메뉴 건너뛰기




Volumn 17, Issue 9, 1997, Pages 5359-5368

Characterization of strand exchange activity of yeast Rad51 protein

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA BINDING PROTEIN; DOUBLE STRANDED DNA; GENE PRODUCT; SINGLE STRANDED DNA;

EID: 0030850017     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.9.5359     Document Type: Article
Times cited : (58)

References (43)
  • 1
    • 0026751086 scopus 로고
    • Semidominant suppressors of Srs2 helicase mutations of Saccharomyces cerevisiae map in the RAD51 gene, whose sequence predicts a protein with similarities to procaryotic Reca proteins
    • Aboussekhra, A., R. Chanet, A. Adjiri, and F. Fabre. 1992. Semidominant suppressors of Srs2 helicase mutations of Saccharomyces cerevisiae map in the RAD51 gene, whose sequence predicts a protein with similarities to procaryotic RecA proteins. Mol. Cell. Biol. 12:3224-3234.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3224-3234
    • Aboussekhra, A.1    Chanet, R.2    Adjiri, A.3    Fabre, F.4
  • 2
    • 0026701665 scopus 로고
    • Characterization of DNA-binding and strand-exchange stimulation properties of y-RPA, a yeast single-strand-DNA-hinding protein
    • Alani, E., R. Thresher, J. D. Griffith, and R. D. Kolodner. 1992. Characterization of DNA-binding and strand-exchange stimulation properties of y-RPA, a yeast single-strand-DNA-hinding protein. J. Mol. Biol. 227:54-71.
    • (1992) J. Mol. Biol. , vol.227 , pp. 54-71
    • Alani, E.1    Thresher, R.2    Griffith, J.D.3    Kolodner, R.D.4
  • 3
    • 0026643384 scopus 로고
    • Nucleotide sequence and transcriptional regulation of the yeast recombinational repair gene RAD51
    • Basile, G., M. Aker, and R. K. Mortimer. 1992. Nucleotide sequence and transcriptional regulation of the yeast recombinational repair gene RAD51. Mol. Cell. Biol. 12:3235-3246.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3235-3246
    • Basile, G.1    Aker, M.2    Mortimer, R.K.3
  • 4
    • 0029911725 scopus 로고    scopus 로고
    • Evidence for the coupling of ATP hydrolysis to the final (extension) phase of RecA protein-mediated DNA strand exchange
    • Bedale, W. A., and M. Cox. 1996. Evidence for the coupling of ATP hydrolysis to the final (extension) phase of RecA protein-mediated DNA strand exchange. J. Biol. Chem. 271:5725-5732.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5725-5732
    • Bedale, W.A.1    Cox, M.2
  • 5
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • Benson, F. E., A. Stasiak, and S. C. West. 1994. Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J. 13:5764-5771.
    • (1994) EMBO J. , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 6
    • 0029759341 scopus 로고    scopus 로고
    • Single-stranded DNA binding alters human replication protein a structure and facilitates interaction with DNA-dependent protein kinase
    • Blackwell, L. J., J. A. Borowiec, and I. A. Mastrangelo. 1996. Single-stranded DNA binding alters human replication protein A structure and facilitates interaction with DNA-dependent protein kinase. Mol. Cell. Biol. 16:4798-4807.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4798-4807
    • Blackwell, L.J.1    Borowiec, J.A.2    Mastrangelo, I.A.3
  • 7
    • 0019853508 scopus 로고
    • Directionality and polarity in recA protein-promoted branch migration
    • Cox, M. M., and I. R. Lehman. 1981. Directionality and polarity in recA protein-promoted branch migration. Proc. Natl. Acad. Sci. USA 78:6018-6022.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6018-6022
    • Cox, M.M.1    Lehman, I.R.2
  • 8
    • 0343551289 scopus 로고
    • RecA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange
    • Cox, M. M., and I. R. Lehman. 1981. recA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange. Proc. Natl. Acad. Sci. USA 78:3433-3437.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3433-3437
    • Cox, M.M.1    Lehman, I.R.2
  • 9
    • 0029119967 scopus 로고
    • Complex formation in yeast double-strand break repair: Participation of Rad51, Rad52, Rad55, and Rad57 proteins
    • Hays, S. L., A. A. Firmenich, and P. Berg. 1995. Complex formation in yeast double-strand break repair: participation of Rad51, Rad52, Rad55, and Rad57 proteins. Proc. Natl. Acad. Sci. USA 92:6925-6929.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6925-6929
    • Hays, S.L.1    Firmenich, A.A.2    Berg, P.3
  • 10
    • 85036483933 scopus 로고    scopus 로고
    • Unpublished data
    • Hays, S. L., et al. Unpublished data.
    • Hays, S.L.1
  • 11
    • 0021337860 scopus 로고
    • Role of RecA protein spiral filaments in genetic recombination
