메뉴 건너뛰기




Volumn 182, Issue 6, 2000, Pages 1659-1670

Analysis of Escherichia coli RecA interactions with LexA, λ CI, and UmuD by site-directed mutagenesis of recA

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; PROTEINASE;

EID: 0034090729     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.6.1659-1670.2000     Document Type: Article
Times cited : (40)

References (63)
  • 1
    • 0029933569 scopus 로고    scopus 로고
    • Genetic characteristics of new recA mutants of Escherichia coli K-12
    • Alexseyev, A. A., I. V. Bakhlanova, E. N. Zaitsev, and V. A. Lanzov. 1996. Genetic characteristics of new recA mutants of Escherichia coli K-12. J. Bacteriol. 178:2018-2024.
    • (1996) J. Bacteriol. , vol.178 , pp. 2018-2024
    • Alexseyev, A.A.1    Bakhlanova, I.V.2    Zaitsev, E.N.3    Lanzov, V.A.4
  • 2
    • 0017839971 scopus 로고
    • Maximizing gene expression on a plasmid using recombination in vitro
    • Backman, K., and M. Ptashne. 1978. Maximizing gene expression on a plasmid using recombination in vitro. Cell 13:65-71.
    • (1978) Cell , vol.13 , pp. 65-71
    • Backman, K.1    Ptashne, M.2
  • 3
    • 0018782266 scopus 로고
    • Inactivation of prophage λ repressor in vivo
    • 2a. Bailone, A., A. Levine, and R. Devoret. 1979. Inactivation of prophage λ repressor in vivo. J. Mol. Biol. 131:553-572.
    • (1979) J. Mol. Biol. , vol.131 , pp. 553-572
    • Bailone, A.1    Levine, A.2    Devoret, R.3
  • 5
    • 0021714276 scopus 로고
    • A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors
    • Churchward, G., D. Belin, and Y. Nagamine. 1984. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors. Gene 31:165-171.
    • (1984) Gene , vol.31 , pp. 165-171
    • Churchward, G.1    Belin, D.2    Nagamine, Y.3
  • 6
    • 0031829701 scopus 로고    scopus 로고
    • A broadening view of recombinational DNA repair in bacteria
    • Cox, M. M. 1998. A broadening view of recombinational DNA repair in bacteria. Genes Cells 3:65-78.
    • (1998) Genes Cells , vol.3 , pp. 65-78
    • Cox, M.M.1
  • 7
    • 0032605682 scopus 로고    scopus 로고
    • Recombinational DNA repair in bacteria and the RecA protein
    • Cox, M. M. 1999. Recombinational DNA repair in bacteria and the RecA protein. Prog. Nucleic Acid Res. Mol. Biol. 63:310-366.
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.63 , pp. 310-366
    • Cox, M.M.1
  • 8
    • 0026511367 scopus 로고
    • A partially deficient mutant, recA 1730. that fails to form normal nucleoprotein filaments
    • Dutreix, M., B. Burnett, A. Bailone, C. M. Radding, and R. Devoret. 1992. A partially deficient mutant, recA 1730. that fails to form normal nucleoprotein filaments. Mol. Gen. Genet. 232:489-497.
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 489-497
    • Dutreix, M.1    Burnett, B.2    Bailone, A.3    Radding, C.M.4    Devoret, R.5
  • 9
    • 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., P. L. Moreau, A. Bailone, F. Galibert, J. R. Battista, G. C. Walker, and R. Devoret. 1989. 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: 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
  • 11
    • 0027485184 scopus 로고
    • Novel mechanism for UV sensitivity and apparent UV nonmutability of recA432 mutants: Persistent LexA cleavage following SOS induction
    • Ennis, D. G., J. W. Little, and D. W. Mount. 1993. Novel mechanism for UV sensitivity and apparent UV nonmutability of recA432 mutants: persistent LexA cleavage following SOS induction. J. Bacteriol. 175:7373-7382.
