CAP) and Cro. Biochemistry 31, 10664-10670
    • (1992) Biochemistry , vol.31 , pp. 10664-10670
    • Ebright, Y.W.1
  • 11
    • 0032568456 scopus 로고    scopus 로고
    • Mapping the σ70 subunit contact sites on Escherichia coli RNA polymerase with a σ70-conjugated chemical protease
    • 11 Owens, J.T. et al. (1998) Mapping the σ70 subunit contact sites on Escherichia coli RNA polymerase with a σ70-conjugated chemical protease. Proc. Natl. Acad. Sci. U. S. A. 95, 6021-6026
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6021-6026
    • Owens, J.T.1
  • 12
    • 0032568637 scopus 로고    scopus 로고
    • Mapping the promoter DNA sites proximal to conserved regions of σ70 in an Escherichia coli RNA polymerase-lacUV5 open promoter complex
    • 12 Owens, J.T. et al. (1998) Mapping the promoter DNA sites proximal to conserved regions of σ70 in an Escherichia coli RNA polymerase-lacUV5 open promoter complex. Biochemistry 37, 7670-7675
    • (1998) Biochemistry , vol.37 , pp. 7670-7675
    • Owens, J.T.1
  • 13
    • 0033528675 scopus 로고    scopus 로고
    • Mapping protein-protein interactions with a library of tethered cutting reagents: The binding site of σ70 on Escherichia coli RNA polymerase
    • 13 Traviglia, S.L. et al. (1999) Mapping protein-protein interactions with a library of tethered cutting reagents: the binding site of σ70 on Escherichia coli RNA polymerase. Biochemistry 38, 4259-4265
    • (1999) Biochemistry , vol.38 , pp. 4259-4265
    • Traviglia, S.L.1
  • 14
    • 0033619725 scopus 로고    scopus 로고
    • Targeted protein footprinting: Where different transcription factors bind to RNA polymerase
    • 14 Traviglia, S.L. et al. (1999) Targeted protein footprinting: where different transcription factors bind to RNA polymerase. Biochemistry 38, 15774-15778
    • (1999) Biochemistry , vol.38 , pp. 15774-15778
    • Traviglia, S.L.1
  • 15
    • 0018199224 scopus 로고
    • DNAse footprinting: A simple method for the detection of protein-DNA binding specificity
    • 15 Galas, D.J. and Schmitz, A. (1978) DNAse footprinting: a simple method for the detection of protein-DNA binding specificity. Nucleic Acids Res. 5, 3157-3170
    • (1978) Nucleic Acids Res. , vol.5 , pp. 3157-3170
    • Galas, D.J.1    Schmitz, A.2
  • 16
    • 0026334831 scopus 로고
    • Characterization of protein-DNA complexes by affinity cleaving
    • 16 Dervan, P.B. (1991) Characterization of protein-DNA complexes by affinity cleaving. Methods Enzymol. 208, 497-515
    • (1991) Methods Enzymol. , vol.208 , pp. 497-515
    • Dervan, P.B.1
  • 17
    • 0023623752 scopus 로고
    • Hydroxyl radical footprinting: A high-resolution method for mapping protein-DNA contacts
    • 17 Tullius, T.D. et al. (1987) Hydroxyl radical footprinting: a high-resolution method for mapping protein-DNA contacts. Methods Enzymol. 155, 537-558
    • (1987) Methods Enzymol. , vol.155 , pp. 537-558
    • Tullius, T.D.1
  • 18
    • 0032562135 scopus 로고    scopus 로고
    • Protease activity of 1,10-phenanthroline-copper(I). Targeted scission of the catalytic site of carbonic anhydrase
    • 18 Gallagher, J. et al. (1998) Protease activity of 1,10-phenanthroline-copper(I). Targeted scission of the catalytic site of carbonic anhydrase. Biochemistry 37, 2096-2104
    • (1998) Biochemistry , vol.37 , pp. 2096-2104
    • Gallagher, J.1
  • 19
    • 0026766292 scopus 로고
    • Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelate
    • 19 Ermácora, M.R. et al. (1992) Conformation-dependent cleavage of staphylococcal nuclease with a disulfide-linked iron chelate. Proc. Natl. Acad. Sci. U. S. A. 89, 6383-6387
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6383-6387
    • Ermácora, M.R.1
  • 20
    • 0027931824 scopus 로고
    • Mapping protein domains involved in macromolecular interactions: A novel protein footprinting approach
    • 20 Heyduk, E. and Heyduk, T. (1994) Mapping protein domains involved in macromolecular interactions: a novel protein footprinting approach. Biochemistry 33, 9643-9650
    • (1994) Biochemistry , vol.33 , pp. 9643-9650
    • Heyduk, E.1    Heyduk, T.2
  • 21
    • 0029664584 scopus 로고    scopus 로고
    • Binding of the σ70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting
