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Volumn 293, Issue 4, 1999, Pages 769-780

The hRad51 and RecA proteins show significant differences in cooperative binding to single-stranded DNA

Author keywords

Cooperative DNA binding; Homologous recombination; hRad51 protein; IAsys biosensor; RecA protein

Indexed keywords

DOUBLE STRANDED DNA; RAD51 PROTEIN; RECA PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 0033527668     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3200     Document Type: Article
Times cited : (58)

References (53)
  • 1
    • 0030766963 scopus 로고    scopus 로고
    • The human Rad51 protein: Polarity of strand transfer and stimulation by hRPA
    • Baumann P., West S. C. The human Rad51 protein: polarity of strand transfer and stimulation by hRPA. EMBO J. 16:1997;5198-5206.
    • (1997) EMBO J. , vol.16 , pp. 5198-5206
    • Baumann, P.1    West, S.C.2
  • 2
    • 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
  • 3
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • Benson F. E., Stasiak A., West S. C. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J. 13:1994;5764-5771.
    • (1994) EMBO J. , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 4
    • 0032556865 scopus 로고    scopus 로고
    • Synergistic actions of Rad51 and Rad52 in recombination and DNA repair
    • Benson F. E., Baumann P., West S. C. Synergistic actions of Rad51 and Rad52 in recombination and DNA repair. Nature. 391:1998;401-404.
    • (1998) Nature , vol.391 , pp. 401-404
    • Benson, F.E.1    Baumann, P.2    West, S.C.3
  • 5
    • 0032559425 scopus 로고    scopus 로고
    • Equilibrium and kinetic binding analysis of the N-terminal domain of the Pf1 gene 5 protein and its interaction with single-stranded DNA
    • Bogdarina I., Fox D. G., Kneale G. G. Equilibrium and kinetic binding analysis of the N-terminal domain of the Pf1 gene 5 protein and its interaction with single-stranded DNA. J. Mol. Biol. 275:1998;443-452.
    • (1998) J. Mol. Biol. , vol.275 , pp. 443-452
    • Bogdarina, I.1    Fox, D.G.2    Kneale, G.G.3
  • 7
    • 0027466424 scopus 로고
    • What do X-ray crystallographic and electron microscopic structural studies of the RecA protein tell us about recombination?
    • Egelman E. H. What do X-ray crystallographic and electron microscopic structural studies of the RecA protein tell us about recombination? Curr. Opin. Struct. Biol. 3:1993;189-197.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 189-197
    • Egelman, E.H.1
  • 8
    • 0030069748 scopus 로고    scopus 로고
    • Exchanging partners: Recombination in E. coli
    • Eggleston A. K., West S. C. Exchanging partners: recombination in E. coli. Trends Genet. 12:1996;20-26.
    • (1996) Trends Genet. , vol.12 , pp. 20-26
    • Eggleston, A.K.1    West, S.C.2
  • 10
    • 0032403121 scopus 로고    scopus 로고
    • Interaction of human Rad51 recombination protein with single-stranded DNA binding protein, RPA
    • Golub E. I., Gupta R. C., Haaf T., Wold M. S., Radding C. M. Interaction of human Rad51 recombination protein with single-stranded DNA binding protein, RPA. Nucl. Acids Res. 26:1998;5388-5393.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 5388-5393
    • Golub, E.I.1    Gupta, R.C.2    Haaf, T.3    Wold, M.S.4    Radding, C.M.5
  • 13
    • 0028297545 scopus 로고
    • Functional characterization of residues in the P-loop motif of the RecA protein ATP binding site
    • Konola J. T., Logan K. M., Knight K. L. Functional characterization of residues in the P-loop motif of the RecA protein ATP binding site. J. Mol. Biol. 237:1994;20-34.
    • (1994) J. Mol. Biol. , vol.237 , pp. 20-34
    • Konola, J.T.1    Logan, K.M.2    Knight, K.L.3
  • 14
    • 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. 270:1995;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
  • 15
    • 0019351776 scopus 로고
    • Interaction of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • Kowalczykowski S. C., Lonberg N., Newport J. W., von Hippel P. H. Interaction of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions. J. Mol. Biol. 145:1981;75-104.
    • (1981) J. Mol. Biol. , vol.145 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.H.4
  • 16
    • 0022549616 scopus 로고
    • Cooperative and noncooperative binding of protein ligands to nucleic acid lattices: Experimental approaches to the determination of thermodynamic parameters
    • Kowalczykowski S. C., Paul L. S., Lonberg N., Newport J. W., McSwiggen J. A., von Hippel P. H. Cooperative and noncooperative binding of protein ligands to nucleic acid lattices: experimental approaches to the determination of thermodynamic parameters. Biochemistry. 25:1986;1226-1240.
    • (1986) Biochemistry , vol.25 , pp. 1226-1240
    • Kowalczykowski, S.C.1    Paul, L.S.2    Lonberg, N.3    Newport, J.W.4    McSwiggen, J.A.5    Von Hippel, P.H.6
  • 18