    • (1993) J. Bacteriol. , vol.175 , pp. 7373-7382
    • Ennis, D.G.1    Little, J.W.2    Mount, D.W.3
  • 12
    • 0025866547 scopus 로고
    • Site-directed mutagenesis of the RecA protein of Escherichia coli. Tyrosine 264 is required for efficient ATP hydrolysis and strand exchange but not for LexA repressor inactivation
    • Freitag, N. E., and K. McEntee. 1991. Site-directed mutagenesis of the RecA protein of Escherichia coli. Tyrosine 264 is required for efficient ATP hydrolysis and strand exchange but not for LexA repressor inactivation. J. Biol. Chem. 266:7058-7066.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7058-7066
    • Freitag, N.E.1    McEntee, K.2
  • 14
    • 0021919232 scopus 로고
    • Mutations in bacteriophage λ repressor that prevent RecA-mediated cleavage
    • Gimble, F. S., and R. T. Sauer. 1985. Mutations in bacteriophage λ repressor that prevent RecA-mediated cleavage. J. Bacteriol. 162:147-154.
    • (1985) J. Bacteriol. , vol.162 , pp. 147-154
    • Gimble, F.S.1    Sauer, R.T.2
  • 15
    • 0023042845 scopus 로고
    • - proteins in the autodigestion and RecA-mediated cleavage reactions
    • - proteins in the autodigestion and RecA-mediated cleavage reactions. J. Mol. Biol. 192:39-47.
    • (1986) J. Mol. Biol. , vol.192 , pp. 39-47
    • Gimble, F.S.1    Sauer, R.T.2
  • 16
    • 0029835784 scopus 로고    scopus 로고
    • Interaction of Escherichia coli RecA protein with LexA repressor. 2. Inhibition of DNA strand exchange by Ihe uncleavable LexA S119A repressor argues that recombination and SOS induction are competitive processes
    • Harmon, F. G., W. M. Rehrauer, and S. C. Kowalczykowski. 1996. Interaction of Escherichia coli RecA protein with LexA repressor. 2. Inhibition of DNA strand exchange by Ihe uncleavable LexA S119A repressor argues that recombination and SOS induction are competitive processes. J. Biol. Chem. 271:23874-23883.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23874-23883
    • Harmon, F.G.1    Rehrauer, W.M.2    Kowalczykowski, S.C.3
  • 17
    • 0026572863 scopus 로고
    • Inhibitory effects of N-and C-terminal truncated Escherichia coli recA gene products on functions of the wild-type recA gene
    • Horii, T., N. Ozawa, T. Ogawa, and H. Ogawa. 1992. Inhibitory effects of N-and C-terminal truncated Escherichia coli recA gene products on functions of the wild-type recA gene. J. Mol. Biol. 223:105-114.
    • (1992) J. Mol. Biol. , vol.223 , pp. 105-114
    • Horii, T.1    Ozawa, N.2    Ogawa, T.3    Ogawa, H.4
  • 18
    • 0030582680 scopus 로고    scopus 로고
    • Characterization of a mutant RecA protein that facilitates homologous genetic recombination but not recombinational DNA repair: RecA423
    • Ishimori, K., S. Sommer, A. Bailone, M. Takahashi, M. M. Cox, and R. Devoret. 1996. Characterization of a mutant RecA protein that facilitates homologous genetic recombination but not recombinational DNA repair: RecA423. J. Mol. Biol. 264:696-712.
    • (1996) J. Mol. Biol. , vol.264 , pp. 696-712
    • Ishimori, K.1    Sommer, S.2    Bailone, A.3    Takahashi, M.4    Cox, M.M.5    Devoret, R.6
  • 19
    • 0027195935 scopus 로고
    • LexA and λ repressors as enzymes: Specific cleavage in an intermolecular reaction
    • Kim, B., and J. W. Little. 1993. LexA and λ repressors as enzymes: specific cleavage in an intermolecular reaction. Cell 73:1165-1173.