    • 21 Greiner, D.P. et al. (1996) Binding of the σ70 protein to the core subunits of Escherichia coli RNA polymerase, studied by iron-EDTA protein footprinting. Proc. Natl. Acad. Sci. U. S. A. 93, 71-75
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 71-75
    • Greiner, D.P.1
  • 22
    • 0031056514 scopus 로고    scopus 로고
    • Synthesis of the protein cutting reagent iron (S-1-(p-bromoacetamidobenzyl ethylenediaminetetraacetate and conjugation to cysteine side chains
    • 22 Greiner, D.P. et al. (1997) Synthesis of the protein cutting reagent iron (S)-1-(p-bromoacetamidobenzyl) ethylenediaminetetraacetate and conjugation to cysteine side chains. Bioconjugate Chem. 8, 44-48
    • (1997) Bioconjugate Chem. , vol.8 , pp. 44-48
    • Greiner, D.P.1
  • 23
    • 0025718819 scopus 로고
    • Transfer of oxygen from an artificial protease to peptide carbon during proteolysis
    • 23 Rana, T.M. and Meares, C.F. (1991) Transfer of oxygen from an artificial protease to peptide carbon during proteolysis. Prac. Natl. Acad. Sci. U. S. A. 88, 10578-10582
    • (1991) Prac. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10578-10582
    • Rana, T.M.1    Meares, C.F.2
  • 24
    • 0027146667 scopus 로고
    • Oxidative polypeptide cleavage mediated by EDTA-Fe covalently linked to cysteine residues
    • 24 Platis, I.E. et al. (1993) Oxidative polypeptide cleavage mediated by EDTA-Fe covalently linked to cysteine residues. Biochemistry 32, 12761-12767
    • (1993) Biochemistry , vol.32 , pp. 12761-12767
    • Platis, I.E.1
  • 25
    • 0023186275 scopus 로고
    • Chemical conversion of a DNA-binding protein into a site-specific nuclease
    • 25 Chen, C.H. and Sigman, D.S. (1987) Chemical conversion of a DNA-binding protein into a site-specific nuclease. Science 237, 1197-1201
    • (1987) Science , vol.237 , pp. 1197-1201
    • Chen, C.H.1    Sigman, D.S.2
  • 26
    • 0030928287 scopus 로고    scopus 로고
    • Repressor induced site-specific binding of HU for transcriptional regulation
    • 26 Aki, T. and Adhya, S. (1997) Repressor induced site-specific binding of HU for transcriptional regulation. EMBO J. 16, 3666-3674
    • (1997) Embo J. , vol.16 , pp. 3666-3674
    • Aki, T.1    Adhya, S.2
  • 27
    • 0025739871 scopus 로고
    • RNA polymerase II
    • 27 Young, R. (1991) RNA polymerase II. Annu. Rev. Biochem. 60, 689-715
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 689-715
    • Young, R.1
  • 28
    • 0001796834 scopus 로고
    • RNA polymerase - An overview
    • (Losick, R. and Chamberlin, M., eds), Cold Spring Harbor Laboratory Press
    • 28 Chamberlin, M. (1976) RNA polymerase - an overview. In RNA Polymerase (Losick, R. and Chamberlin, M., eds), pp. 17-67, Cold Spring Harbor Laboratory Press
    • (1976) Rna Polymerase , pp. 17-67
    • Chamberlin, M.1
  • 29
    • 0002625988 scopus 로고    scopus 로고
    • Promoter selectivity control of RNA polymerase
    • (Eckstein, F. and Lilley, D.M.J., eds), Springer-Verlag
    • 29 Ishihama, A. (1997) Promoter selectivity control of RNA polymerase. In Nucleic Acids and Molecular Biology (Vol. 11) (Eckstein, F. and Lilley, D.M.J., eds), pp. 53-70, Springer-Verlag
    • (1997) Nucleic Acids and Molecular Biology , vol.11 , pp. 53-70
    • Ishihama, A.1
  • 30
    • 0025744584 scopus 로고
    • Escherichia coli σ70 and NusA proteins, I. Binding interactions with core RNA polymerase in solution and within the transcription complex
    • 30 Gill, S.C. et al. (1991) Escherichia coli σ70 and NusA proteins, I. Binding interactions with core RNA polymerase in solution and within the transcription complex. J. Mol. Biol. 220, 307-324
    • (1991) J. Mol. Biol. , vol.220 , pp. 307-324
    • Gill, S.C.1
  • 31
    • 0017399651 scopus 로고
    • Subunit topography of RNA polymerase from Escherichia coli. A cross-linking study with bifunctional reagents
    • 31 Hillel, Z. and Wu, C.W. (1977) Subunit topography of RNA polymerase from Escherichia coli. A cross-linking study with bifunctional reagents. Biochemistry 16, 3334-3342
    • (1977) Biochemistry , vol.16 , pp. 3334-3342
    • Hillel, Z.1    Wu, C.W.2
  • 32
    • 0032553125 scopus 로고    scopus 로고
    • Localization of a σ70 binding site on the N terminus of the Escherichia coli RNA polymerase β' subunit