    • 0029909565 scopus 로고    scopus 로고
    • A mutation in mouse rad51 results in an early embryonic lethal that is suppressed by a mutation in p53
    • Lim D.-S., Hasty P. A mutation in mouse rad51 results in an early embryonic lethal that is suppressed by a mutation in p53. Mol. Cell. Biol. 16:1996;7133-7143.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 7133-7143
    • Lim, D.-S.1    Hasty, P.2
  • 19
    • 0019835729 scopus 로고
    • Binding of the recA protein of Escherichia coli to single- And double-stranded DNA
    • McEntee K., Weinstock G. M., 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
  • 20
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee J. D., von Hippel P. H. Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol. 86:1974;469-489.
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Von Hippel, P.H.2
  • 21
    • 0022429092 scopus 로고
    • Interaction of recA protein with single-stranded DNA: Quantitative aspects of binding affinity modulation by nucleotide cofactors
    • Menetski J. P., Kowalczykowski S. C. Interaction of recA protein with single-stranded DNA: quantitative aspects of binding affinity modulation by nucleotide cofactors. J. Mol. Biol. 181:1985;281-295.
    • (1985) J. Mol. Biol. , vol.181 , pp. 281-295
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 22
    • 0033556206 scopus 로고    scopus 로고
    • Role of the conserved lysine 80 in stabilisation of NF-kappaB p50 DNA binding
    • Michalopoulos I., Hays R. T. Role of the conserved lysine 80 in stabilisation of NF-kappaB p50 DNA binding. Nucl. Acids Res. 27:1999;503-509.
    • (1999) Nucl. Acids Res. , vol.27 , pp. 503-509
    • Michalopoulos, I.1    Hays, R.T.2
  • 23
    • 0032535149 scopus 로고    scopus 로고
    • Equilibrium analysis of high affinity interactions using BIACORE
    • Myszka D. G., Jonsen M. D., Graves B. J. Equilibrium analysis of high affinity interactions using BIACORE. Anal. Biochem. 265:1998;326-330.
    • (1998) Anal. Biochem. , vol.265 , pp. 326-330
    • Myszka, D.G.1    Jonsen, M.D.2    Graves, B.J.3
  • 24
    • 0032513226 scopus 로고    scopus 로고
    • Binding of Rad51p to DNA: Interaction of Rad51p with single- And double-stranded DNA
    • Namsaraev E., Berg P. Binding of Rad51p to DNA: interaction of Rad51p with single- and double-stranded DNA. J. Biol. Chem. 273:1998;6177-6182.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6177-6182
    • Namsaraev, E.1    Berg, P.2
  • 25
    • 0032556870 scopus 로고    scopus 로고
    • Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A
    • New J. H., Sugiyama T., Zaitsev E., Kowalczykowski S. C. Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein A. Nature. 391:1998;407-410.
    • (1998) Nature , vol.391 , pp. 407-410
    • New, J.H.1    Sugiyama, T.2    Zaitsev, E.3    Kowalczykowski, S.C.4
  • 27
    • 0027167689 scopus 로고
    • Similarity of the yeast Rad51 filament to the bacterial RecA filament
    • Ogawa T., Yu X., Shinohara A., Egelman E. H. Similarity of the yeast Rad51 filament to the bacterial RecA filament. Science. 259:1993b;1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 28
    • 0028922514 scopus 로고
    • A species-specific interaction of Rad51 and Rad52 proteins in eukaryotes
    • Ogawa T., Shinohara A., Ikeya T. A species-specific interaction of Rad51 and Rad52 proteins in eukaryotes. Advan. Biophys. 31:1995;93-100.
    • (1995) Advan. Biophys. , vol.31 , pp. 93-100
    • Ogawa, T.1    Shinohara, A.2    Ikeya, T.3
  • 29
  • 30
    • 0032492853 scopus 로고    scopus 로고
    • Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins
    • Petukhova G., Stratton S., Sung P. Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins. Nature. 393:1998;91-94.
    • (1998) Nature , vol.393 , pp. 91-94
    • Petukhova, G.1    Stratton, S.2    Sung, P.3
  • 31
    • 0024360742 scopus 로고
    • Helical RecA nucleoprotein filaments mediate homologous pairing and strand exchange
    • Radding C. M. Helical RecA nucleoprotein filaments mediate homologous pairing and strand exchange. Biochim. Biophys. Acta. 1008:1989;131-145.
    • (1989) Biochim. Biophys. Acta , vol.1008 , pp. 131-145
    • Radding, C.M.1
  • 32
    • 0027397313 scopus 로고
    • Alteration of the nucleoside triphosphate (NTP) catalytic domain within the 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 the 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
  • 33
    • 0030633568 scopus 로고    scopus 로고
    • RecA protein: Structure, function, and role in recombinational DNA repair
    • Roca A. I., Cox M. M. RecA protein: structure, function, and role in recombinational DNA repair. Prog. Nucl. Acid Res. Mol. Biol. 56:1997;129-222.
    • (1997) Prog. Nucl. Acid Res. Mol. Biol. , vol.56 , pp. 129-222
    • Roca, A.I.1    Cox, M.M.2
  • 35
    • 0003518480 scopus 로고
    • New York: John Wiley & Sons, Inc. p. 346-385