    • (1993) Cell , vol.73 , pp. 1165-1173
    • Kim, B.1    Little, J.W.2
  • 20
    • 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., A. Guzzo, J. B. Gow, G. C. Walker, and K. L. Knight. 1998. Differential cleavage of LexA and UmuD mediated by recA pro67 mutants: implications for common LexA and UmuD binding sites on RecA. J. Mol. Biol. 276:405-415.
    • (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
  • 21
    • 0028988009 scopus 로고
    • 67 in the RecA protein P-loop motif differentially modify coprotease function and separate coprotease from recombination activities
    • 67 in the RecA protein P-loop motif differentially modify coprotease function and separate coprotease from recombination activities. J. Biol. Chem. 270:8411-8419.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8411-8419
    • Konola, J.T.1    Nastri, H.G.2    Logan, K.M.3    Knight, K.L.4
  • 22
    • 0025848721 scopus 로고
    • Biochemical and biological function of Escherichia coli RecA protein: Behavior of mutant RecA proteins
    • Kowalczykowski, S. C. 1991. Biochemical and biological function of Escherichia coli RecA protein: behavior of mutant RecA proteins. Biochimie 73: 289-304.
    • (1991) Biochimie , vol.73 , pp. 289-304
    • Kowalczykowski, S.C.1
  • 23
    • 0026758817 scopus 로고
    • New mutations in and around the L2 disordered loop of the RecA protein modulate recombination and/or coprotease activity
    • Larminat, F., C. Cazaux, M. Germanier, and M. Defais. 1992. New mutations in and around the L2 disordered loop of the RecA protein modulate recombination and/or coprotease activity. J. Bacteriol. 174:6264-6269.
    • (1992) J. Bacteriol. , vol.174 , pp. 6264-6269
    • Larminat, F.1    Cazaux, C.2    Germanier, M.3    Defais, M.4
  • 25
    • 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. 170:2163-2173.
    • (1988) J. Bacteriol. , vol.170 , pp. 2163-2173
    • Lin, L.L.1    Little, J.W.2
  • 27
    • 0021104403 scopus 로고
    • The SOS regulatory system: Control of its state by the level of RecA protease
    • Little, J. W. 1983. The SOS regulatory system: control of its state by the level of RecA protease. J. Mol. Biol. 167:791-808.
    • (1983) J. Mol. Biol. , vol.167 , pp. 791-808
    • Little, J.W.1
  • 28
    • 0012740578 scopus 로고
    • Variations in the stability of lexA repressor during the SOS regulatory cycle
    • E. C. Friedberg and B. A. Bridges (ed.), Alan R. Liss, Inc., New York, N.Y.
    • Little, J. W. 1983. Variations in the stability of lexA repressor during the SOS regulatory cycle, p. 369-378. In E. C. Friedberg and B. A. Bridges (ed.), Cellular responses to DNA damage. Alan R. Liss, Inc., New York, N.Y.
    • (1983) Cellular Responses to DNA Damage , pp. 369-378
    • Little, J.W.1
  • 29
    • 0343188817 scopus 로고
    • Autodigestion of lexA and phage lambda repressers
    • Little, J. W. 1984. Autodigestion of lexA and phage lambda repressers. Proc. Natl. Acad. Sci. USA 81:1375-1379.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 1375-1379
    • Little, J.W.1
  • 30
    • 0342663952 scopus 로고
    • Deletions within a hinge region of a specific DNA-binding protein
    • Little, J. W., and S. A. Hill. 1985. Deletions within a hinge region of a specific DNA-binding protein. Proc. Natl. Acad. Sci. USA 82:2301-2305.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 2301-2305
    • Little, J.W.1    Hill, S.A.2
  • 31
    • 0020316054 scopus 로고
    • The SOS regulatory system of Escherichia coli
    • Little, J. W., and D. W. Mount. 1982. The SOS regulatory system of Escherichia coli. Cell 29:11-22.
