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Volumn 377, Issue 1, 2008, Pages 148-161

RecA-Dependent Cleavage of LexA Dimers

Author keywords

dimer; LexA; RecA; SOS; specific cleavage

Indexed keywords

LEXA PROTEIN; RECA PROTEIN;

EID: 39649098477     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.12.025     Document Type: Article
Times cited : (75)

References (53)
  • 1
    • 0020316054 scopus 로고
    • The SOS regulatory system of Escherichia coli
    • Little J.W., and Mount D.W. The SOS regulatory system of Escherichia coli. Cell 29 (1982) 11-22
    • (1982) Cell , vol.29 , pp. 11-22
    • Little, J.W.1    Mount, D.W.2
  • 2
    • 0018904882 scopus 로고
    • E. coli recA protein-directed cleavage of phage lambda repressor requires polynucleotide
    • Craig N.L., and Roberts J.W. E. coli recA protein-directed cleavage of phage lambda repressor requires polynucleotide. Nature 283 (1980) 26-30
    • (1980) Nature , vol.283 , pp. 26-30
    • Craig, N.L.1    Roberts, J.W.2
  • 3
    • 0343188817 scopus 로고
    • Autodigestion of lexA and phage lambda repressors
    • Little J.W. Autodigestion of lexA and phage lambda repressors. Proc. Natl Acad. Sci. USA 81 (1984) 1375-1379
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 1375-1379
    • Little, J.W.1
  • 4
    • 0025810994 scopus 로고
    • Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease
    • Little J.W. Mechanism of specific LexA cleavage: autodigestion and the role of RecA coprotease. Biochimie 73 (1991) 411-421
    • (1991) Biochimie , vol.73 , pp. 411-421
    • Little, J.W.1
  • 5
    • 0021886438 scopus 로고
    • Large-scale purification, oligomerization equilibria, and specific interaction of the LexA repressor of Escherichia coli
    • Schnarr M., Pouyet J., Granger-Schnarr M., and Daune M. Large-scale purification, oligomerization equilibria, and specific interaction of the LexA repressor of Escherichia coli. Biochemistry 24 (1985) 2812-2818
    • (1985) Biochemistry , vol.24 , pp. 2812-2818
    • Schnarr, M.1    Pouyet, J.2    Granger-Schnarr, M.3    Daune, M.4
  • 6
    • 0034681384 scopus 로고    scopus 로고
    • LexA repressor forms stable dimers in solution. The role of specific DNA in tightening protein-protein interactions
    • Mohana-Borges R., Pacheco A.B., Sousa F.J., Foguel D., Almeida D.F., and Silva J.L. LexA repressor forms stable dimers in solution. The role of specific DNA in tightening protein-protein interactions. J. Biol. Chem. 275 (2000) 4708-4712
    • (2000) J. Biol. Chem. , vol.275 , pp. 4708-4712
    • Mohana-Borges, R.1    Pacheco, A.B.2    Sousa, F.J.3    Foguel, D.4    Almeida, D.F.5    Silva, J.L.6
  • 7
    • 0025361131 scopus 로고
    • Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication
    • Sassanfar M., and Roberts J.W. Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication. J. Mol. Biol. 212 (1990) 79-96
    • (1990) J. Mol. Biol. , vol.212 , pp. 79-96
    • Sassanfar, M.1    Roberts, J.W.2
  • 8
    • 0035823008 scopus 로고    scopus 로고
    • Crystal structure of LexA: a conformational switch for regulation of self-cleavage
    • Luo Y., Pfuetzner R.A., Mosimann S., Paetzel M., Frey E.A., Cherney M., et al. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell 106 (2001) 585-594
    • (2001) Cell , vol.106 , pp. 585-594
    • Luo, Y.1    Pfuetzner, R.A.2    Mosimann, S.3    Paetzel, M.4    Frey, E.A.5    Cherney, M.6
  • 9
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 10
    • 0019847880 scopus 로고
    • Regulation of SOS functions: purification of E. coli LexA protein and determination of its specific site cleaved by the RecA protein
    • Horii T., Ogawa T., Nakatani T., Hase T., Matsubara H., and Ogawa H. Regulation of SOS functions: purification of E. coli LexA protein and determination of its specific site cleaved by the RecA protein. Cell 27 (1981) 515-522