    • Segel I. H. Enzyme Kinetics. 1975;John Wiley & Sons, Inc. New York. p. 346-385.
    • (1975) Enzyme Kinetics
    • Segel, I.H.1
  • 36
    • 0030047343 scopus 로고    scopus 로고
    • Specific interactions between the human RAD51 and RAD52 proteins
    • Shen Z., Cloud K. G., Chen D. J., Park M. S. Specific interactions between the human RAD51 and RAD52 proteins. J. Biol. Chem. 271:1996;148-152.
    • (1996) J. Biol. Chem. , vol.271 , pp. 148-152
    • Shen, Z.1    Cloud, K.G.2    Chen, D.J.3    Park, M.S.4
  • 37
    • 0032556898 scopus 로고    scopus 로고
    • Stimulation by Rad52 of Rad51-mediated recombination
    • Shinohara A., Ogawa T. Stimulation by Rad52 of Rad51-mediated recombination. Nature. 391:1998;404-407.
    • (1998) Nature , vol.391 , pp. 404-407
    • Shinohara, A.1    Ogawa, T.2
  • 38
    • 0027325816 scopus 로고
    • Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA
    • Shinohara A., Ogawa H., Matsudea Y., Ushio N., Ikeo K., Ogawa T. Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. Nature Genet. 4:1993;239-243.
    • (1993) Nature Genet. , vol.4 , pp. 239-243
    • Shinohara, A.1    Ogawa, H.2    Matsudea, Y.3    Ushio, N.4    Ikeo, K.5    Ogawa, T.6
  • 39
    • 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
  • 40
    • 0021096846 scopus 로고
    • Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxynucleic acid derivative
    • Silver M. S., Fersht A. R. Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxynucleic acid derivative. Biochemistry. 22:1983;2860-2866.
    • (1983) Biochemistry , vol.22 , pp. 2860-2866
    • Silver, M.S.1    Fersht, A.R.2
  • 41
    • 0031004885 scopus 로고    scopus 로고
    • A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein
    • Sugiyama T., Zaitsev E. M., Kowalczykowski S. C. A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem. 272:1997;7940-7945.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7940-7945
    • Sugiyama, T.1    Zaitsev, E.M.2    Kowalczykowski, S.C.3
  • 42
    • 0027978039 scopus 로고
    • Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast Rad51 protein
    • Sung P. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast Rad51 protein. Science. 265:1994;1241-1243.
    • (1994) Science , vol.265 , pp. 1241-1243
    • Sung, P.1
  • 43
    • 0030666945 scopus 로고    scopus 로고
    • Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase
    • Sung P. Function of yeast Rad52 protein as a mediator between replication protein A and the Rad51 recombinase. J. Biol. Chem. 272:1997;28194-28197.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28194-28197
    • Sung, P.1
  • 44
    • 0029112483 scopus 로고
    • DNA strand exchange mediated by a Rad51-ssDNA nucleoprotein filament with polarity opposite to that of RecA
    • Sung P., Robberson D. L. DNA strand exchange mediated by a Rad51-ssDNA nucleoprotein filament with polarity opposite to that of RecA. Cell. 82:1995;453-461.
    • (1995) Cell , vol.82 , pp. 453-461
    • Sung, P.1    Robberson, D.L.2
  • 45
    • 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
  • 47
    • 0029974806 scopus 로고    scopus 로고
    • Homologous DNA pairing by a 20-amino acid peptide derived from RecA
    • Voloshin O. N., Wang L., Camerini-Otero R. D. Homologous DNA pairing by a 20-amino acid peptide derived from RecA. Science. 272:1996;868-872.
    • (1996) Science , vol.272 , pp. 868-872
    • Voloshin, O.N.1    Wang, L.2    Camerini-Otero, R.D.3
  • 48
    • 0019839856 scopus 로고
    • Hydrolysis of nucleoside triphosphates catalyzed by the RecA protein of Escherichia coli
    • Weinstock G. M., McEntee K., Lehman I. R. Hydrolysis of nucleoside triphosphates catalyzed by the RecA protein of Escherichia coli. J. Biol. Chem. 256:1981;8845-8849.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8845-8849
    • Weinstock, G.M.1    McEntee, K.2    Lehman, I.R.3
  • 49
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong I., Lohman T. M. A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions. Proc. Natl Acad. Sci. USA. 90:1993;5438-5432.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5438-5432
    • Wong, I.1    Lohman, T.M.2
  • 52
    • 0033614034 scopus 로고    scopus 로고
    • The DNA binding properties of Saccharomyces cerevisiae Rad51 protein
    • Zaitsev E. M., Zaitsev E. N., Kowalczykowski S. C. The DNA binding properties of Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem. 274:1999;2907-2915.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2907-2915
    • Zaitsev, E.M.1    Zaitsev, E.N.2    Kowalczykowski, S.C.3
  • 53
    • 0027375810 scopus 로고
    • Analysis of two distinct single-stranded DNA binding sites on the recA nucleoprotein filament
    • Zlotnik 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
    • Zlotnik, A.1    Mitchell, R.S.2    Steed, R.K.3    Brenner, S.L.4


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