    • 32 Arthur, T.M. and Burgess, R.R. (1998) Localization of a σ70 binding site on the N terminus of the Escherichia coli RNA polymerase β' subunit. J. Biol. Chem. 273, 31381-31387
    • (1998) J. Biol. Chem. , vol.273 , pp. 31381-31387
    • Arthur, T.M.1    Burgess, R.R.2
  • 33
    • 0030271890 scopus 로고    scopus 로고
    • Crystal structure of a σ70 subunit fragment from E. coli RNA polymerase
    • 33 Malhotra, A. et al. (1996) Crystal structure of a σ70 subunit fragment from E. coli RNA polymerase. Cell 87, 127-136
    • (1996) Cell , vol.87 , pp. 127-136
    • Malhotra, A.1
  • 34
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • 34 Zhang, G. et al. (1999) Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell 98, 811-824
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1
  • 35
    • 0028875725 scopus 로고
    • Three-dimensional structure of E. coli core RNA polymerase: Promoter binding and elongation conformations of the enzyme
    • 35 Polyakov, A. et al. (1995) Three-dimensional structure of E. coli core RNA polymerase: promoter binding and elongation conformations of the enzyme. Cell 83, 365-373
    • (1995) Cell , vol.83 , pp. 365-373
    • Polyakov, A.1
  • 37
    • 0034625251 scopus 로고    scopus 로고
    • Structural organization of the RNA polymerase-promoter open complex
    • 37 Naryshkin, N. et al. (2000) Structural organization of the RNA polymerase-promoter open complex. Cell 101, 601-611
    • (2000) Cell , vol.101 , pp. 601-611
    • Naryshkin, N.1
  • 38
    • 0032450639 scopus 로고    scopus 로고
    • RNA polymerase-DNA interaction: Structures of intermediate, open, and elongation complexes
    • 38 Ebright, R.H. (1998) RNA polymerase-DNA interaction: structures of intermediate, open, and elongation complexes. Cold Spring Harbor Symp. Quant. Biol. 63, 11-20
    • (1998) Cold Spring Harbor Symp. Quant. Biol. , vol.63 , pp. 11-20
    • Ebright, R.H.1
  • 39
    • 18344418394 scopus 로고    scopus 로고
    • Protein-nucleic acid interactions during open complex formation investigated by systematic alteration of the protein and DNA binding partners
    • 39 Helmann, J.D. and deHaseth, P.L. (1999) Protein-nucleic acid interactions during open complex formation investigated by systematic alteration of the protein and DNA binding partners. Biochemistry 38, 5959-5967
    • (1999) Biochemistry , vol.38 , pp. 5959-5967
    • Helmann, J.D.1    DeHaseth, P.L.2
  • 40
    • 0022132080 scopus 로고
    • Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases
    • 40 Allison, L.A. et al. (1985) Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell 42, 599-610
    • (1985) Cell , vol.42 , pp. 599-610
    • Allison, L.A.1
  • 41
    • 0002191192 scopus 로고
    • Bacterial sigma factors
    • (Conaway, R.C. and Conaway, J.W., eds), Raven Press, New York, NY, USA
    • 41 Helmann, J.D. (1994) Bacterial sigma factors. In Transcription: Mechanisms and Regulation (Conaway, R.C. and Conaway, J.W., eds), pp. 1-17, Raven Press, New York, NY, USA
    • (1994) Transcription: Mechanisms and Regulation , pp. 1-17
    • Helmann, J.D.1
  • 42
    • 0034660249 scopus 로고    scopus 로고
    • Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes
    • 42 Wigneshweraraj, S.R. et al. (2000) Conservation of sigma-core RNA polymerase proximity relationships between the enhancer-independent and enhancer-dependent sigma classes. EMBO J. 19, 3038-3048
    • (2000) Embo J. , vol.19 , pp. 3038-3048
    • Wigneshweraraj, S.R.1
  • 43
    • 0032849011 scopus 로고    scopus 로고
    • Identification of an RNA-protein bridge spanning the ribosomal subunit interface
    • 43 Culver, G.M. et al. (1999) Identification of an RNA-protein bridge spanning the ribosomal subunit interface. Science 285, 2133-2136
    • (1999) Science , vol.285 , pp. 2133-2136
    • Culver, G.M.1
  • 44
    • 0032993062 scopus 로고    scopus 로고
    • Directed hydroxyl radical probing of 16S rRNA in the ribosome: Spatial proximity of RNA elements of the 3′ and 5′ domains
    • 44 Newcomb, L.F. and Noller, H.F. (1999) Directed hydroxyl radical probing of 16S rRNA in the ribosome: spatial proximity of RNA elements of the 3′ and 5′ domains. RNA 5, 849-855
    • (1999) Rna , vol.5 , pp. 849-855
    • Newcomb, L.F.1    Noller, H.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.