    • (1981) Cell , vol.27 , pp. 515-522
    • Horii, T.1    Ogawa, T.2    Nakatani, T.3    Hase, T.4    Matsubara, H.5    Ogawa, H.6
  • 11
    • 0023186212 scopus 로고
    • Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism
    • Slilaty S.N., and Little J.W. Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. Proc. Natl Acad. Sci. USA 84 (1987) 3987-3991
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3987-3991
    • Slilaty, S.N.1    Little, J.W.2
  • 13
    • 0026620486 scopus 로고
    • In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage
    • Roland K.L., Smith M.H., Rupley J.A., and Little J.W. In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage. J. Mol. Biol. 228 (1992) 395-408
    • (1992) J. Mol. Biol. , vol.228 , pp. 395-408
    • Roland, K.L.1    Smith, M.H.2    Rupley, J.A.3    Little, J.W.4
  • 14
    • 0023883295 scopus 로고
    • -) mutants of the LexA repressor of Escherichia coli K-12
    • -) mutants of the LexA repressor of Escherichia coli K-12. J. Bacteriol. 170 (1988) 2163-2173
    • (1988) J. Bacteriol. , vol.170 , pp. 2163-2173
    • Lin, L.L.1    Little, J.W.2
  • 15
    • 0021919232 scopus 로고
    • Mutations in bacteriophage lambda repressor that prevent RecA-mediated cleavage
    • Gimble F.S., and Sauer R.T. Mutations in bacteriophage lambda repressor that prevent RecA-mediated cleavage. J. Bacteriol. 162 (1985) 147-154
    • (1985) J. Bacteriol. , vol.162 , pp. 147-154
    • Gimble, F.S.1    Sauer, R.T.2
  • 16
    • 0023042845 scopus 로고
    • - proteins in the autodigestion and RecA-mediated cleavage reactions
    • - proteins in the autodigestion and RecA-mediated cleavage reactions. J. Mol. Biol. 192 (1986) 39-47
    • (1986) J. Mol. Biol. , vol.192 , pp. 39-47
    • Gimble, F.S.1    Sauer, R.T.2
  • 17
    • 0023041678 scopus 로고
    • Intramolecular cleavage of LexA and phage lambda repressors: dependence of kinetics on repressor concentration, pH, temperature, and solvent
    • Slilaty S.N., Rupley J.A., and Little J.W. Intramolecular cleavage of LexA and phage lambda repressors: dependence of kinetics on repressor concentration, pH, temperature, and solvent. Biochemistry 25 (1986) 6866-6875
    • (1986) Biochemistry , vol.25 , pp. 6866-6875
    • Slilaty, S.N.1    Rupley, J.A.2    Little, J.W.3
  • 18
    • 0024121565 scopus 로고
    • UmuD mutagenesis protein of Escherichia coli: overproduction, purification, and cleavage by RecA
    • Burckhardt S.E., Woodgate R., Scheuermann R.H., and Echols H. UmuD mutagenesis protein of Escherichia coli: overproduction, purification, and cleavage by RecA. Proc. Natl Acad. Sci. USA 85 (1988) 1811-1815
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1811-1815
    • Burckhardt, S.E.1    Woodgate, R.2    Scheuermann, R.H.3    Echols, H.4
  • 20
    • 0034705320 scopus 로고    scopus 로고
    • Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding
    • Bell C.E., Frescura P., Hochschild A., and Lewis M. Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding. Cell 101 (2000) 801-811
    • (2000) Cell , vol.101 , pp. 801-811
    • Bell, C.E.1    Frescura, P.2    Hochschild, A.3    Lewis, M.4
  • 21
    • 33748103187 scopus 로고    scopus 로고
    • Structure of a hyper-cleavable monomeric fragment of phage lambda repressor containing the cleavage site region
    • Ndjonka D., and Bell C.E. Structure of a hyper-cleavable monomeric fragment of phage lambda repressor containing the cleavage site region. J. Mol. Biol. 362 (2006) 479-489
    • (2006) J. Mol. Biol. , vol.362 , pp. 479-489
    • Ndjonka, D.1    Bell, C.E.2
  • 22
    • 0024583633 scopus 로고