    • Howard-Flanders, P., S. C. West, and A. Stasiak. 1984. Role of RecA protein spiral filaments in genetic recombination. Nature 309:215-219.
    • (1984) Nature , vol.309 , pp. 215-219
    • Howard-Flanders, P.1    West, S.C.2    Stasiak, A.3
  • 12
    • 0028131478 scopus 로고
    • On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. III. Unidirectional branch migration and extensive hybrid DNA formation
    • Jain, S. K., M. M. Cox, and R. B. Inman. 1994. On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. III. Unidirectional branch migration and extensive hybrid DNA formation. J. Biol. Chem. 269:20653-20661.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20653-20661
    • Jain, S.K.1    Cox, M.M.2    Inman, R.B.3
  • 14
    • 0027937138 scopus 로고
    • The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation
    • Johnson, A. W., and R. D. Kolodner. 1994. The activity of the Saccharomyces cerevisiae strand exchange protein 1 intrinsic exonuclease during joint molecule formation. J. Biol. Chem. 269:3664-3672.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3664-3672
    • Johnson, A.W.1    Kolodner, R.D.2
  • 15
    • 0025768557 scopus 로고
    • Strand exchange protein 1 from Saccharomyces cerevisiae. A novel multifunctional protein that contains DNA strand exchange and exonuclease activities
    • Johnson, A. W., and R. D. Kolodner. 1991. Strand exchange protein 1 from Saccharomyces cerevisiae. A novel multifunctional protein that contains DNA strand exchange and exonuclease activities. J. Biol. Chem. 266:14046-14054.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14046-14054
    • Johnson, A.W.1    Kolodner, R.D.2
  • 16
    • 0029164962 scopus 로고
    • Functional differences and interactions among the putative RecA homologs Rad51, Rad55, and Rad57
    • Johnson, R. D., and L. S. Symington. 1995. Functional differences and interactions among the putative RecA homologs Rad51, Rad55, and Rad57. Mol. Cell. Biol. 15:4843-4850.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4843-4850
    • Johnson, R.D.1    Symington, L.S.2
  • 17
    • 0027939024 scopus 로고
    • Interactions of human replication protein A with oligonucleotides
    • Kim, C., B. F. Paulus, and M. S. Wold. 1994. Interactions of human replication protein A with oligonucleotides. Biochemistry 33:14197-14206.
    • (1994) Biochemistry , vol.33 , pp. 14197-14206
    • Kim, C.1    Paulus, B.F.2    Wold, M.S.3
  • 18
    • 0026737631 scopus 로고
    • On the role of ATP hydrolysis in Reca protein-mediated DNA strand exchange. I. Bypassing a short heterologous insert in one DNA substrate
    • Kim, J. I., M. M. Cox, and R. B. Inman. 1992. On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. I. Bypassing a short heterologous insert in one DNA substrate. J. Biol. Chem. 267:16438-16443.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16438-16443
    • Kim, J.I.1    Cox, M.M.2    Inman, R.B.3
  • 19
    • 0026688302 scopus 로고
    • ATP hydrolysis and the displaced strand are two factors that determine the polarity of RecA-promoted DNA strand exchange
    • Konforti, B. B., and R. W. Davis. 1992. ATP hydrolysis and the displaced strand are two factors that determine the polarity of RecA-promoted DNA strand exchange. J. Mol. Biol. 227:38-53.
    • (1992) J. Mol. Biol. , vol.227 , pp. 38-53
    • Konforti, B.B.1    Davis, R.W.2
  • 20
    • 0023108585 scopus 로고
    • Effects of the Escherichia coli SSB protein on the binding of Escherichia coli Reca protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction
    • Erratum, 198:359
    • Kowalczykowski, S. C., J. Clow, R. Somani, and A. Varghese. 1987. Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction. J. Mol. Biol. 193:81-95. (Erratum, 198:359.)
    • (1987) J. Mol. Biol. , vol.193 , pp. 81-95
    • Kowalczykowski, S.C.1    Clow, J.2    Somani, R.3    Varghese, A.4
  • 21
    • 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., and R. A. Krupp. 1987. 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. 193:97-113.
    • (1987) J. Mol. Biol. , vol.193 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029762349 scopus 로고    scopus 로고
    • The specificity of the second-ary DNA binding site of RecA protein defines its role in DNA strand exchange
    • Mazin, A. V., and S. C. Kowalczykowski. 1996. The specificity of the second-ary DNA binding site of RecA protein defines its role in DNA strand exchange. Proc. Natl. Acad. Sci. USA 93:10673-10678.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10673-10678
    • Mazin, A.V.1    Kowalczykowski, S.C.2
  • 24
    • 0346660225 scopus 로고
    • Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli
