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Volumn 286, Issue 2, 1999, Pages 437-445

On the in vivo function of the RecA ATPase

Author keywords

Allosteric effector; ATP hydrolysis; Branch migration; RecA; Recombination

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; RECA PROTEIN; RNA; SINGLE STRANDED DNA;

EID: 0033582802     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2457     Document Type: Article
Times cited : (38)

References (40)
  • 1
    • 0030584084 scopus 로고    scopus 로고
    • Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro
    • Baumann P., Benson F. E., West S. C. Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell. 87:1996;757-766.
    • (1996) Cell , vol.87 , pp. 757-766
    • Baumann, P.1    Benson, F.E.2    West, S.C.3
  • 2
    • 0033582679 scopus 로고    scopus 로고
    • Toxic mutations in the recA gene of E. coli prevent proper chromosome segregation
    • Campbell M. J., Davis R. W. Toxic mutations in the recA gene of E. coli prevent proper chromosome segregation. J. Mol. Biol. 286:1999;417-435.
    • (1999) J. Mol. Biol. , vol.286 , pp. 417-435
    • Campbell, M.J.1    Davis, R.W.2
  • 3
    • 0020997753 scopus 로고
    • Binding of RecA protein to single-stranded nucleic acids: Spectroscopic studies using fluorescent polynucleotides
    • Cazenave C., Toulme J. J., Helene C. Binding of RecA protein to single-stranded nucleic acids: spectroscopic studies using fluorescent polynucleotides. EMBO J. 2:1983;2247-2251.
    • (1983) EMBO J. , vol.2 , pp. 2247-2251
    • Cazenave, C.1    Toulme, J.J.2    Helene, C.3
  • 4
    • 0343551289 scopus 로고
    • RecA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange
    • Cox M. M., Lehman I. R. recA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange. Proc. Natl Acad. Sci. USA. 78:1981;3433-3437.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 3433-3437
    • Cox, M.M.1    Lehman, I.R.2
  • 5
    • 0023069449 scopus 로고
    • Enzymes of general recombination
    • Cox M. M., Lehman I. R. Enzymes of general recombination. Annu. Rev. Biochem. 56:1987;229-262.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 229-262
    • Cox, M.M.1    Lehman, I.R.2
  • 7
    • 0028790871 scopus 로고
    • Evidence for elongation of the helical pitch of the RecA filament upon ATP and ADP binding using small-angle neutron scattering
    • Ellouze C., Takahashi M., Wittung P., Mortensen K., Schnarr M., Norden B. Evidence for elongation of the helical pitch of the RecA filament upon ATP and ADP binding using small-angle neutron scattering. Eur. J. Biochem. 233:1995;579-583.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 579-583
    • Ellouze, C.1    Takahashi, M.2    Wittung, P.3    Mortensen, K.4    Schnarr, M.5    Norden, B.6
  • 8
    • 0016816177 scopus 로고
    • Prophage induction and cell division in E. coli. III. Mutations sfiA and sfiB restore division in tif and lon strains and permit the expression of mutator properties of tif
    • George J., Castellazzi M., Buttin G. Prophage induction and cell division in E. coli. III. Mutations sfiA and sfiB restore division in tif and lon strains and permit the expression of mutator properties of tif. Mol. Gen. Genet. 140:1975;309-332.
    • (1975) Mol. Gen. Genet. , vol.140 , pp. 309-332
    • George, J.1    Castellazzi, M.2    Buttin, G.3
  • 9
    • 0022635264 scopus 로고
    • A genetic analysis of primary products of bacteriophage lambda recombination
    • Huisman O., Fox M. S. A genetic analysis of primary products of bacteriophage lambda recombination. Genetics. 112:1986;409-420.
    • (1986) Genetics , vol.112 , pp. 409-420
    • Huisman, O.1    Fox, M.S.2
  • 10
    • 0022971443 scopus 로고
    • Interaction of recA protein with a photoaffinity analogue of ATP, 8-azido-ATP: Determination of nucleotide cofactor binding parameters and of the relationship between ATP binding and ATP hydrolysis
    • Kowalczykowski S. C. Interaction of recA protein with a photoaffinity analogue of ATP, 8-azido-ATP: determination of nucleotide cofactor binding parameters and of the relationship between ATP binding and ATP hydrolysis. Biochemistry. 25:1986;5872-5881.
    • (1986) Biochemistry. , vol.25 , pp. 5872-5881
    • Kowalczykowski, S.C.1
  • 11
    • 0025891414 scopus 로고
    • Biochemistry of genetic recombination: Energetics and mechanism of DNA strand exchange
    • Kowalczykowski S. C. Biochemistry of genetic recombination: energetics and mechanism of DNA strand exchange. Annu. Rev. Biophys. Chem. 20:1991;539-575.