    • New recA mutations that dissociate the various RecA protein activities in Escherichia coli provide evidence for an additional role for RecA protein in UV mutagenesis
    • Dutreix M., Moreau P.L., Bailone A., Galibert F., Battista J.R., Walker G.C., and Devoret R. New recA mutations that dissociate the various RecA protein activities in Escherichia coli provide evidence for an additional role for RecA protein in UV mutagenesis. J. Bacteriol. 171 (1989) 2415-2423
    • (1989) J. Bacteriol. , vol.171 , pp. 2415-2423
    • Dutreix, M.1    Moreau, P.L.2    Bailone, A.3    Galibert, F.4    Battista, J.R.5    Walker, G.C.6    Devoret, R.7
  • 23
    • 0032548822 scopus 로고    scopus 로고
    • Differential cleavage of LexA and UmuD mediated by recA Pro67 mutants: implications for common LexA and UmuD binding sites on RecA
    • Konola J.T., Guzzo A., Gow J.B., Walker G.C., and Knight K.L. Differential cleavage of LexA and UmuD mediated by recA Pro67 mutants: implications for common LexA and UmuD binding sites on RecA. J. Mol. Biol. 276 (1998) 405-415
    • (1998) J. Mol. Biol. , vol.276 , pp. 405-415
    • Konola, J.T.1    Guzzo, A.2    Gow, J.B.3    Walker, G.C.4    Knight, K.L.5
  • 24
    • 0029786592 scopus 로고    scopus 로고
    • In vitro selection of preferred DNA pairing sequences by the Escherichia coli RecA protein
    • Tracy R.B., and Kowalczykowski S.C. In vitro selection of preferred DNA pairing sequences by the Escherichia coli RecA protein. Genes Dev. 10 (1996) 1890-1903
    • (1996) Genes Dev. , vol.10 , pp. 1890-1903
    • Tracy, R.B.1    Kowalczykowski, S.C.2
  • 25
    • 39649119942 scopus 로고    scopus 로고
    • Lin, L.-L. (1988). A genetic and biochemical analysis of LexA repressor cleavage in Escherichia coli K-12. Ph.D. thesis, University of Arizona, Tucson, AZ.
    • Lin, L.-L. (1988). A genetic and biochemical analysis of LexA repressor cleavage in Escherichia coli K-12. Ph.D. thesis, University of Arizona, Tucson, AZ.
  • 26
    • 0024549529 scopus 로고
    • Lambda repressor mutants that are better substrates for RecA-mediated cleavage
    • Gimble F.S., and Sauer R.T. Lambda repressor mutants that are better substrates for RecA-mediated cleavage. J. Mol. Biol. 206 (1989) 29-39
    • (1989) J. Mol. Biol. , vol.206 , pp. 29-39
    • Gimble, F.S.1    Sauer, R.T.2
  • 27
    • 0025939212 scopus 로고
    • Energetics of subunit dimerization in bacteriophage lambda cI repressor: linkage to protons, temperature, and KCl
    • Koblan K.S., and Ackers G.K. Energetics of subunit dimerization in bacteriophage lambda cI repressor: linkage to protons, temperature, and KCl. Biochemistry 30 (1991) 7817-7821
    • (1991) Biochemistry , vol.30 , pp. 7817-7821
    • Koblan, K.S.1    Ackers, G.K.2
  • 28
    • 0026657433 scopus 로고
    • Refined 1.8 Å crystal structure of the lambda repressor-operator complex
    • Beamer L.J., and Pabo C.O. Refined 1.8 Å crystal structure of the lambda repressor-operator complex. J. Mol. Biol. 227 (1992) 177-196
    • (1992) J. Mol. Biol. , vol.227 , pp. 177-196
    • Beamer, L.J.1    Pabo, C.O.2
  • 29
    • 0028232652 scopus 로고
    • Specificity determinants for the interaction of lambda repressor and P22 repressor dimers
    • Whipple F.W., Kuldell N.H., Cheatham L.A., and Hochschild A. Specificity determinants for the interaction of lambda repressor and P22 repressor dimers. Genes Dev. 8 (1994) 1212-1223
    • (1994) Genes Dev. , vol.8 , pp. 1212-1223
    • Whipple, F.W.1    Kuldell, N.H.2    Cheatham, L.A.3    Hochschild, A.4
  • 30
    • 0019844815 scopus 로고
    • Preferential cleavage of phage lambda repressor monomers by recA protease
    • Cohen S., Knoll B.J., Little J.W., and Mount D.W. Preferential cleavage of phage lambda repressor monomers by recA protease. Nature 294 (1981) 182-184
    • (1981) Nature , vol.294 , pp. 182-184