    • (1982) Cell , vol.29 , pp. 11-22
    • Little, J.W.1    Mount, D.W.2
  • 32
    • 0033517148 scopus 로고    scopus 로고
    • Robustness of a gene regulatory circuit
    • Little, J. W., D. P. Shepley, and D. W. Wert. 1999. Robustness of a gene regulatory circuit. EMBO J. 18:4299-4307.
    • (1999) EMBO J. , vol.18 , pp. 4299-4307
    • Little, J.W.1    Shepley, D.P.2    Wert, D.W.3
  • 33
    • 0027490946 scopus 로고
    • c) protein: Possible involvement of interfilament association in proteolytic and recombination activities
    • c) protein: possible involvement of interfilament association in proteolytic and recombination activities. J. Bacteriol. 175:6518-6529.
    • (1993) J. Bacteriol. , vol.175 , pp. 6518-6529
    • Liu, S.-K.1    Eisen, J.A.2    Hanawalt, P.C.3    Tessman, I.4
  • 35
  • 36
    • 0021767948 scopus 로고
    • Specificity of mutations induced in transfected DNA by mammalian cells
    • Miller, J. H., J. S. Lebkowski, K. S. Greisen, and M. P. Calos. 1984. Specificity of mutations induced in transfected DNA by mammalian cells. EMBO J. 3:3117-3121.
    • (1984) EMBO J. , vol.3 , pp. 3117-3121
    • Miller, J.H.1    Lebkowski, J.S.2    Greisen, K.S.3    Calos, M.P.4
  • 37
    • 0023218266 scopus 로고
    • Effects of overproduction of single-stranded DNA-binding protein on RecA-dependent processes in Escherichia coli
    • Moreau, P. L. 1987. Effects of overproduction of single-stranded DNA-binding protein on RecA-dependent processes in Escherichia coli. J. Mol. Biol. 194:621-634.
    • (1987) J. Mol. Biol. , vol.194 , pp. 621-634
    • Moreau, P.L.1
  • 38
    • 0030979685 scopus 로고    scopus 로고
    • Mutational analysis of the RecA protein L1 region identifies this area as a probable part of the co-protease substrate binding site
    • Nastri, H. G., A. Guzzo, C. S. Lange, G. C. Walker, and K. L. Knight. 1997. Mutational analysis of the RecA protein L1 region identifies this area as a probable part of the co-protease substrate binding site. Mol. Microbiol. 25: 967-978.
    • (1997) Mol. Microbiol. , vol.25 , pp. 967-978
    • Nastri, H.G.1    Guzzo, A.2    Lange, C.S.3    Walker, G.C.4    Knight, K.L.5
  • 39
    • 0027457534 scopus 로고
    • Inactivation of the recA protein by mutation of histidine 97 or lysine 248 at the subunit interface
    • Nguyen, T. T., K. A. Muench, and F. R. Bryant. 1993. Inactivation of the recA protein by mutation of histidine 97 or lysine 248 at the subunit interface. J. Biol. Chem. 268:3107-3113.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3107-3113
    • Nguyen, T.T.1    Muench, K.A.2    Bryant, F.R.3
  • 40
    • 0022527943 scopus 로고
    • General recombination: Functions and structure of RecA protein
    • Ogawa, H., and T. Ogawa. 1986. General recombination: functions and structure of RecA protein. Adv. Biophys. 21:135-148.
    • (1986) Adv. Biophys. , vol.21 , pp. 135-148
    • Ogawa, H.1    Ogawa, T.2
  • 41
    • 0023135141 scopus 로고
    • Differential repression of SOS genes by unstable LexA41 (Tsl-1) protein causes a "split-phenotype" in Escherichia coli K-12
    • Peterson, K. R., and D. W. Mount. 1987. Differential repression of SOS genes by unstable LexA41 (Tsl-1) protein causes a "split-phenotype" in Escherichia coli K-12. J. Mol. Biol. 193:27-40.