    • (1991) Annu. Rev. Biophys. Chem. , vol.20 , pp. 539-575
    • Kowalczykowski, S.C.1
  • 12
    • 0028308710 scopus 로고
    • Homologous pairing and DNA strand-exchange proteins
    • Kowalczykowski S. C., Eggleston A. K. Homologous pairing and DNA strand-exchange proteins. Annu. Rev. Biochem. 63:1994;991-1043.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 991-1043
    • Kowalczykowski, S.C.1    Eggleston, A.K.2
  • 13
    • 0023135142 scopus 로고
    • Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
    • Kowalczykowski S. C., Krupp R. A. Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA. J. Mol. Biol. 193:1987;97-113.
    • (1987) J. Mol. Biol. , vol.193 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 14
    • 0025240670 scopus 로고
    • Properties of recA441 protein-catalyzed DNA strand exchange can be attributed to an enhanced ability to compete with SSB protein
    • Lavery P. E., Kowalczykowski S. C. Properties of recA441 protein-catalyzed DNA strand exchange can be attributed to an enhanced ability to compete with SSB protein. J. Biol. Chem. 265:1990;4004-4010.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4004-4010
    • Lavery, P.E.1    Kowalczykowski, S.C.2
  • 15
    • 0024999088 scopus 로고
    • Inhibition of recA protein promoted ATP hydrolysis. 1. ATP gamma S and ADP are antagonistic inhibitors
    • Lee J. W., Cox M. M. Inhibition of recA protein promoted ATP hydrolysis. 1. ATP gamma S and ADP are antagonistic inhibitors. Biochemistry. 29:1990;7666-7676.
    • (1990) Biochemistry , vol.29 , pp. 7666-7676
    • Lee, J.W.1    Cox, M.M.2
  • 16
    • 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
  • 18
    • 0020316054 scopus 로고
    • The SOS regulatory system of Escherichia coli
    • Little J. W., 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
  • 19
    • 0026009412 scopus 로고
    • Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG
    • Lloyd R. G. Conjugational recombination in resolvase-deficient ruvC mutants of Escherichia coli K-12 depends on recG. J. Bacteriol. 173:1991;5414-5418.
    • (1991) J. Bacteriol. , vol.173 , pp. 5414-5418
    • Lloyd, R.G.1
  • 20
    • 0027397630 scopus 로고
    • Dissociation of synthetic Holliday junctions by E. coli RecG protein
    • Lloyd R. G., Sharples G. J. Dissociation of synthetic Holliday junctions by E. coli RecG protein. EMBO J. 12:1993a;17-22.
    • (1993) EMBO J. , vol.12 , pp. 17-22
    • Lloyd, R.G.1    Sharples, G.J.2
  • 21
    • 0027212716 scopus 로고
    • Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli
    • Lloyd R. G., Sharples G. J. Processing of recombination intermediates by the RecG and RuvAB proteins of Escherichia coli. Nucl. Acids Res. 21:1993b;1719-1725.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 1719-1725
    • Lloyd, R.G.1    Sharples, G.J.2
  • 22
    • 0030794026 scopus 로고    scopus 로고
    • RecA as a motor protein. Testing models for the role of ATP hydrolysis in DNA strand exchange
    • MacFarland K. J., Shan Q., Inman R. B., Cox M. M. RecA as a motor protein. Testing models for the role of ATP hydrolysis in DNA strand exchange. J. Biol. Chem. 272:1997;17675-17685.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17675-17685
    • MacFarland, K.J.1    Shan, Q.2    Inman, R.B.3    Cox, M.M.4
  • 23
    • 0019789922 scopus 로고
    • Tif-1 mutation alters polynucleotide recognition by the recA protein of Escherichia coli
    • McEntee K., Weinstock G. M. tif-1 mutation alters polynucleotide recognition by the recA protein of Escherichia coli. Proc. Natl Acad. Sci. USA. 78:1981;6061-6065.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 6061-6065
    • McEntee, K.1    Weinstock, G.M.2
  • 24
    • 0025269888 scopus 로고
    • Biochemical properties of the Escherichia coli recA430 protein. Analysis of a mutation that affects the interaction of the ATP-recA protein complex with single-stranded DNA
    • Menetski J. P., Kowalczykowski S. C. Biochemical properties of the Escherichia coli recA430 protein. Analysis of a mutation that affects the interaction of the ATP-recA protein complex with single-stranded DNA. J. Mol. Biol. 211:1990;845-855.
    • (1990) J. Mol. Biol. , vol.211 , pp. 845-855
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 25
    • 0025166577 scopus 로고
    • Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis
    • Menetski J. P., Bear D. G., Kowalczykowski S. C. Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis. Proc. Natl Acad. Sci. USA. 87:1990;21-25.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 21-25