    • Cohen, S.1    Knoll, B.J.2    Little, J.W.3    Mount, D.W.4
  • 31
    • 0019787267 scopus 로고
    • Repressor cleavage as a prophage induction mechanism: hypersensitivity of a mutant lambda cI protein to recA-mediated proteolysis
    • Crowl R.M., Boyce R.P., and Echols H. Repressor cleavage as a prophage induction mechanism: hypersensitivity of a mutant lambda cI protein to recA-mediated proteolysis. J. Mol. Biol. 152 (1981) 815-819
    • (1981) J. Mol. Biol. , vol.152 , pp. 815-819
    • Crowl, R.M.1    Boyce, R.P.2    Echols, H.3
  • 32
    • 0346991734 scopus 로고    scopus 로고
    • The preferred substrate for RecA-mediated cleavage of bacteriophage 434 repressor is the DNA-bound dimer
    • Pawlowski D.R., and Koudelka G.B. The preferred substrate for RecA-mediated cleavage of bacteriophage 434 repressor is the DNA-bound dimer. J. Bacteriol. 186 (2004) 1-7
    • (2004) J. Bacteriol. , vol.186 , pp. 1-7
    • Pawlowski, D.R.1    Koudelka, G.B.2
  • 33
    • 0033524962 scopus 로고    scopus 로고
    • Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity
    • McDonald J.P., Peat T.S., Levine A.S., and Woodgate R. Intermolecular cleavage by UmuD-like enzymes: identification of residues required for cleavage and substrate specificity. J. Mol. Biol. 285 (1999) 2199-2209
    • (1999) J. Mol. Biol. , vol.285 , pp. 2199-2209
    • McDonald, J.P.1    Peat, T.S.2    Levine, A.S.3    Woodgate, R.4
  • 34
    • 0019835729 scopus 로고
    • Binding of the recA protein of Escherichia coli to single- and double-stranded DNA
    • McEntee K., Weinstock G.M., and Lehman I.R. Binding of the recA protein of Escherichia coli to single- and double-stranded DNA. J. Biol. Chem. 256 (1981) 8835-8844
    • (1981) J. Biol. Chem. , vol.256 , pp. 8835-8844
    • McEntee, K.1    Weinstock, G.M.2    Lehman, I.R.3
  • 35
    • 0027255851 scopus 로고
    • The LexA repressor binds within the deep helical groove of the activated RecA filament
    • Yu X., and Egelman E.H. The LexA repressor binds within the deep helical groove of the activated RecA filament. J. Mol. Biol. 231 (1993) 29-40
    • (1993) J. Mol. Biol. , vol.231 , pp. 29-40
    • Yu, X.1    Egelman, E.H.2
  • 36
    • 0029835784 scopus 로고    scopus 로고
    • Interaction of Escherichia coli RecA protein with LexA repressor: II. Inhibition of DNA strand exchange by the uncleavable LexA S119A repressor argues that recombination and SOS induction are competitive processes
    • Harmon F.G., Rehrauer W.M., and Kowalczykowski S.C. Interaction of Escherichia coli RecA protein with LexA repressor: II. Inhibition of DNA strand exchange by the uncleavable LexA S119A repressor argues that recombination and SOS induction are competitive processes. J. Biol. Chem. 271 (1996) 23874-23883
    • (1996) J. Biol. Chem. , vol.271 , pp. 23874-23883
    • Harmon, F.G.1    Rehrauer, W.M.2    Kowalczykowski, S.C.3
  • 37
    • 0025915719 scopus 로고
    • Mutant LexA proteins with an increased rate of in vivo cleavage
    • Smith M.H., Cavenagh M.M., and Little J.W. Mutant LexA proteins with an increased rate of in vivo cleavage. Proc. Natl Acad. Sci. USA 88 (1991) 7356-7360
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 7356-7360
    • Smith, M.H.1    Cavenagh, M.M.2    Little, J.W.3
  • 38
    • 0021104403 scopus 로고
    • The SOS regulatory system: control of its state by the level of RecA protease
    • Little J.W. The SOS regulatory system: control of its state by the level of RecA protease. J. Mol. Biol. 167 (1983) 791-808
    • (1983) J. Mol. Biol. , vol.167 , pp. 791-808
    • Little, J.W.1
  • 39
    • 0141757508 scopus 로고    scopus 로고
    • Complexes of RecA with LexA and RecX differentiate between active and inactive RecA nucleoprotein filaments