    • (1987) J. Mol. Biol. , vol.193 , pp. 27-40
    • Peterson, K.R.1    Mount, D.W.2
  • 42
    • 0032484207 scopus 로고    scopus 로고
    • Modulation of RecA nucleoprotein function by the mutagenic UmuD'C protein complex
    • Rehrauer, W. M., I. Bruck, R. Woodgate, M. F. Goodmann, and S. C. Kowalczykowski. 1998. Modulation of RecA nucleoprotein function by the mutagenic UmuD'C protein complex. J. Biol. Chem. 273:32384-32387.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32384-32387
    • Rehrauer, W.M.1    Bruck, I.2    Woodgate, R.3    Goodmann, M.F.4    Kowalczykowski, S.C.5
  • 43
    • 0029848426 scopus 로고    scopus 로고
    • Interaction of Escherichia coli RecA protein with LexA repressor. 1. LexA repressor cleavage is competitive with binding of a secondary DNA molecule
    • Rehrauer, W. M., P. E. Lavery, E. L. Palmer, R. N. Singh, and S. C. Kowalczykowski. 1996. Interaction of Escherichia coli RecA protein with LexA repressor. 1. LexA repressor cleavage is competitive with binding of a secondary DNA molecule. J. Biol. Chem. 271:23865-23873.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23865-23873
    • Rehrauer, W.M.1    Lavery, P.E.2    Palmer, E.L.3    Singh, R.N.4    Kowalczykowski, S.C.5
  • 44
    • 0002773599 scopus 로고
    • Lysogenic induction
    • R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y.
    • Roberts, J. W., and R. Devoret. 1983. Lysogenic induction, p. 123-144. In R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Lambda II. Cold Spring Harbor Laboratory, Cold Spring Harbor, N. Y.
    • (1983) Lambda II , pp. 123-144
    • Roberts, J.W.1    Devoret, R.2
  • 45
    • 0026620486 scopus 로고
    • In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage
    • Roland, K. L., M. H. Smith, J. A. Rupley, and J. W. Little. 1992. In vitro analysis of mutant LexA proteins with an increased rate of specific cleavage. J. Mol. Biol. 228:395-408.
    • (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
  • 46
    • 0025361131 scopus 로고
    • Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication
    • Sassanfar, M., and J. W. Roberts. 1990. Nature of the SOS-inducing signal in Escherichia coli. The involvement of DNA replication. J. Mol. Biol. 212: 79-96.
    • (1990) J. Mol. Biol. , vol.212 , pp. 79-96
    • Sassanfar, M.1    Roberts, J.W.2
  • 48
    • 0032127912 scopus 로고    scopus 로고
    • GTPase-activating proteins: Helping hands to complement an active site
    • Scheffzek, K., M. R. Ahmadian, and A. Wittinghofer. 1998. GTPase-activating proteins: helping hands to complement an active site. Trends Biochem. Sci. 23:257-262.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 257-262
    • Scheffzek, K.1    Ahmadian, M.R.2    Wittinghofer, A.3
  • 50
    • 0028129812 scopus 로고
    • Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli
    • Skiba, M. C., and K. L. Knight. 1994. Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli. J. Biol. Chem. 269:3823-3828.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3823-3828
    • Skiba, M.C.1    Knight, K.L.2
  • 51
    • 0023186212 scopus 로고
    • Lysine-156 and serine-119 are required for LexA represser cleavage: A possible mechanism
    • Slilaty, S. N., and J. W. Little. 1987. Lysine-156 and serine-119 are required for LexA represser cleavage: a possible mechanism. Proc. Natl. Acad. Sci. USA 84:3987-3991.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3987-3991
    • Slilaty, S.N.1    Little, J.W.2
  • 52
    • 0000802462 scopus 로고
    • General recombination
    • R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Smith, G. 1983. General recombination, p. 175-209. In R. W. Hendrix, J. W. Roberts, F. W. Stahl, and R. A. Weisberg (ed.), Lambda II. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1983) Lambda II , pp. 175-209
    • Smith, G.1
  • 53
    • 0025915719 scopus 로고
    • Mutant LexA proteins with an increased rate of in vivo cleavage
    • Smith, M. H., M. M. Cavenagh, and J. W. Little. 1991. Mutant LexA proteins with an increased rate of in vivo cleavage. Proc. Natl. Acad. Sci. USA 88: 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
  • 54
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story, R. M., I. T. Weber, and T. A. Steitz. 1992. The structure of the E. coli recA protein monomer and polymer. Nature 355:318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 55
    • 0025314791 scopus 로고
    • RecA protein of Escherichia coli has a third essential role in SOS mutator activity
    • Sweasy, J. B., E. M. Witkin, N. Sinha, and V. Roegner-Maniscalco. 1990. RecA protein of Escherichia coli has a third essential role in SOS mutator activity. J. Bacteriol. 172:3030-3036.