    • Menetski, J.P.1    Bear, D.G.2    Kowalczykowski, S.C.3
  • 26
    • 0026741832 scopus 로고
    • Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
    • Parsons C. A., Tsaneva I., Lloyd R. G., West S. C. Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions. Proc. Natl Acad. Sci USA. 89:1992;5452-5456.
    • (1992) Proc. Natl Acad. Sci USA , vol.89 , pp. 5452-5456
    • Parsons, C.A.1    Tsaneva, I.2    Lloyd, R.G.3    West, S.C.4
  • 27
    • 0023139868 scopus 로고
    • Stable binding of recA protein to duplex DNA. Unraveling a paradox
    • Pugh B. F., Cox M. M. Stable binding of recA protein to duplex DNA. Unraveling a paradox. J. Biol. Chem. 262:1987;1326-1336.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1326-1336
    • Pugh, B.F.1    Cox, M.M.2
  • 28
    • 0023726413 scopus 로고
    • General mechanism for RecA protein binding to duplex DNA
    • Pugh B. F., Cox M. M. General mechanism for RecA protein binding to duplex DNA. J. Mol. Biol. 203:1988;479-493.
    • (1988) J. Mol. Biol. , vol.203 , pp. 479-493
    • Pugh, B.F.1    Cox, M.M.2
  • 29
    • 0020349256 scopus 로고
    • Homologous pairing and strand exchange in genetic recombination
    • Radding C. M. Homologous pairing and strand exchange in genetic recombination. Annu. Rev. Genet. 16:1982;405-437.
    • (1982) Annu. Rev. Genet. , vol.16 , pp. 405-437
    • Radding, C.M.1
  • 30
    • 0027397313 scopus 로고
    • Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation
    • Rehrauer W. M., Kowalczykowski S. C. Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation. J. Biol. Chem. 268:1993;1292-1297.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1292-1297
    • Rehrauer, W.M.1    Kowalczykowski, S.C.2
  • 32
    • 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., 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
  • 34
    • 0020489557 scopus 로고
    • Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative
    • Silver M. S., Fersht A. R. Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative. Biochemistry. 21:1982;6066-6072.
    • (1982) Biochemistry , vol.21 , pp. 6066-6072
    • Silver, M.S.1    Fersht, A.R.2
  • 35
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story R. M., Steitz T. A. Structure of the recA protein-ADP complex. Nature. 355:1992;374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 36
    • 0029953512 scopus 로고    scopus 로고
    • Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis
    • Sung P., Stratton S. A. Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis. J. Biol. Chem. 271:1996;27983-27986.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27983-27986
    • Sung, P.1    Stratton, S.A.2
  • 37
    • 0023027015 scopus 로고
    • Location and functional regions of the Escherichia coli RecA protein by DNA sequence analysis of RecA protease-constitutive mutants
    • Wang W. B., Tessman E. S. Location and functional regions of the Escherichia coli RecA protein by DNA sequence analysis of RecA protease-constitutive mutants. J. Bacteriol. 168:1986;901-910.
    • (1986) J. Bacteriol , vol.168 , pp. 901-910
    • Wang, W.B.1    Tessman, E.S.2
  • 38
    • 0024094431 scopus 로고
    • Activation of protease-constitutive recA proteins of Escherichia coli by all of the common nucleoside triphosphates
    • Wang W. B., Sassanfar M., Tessman I., Roberts J. W., Tessman E. S. Activation of protease-constitutive recA proteins of Escherichia coli by all of the common nucleoside triphosphates. J. Bacteriol. 170:1988a;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
  • 39
    • 0024095244 scopus 로고
    • Activation of protease-constitutive recA proteins of Escherichia coli by rRNA and tRNA
    • Wang W. B., Tessman E. S., Tessman I. Activation of protease-constitutive recA proteins of Escherichia coli by rRNA and tRNA. J. Bacteriol. 170:1988b;4823-4827.
    • (1988) J. Bacteriol. , vol.170 , pp. 4823-4827
    • Wang, W.B.1    Tessman, E.S.2    Tessman, I.3
  • 40
    • 0027375810 scopus 로고
    • Analysis of two distinct single-stranded DNA binding sites on the recA nucleoprotein filament
    • Zlotnick A., Mitchell R. S., Steed R. K., Brenner S. L. Analysis of two distinct single-stranded DNA binding sites on the recA nucleoprotein filament. J. Biol. Chem. 268:1993;22525-22530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22525-22530
    • Zlotnick, A.1    Mitchell, R.S.2    Steed, R.K.3    Brenner, S.L.4


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