    • VanLoock M.S., Yu X., Yang S., Galkin V.E., Huang H., Rajan S.S., et al. Complexes of RecA with LexA and RecX differentiate between active and inactive RecA nucleoprotein filaments. J. Mol. Biol. 333 (2003) 345-354
    • (2003) J. Mol. Biol. , vol.333 , pp. 345-354
    • VanLoock, M.S.1    Yu, X.2    Yang, S.3    Galkin, V.E.4    Huang, H.5    Rajan, S.S.6
  • 40
    • 0020475459 scopus 로고
    • Characterization of complexes between recA protein and duplex DNA by electron microscopy
    • Di Capua E., Engel A., Stasiak A., and Koller T. Characterization of complexes between recA protein and duplex DNA by electron microscopy. J. Mol. Biol. 157 (1982) 87-103
    • (1982) J. Mol. Biol. , vol.157 , pp. 87-103
    • Di Capua, E.1    Engel, A.2    Stasiak, A.3    Koller, T.4
  • 43
    • 0029973975 scopus 로고    scopus 로고
    • Mutant LexA proteins with specific defects in autodigestion
    • Shepley D.P., and Little J.W. Mutant LexA proteins with specific defects in autodigestion. Proc. Natl Acad. Sci. USA 93 (1996) 11528-11533
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11528-11533
    • Shepley, D.P.1    Little, J.W.2
  • 44
    • 0036782672 scopus 로고    scopus 로고
    • 32P-labeling of cytokines, monoclonal antibodies, and other protein substrates for quantitative assays and therapeutic application
    • 32P-labeling of cytokines, monoclonal antibodies, and other protein substrates for quantitative assays and therapeutic application. BioTechniques 33 (2002) S76-S87
    • (2002) BioTechniques , vol.33
    • Clark, W.A.1    Izotova, L.2    Philipova, D.3    Wu, W.4    Lin, L.5    Pestka, S.6
  • 45
    • 0033517148 scopus 로고    scopus 로고
    • Robustness of a gene regulatory circuit
    • Little J.W., Shepley D.P., and Wert D.W. Robustness of a gene regulatory circuit. EMBO J. 18 (1999) 4299-4307
    • (1999) EMBO J. , vol.18 , pp. 4299-4307
    • Little, J.W.1    Shepley, D.P.2    Wert, D.W.3
  • 46
    • 0037938848 scopus 로고    scopus 로고
    • C-terminal deletions of the Escherichia coli RecA protein. Characterization of in vivo and in vitro effects
    • Lusetti S.L., Wood E.A., Fleming C.D., Modica M.J., Korth J., Abbott L., et al. C-terminal deletions of the Escherichia coli RecA protein. Characterization of in vivo and in vitro effects. J. Biol. Chem. 278 (2003) 16372-16380
    • (2003) J. Biol. Chem. , vol.278 , pp. 16372-16380
    • Lusetti, S.L.1    Wood, E.A.2    Fleming, C.D.3    Modica, M.J.4    Korth, J.5    Abbott, L.6
  • 48
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., and Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4 (1995) 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 50
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 51
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 52
    • 0023809601 scopus 로고
    • Determination of quaternary structure of an active enzyme using chemical cross-linking with glutaraldehyde
    • Fleischer S., and Fleischer B. (Eds), Academic Press, New York, NY
    • Craig W.S. Determination of quaternary structure of an active enzyme using chemical cross-linking with glutaraldehyde. In: Fleischer S., and Fleischer B. (Eds). Methods in Enzymology vol. 156 (1988), Academic Press, New York, NY 333-345
    • (1988) Methods in Enzymology , vol.156 , pp. 333-345
    • Craig, W.S.1
  • 53
    • 0029940132 scopus 로고    scopus 로고
    • Cooperativity mutants of bacteriophage λ cI repressor: temperature dependence of self-assembly
    • Burz D.S., and Ackers G.K. Cooperativity mutants of bacteriophage λ cI repressor: temperature dependence of self-assembly. Biochemistry 35 (1996) 3341-3350
    • (1996) Biochemistry , vol.35 , pp. 3341-3350
    • Burz, D.S.1    Ackers, G.K.2


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