    • (1990) J. Bacteriol. , vol.172 , pp. 3030-3036
    • Sweasy, J.B.1    Witkin, E.M.2    Sinha, N.3    Roegner-Maniscalco, V.4
  • 56
    • 0026583199 scopus 로고
    • Genetic identification of the DNA binding domain of Escherichia coli LexA protein
    • Thliveris, A. T., and D. W. Mount. 1992. Genetic identification of the DNA binding domain of Escherichia coli LexA protein. Proc. Natl. Acad. Sci. USA 89:4500-4504.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4500-4504
    • Thliveris, A.T.1    Mount, D.W.2
  • 58
    • 0024094431 scopus 로고
    • Activation of protease-constitutive RecA proteins of Escherichia coli by all of the common nucleoside triphosphates
    • Wang, W.-B., M. Sassanfar, I. Tessman, J. W. Roberts, and E. S. Tessman. 1988. Activation of protease-constitutive RecA proteins of Escherichia coli by all of the common nucleoside triphosphates. J. Bacteriol. 170:4816-4822.
    • (1988) J. Bacteriol. , vol.170 , pp. 4816-4822
    • Wang, W.-B.1    Sassanfar, M.2    Tessman, I.3    Roberts, J.W.4    Tessman, E.S.5
  • 59
    • 0023027015 scopus 로고
    • Location of functional regions of the Escherichia coli RecA protein by DNA sequence analysis of RecA protease-constitutive mutants
    • Wang, W.-B., and E. S. Tessman. 1986. Location of functional regions of the Escherichia coli RecA protein by DNA sequence analysis of RecA protease-constitutive mutants. J. Bacteriol. 168:901-910.
    • (1986) J. Bacteriol. , vol.168 , pp. 901-910
    • Wang, W.-B.1    Tessman, E.S.2
  • 60
    • 0024095244 scopus 로고
    • Activation of protease-constitutive RecA proteins of Escherichia coli by rRNA and tRNA
    • Wang, W.-B., E. S. Tessman, and I. Tessman. 1988. Activation of protease-constitutive RecA proteins of Escherichia coli by rRNA and tRNA. J. Bacteriol. 170:4823-4827.
    • (1988) J. Bacteriol. , vol.170 , pp. 4823-4827
    • Wang, W.-B.1    Tessman, E.S.2    Tessman, I.3
  • 61
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman, K F., D. G. Drubin, and D. Botstein. 1992. Systematic mutational analysis of the yeast ACT1 gene. Genetics 132:337-350.
    • (1992) Genetics , vol.132 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 62
    • 0026666652 scopus 로고
    • Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible
    • Yu, X., and E. H. Egelman. 1992. Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertible. J. Mol. Biol. 227:334-346.
    • (1992) J. Mol. Biol. , vol.227 , pp. 334-346
    • Yu, X.1    Egelman, E.H.2
  • 63
    • 0027255851 scopus 로고
    • The LexA repressor binds within the deep helical groove of the activated RecA filament
    • Yu, X., and E. H. Egelman. 1993. The LexA repressor binds within the deep helical groove of the activated RecA filament. J. Mol. Biol. 231:29-40.
    • (1993) J. Mol. Biol. , vol.231 , pp. 29-40
    • Yu, X.1    Egelman, E.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.