    • McEntee, K., G. M. Weinstock, and I. R. Lehman. 1979. Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli. Proc. Natl. Acad. Sci. USA 76:2615-2619.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2615-2619
    • McEntee, K.1    Weinstock, G.M.2    Lehman, I.R.3
  • 25
    • 0025166577 scopus 로고
    • Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis
    • Menetski, J. P., D. G. Bear, and S. C. Kowalczykowski. 1990. Stable DNA heteroduplex formation catalyzed by the Escherichia coli RecA protein in the absence of ATP hydrolysis. Proc. Natl. Acad. Sci. USA 87:21-25.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 21-25
    • Menetski, J.P.1    Bear, D.G.2    Kowalczykowski, S.C.3
  • 27
    • 0027227980 scopus 로고
    • Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52
    • Milne, G. T., and D. T. Weaver. 1993. Dominant negative alleles of RAD52 reveal a DNA repair/recombination complex including Rad51 and Rad52. Genes Dev. 7:1755-1765.
    • (1993) Genes Dev. , vol.7 , pp. 1755-1765
    • Milne, G.T.1    Weaver, D.T.2
  • 28
    • 0030071197 scopus 로고    scopus 로고
    • Partial purification and characterization of two types of homologous DNA pairing activity from rat testis nuclei
    • Namsaraev, E. A., V. A. Lanzov, and A. T. Akhmedov. 1996. Partial purification and characterization of two types of homologous DNA pairing activity from rat testis nuclei. Biochim. Biophys. Acta 1305:172-180.
    • (1996) Biochim. Biophys. Acta , vol.1305 , pp. 172-180
    • Namsaraev, E.A.1    Lanzov, V.A.2    Akhmedov, A.T.3
  • 29
    • 0027167689 scopus 로고
    • Similarity of the yeast Rad51 filament to the bacterial RecA filament
    • Ogawa, T., X. Yu, A. Shinohara, and E. H. Egelman. 1993. Similarity of the yeast Rad51 filament to the bacterial RecA filament. Science 259:1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 30
    • 0024284762 scopus 로고
    • Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB) 65 binding mode. Cation and anion effects and polynucleotide specificity
    • Overman, L. B., W. Bujalowski, and T. M. Lohman. 1988. Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB) 65 binding mode. Cation and anion effects and polynucleotide specificity. Biochemistry 27:456-471.
    • (1988) Biochemistry , vol.27 , pp. 456-471
    • Overman, L.B.1    Bujalowski, W.2    Lohman, T.M.3
  • 31
    • 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., and S. C. Kowalczykowski. 1993. Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation. J. Biol. Chem. 268:1292-1297.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1292-1297
    • Rehrauer, W.M.1    Kowalczykowski, S.C.2
  • 34
    • 0000133316 scopus 로고
    • Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments
    • Shibata, T., C. DasGupta, R. P. Cunningham, and C. M. Radding. 1979. Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments. Proc. Natl. Acad. Sci. USA 76:1638-1642.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1638-1642
    • Shibata, T.1    Dasgupta, C.2    Cunningham, R.P.3    Radding, C.M.4
  • 35
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • Erratum. 71:180
    • Shinohara, A., H. Ogawa, and T. Ogawa. 1992. Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell 69: 457-470. (Erratum. 71:180.)
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 36
    • 0021219501 scopus 로고
    • RecA protein-promoted DNA strand exchange. Effect of ionic strength
    • Soltis, D. A., and I. R. Lehman. 1984. recA protein-promoted DNA strand exchange. Effect of ionic strength. J. Biol. Chem. 259:12020-12024.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12020-12024
    • Soltis, D.A.1    Lehman, I.R.2
  • 37
    • 0021100339 scopus 로고
    • An unpaired 3′ terminus stimulates recA protein-promoted DNA strand exchange
    • Soltis, D. A., and I. R. Lehman. 1983. An unpaired 3′ terminus stimulates recA protein-promoted DNA strand exchange. J. Biol. Chem. 258:14073-14075.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14073-14075
    • Soltis, D.A.1    Lehman, I.R.2
  • 38
    • 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., E. M. Zaitseva, and S. C. Kowalczykowski. 1997. A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem. 272:7940-7945.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7940-7945
    • Sugiyama, T.1    Zaitseva, E.M.2    Kowalczykowski, S.C.3
  • 39
    • 0027978039 scopus 로고
    • Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein
    • Sung, P. 1994. Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science 265:1241-1243.
    • (1994) Science , vol.265 , pp. 1241-1243
    • Sung, P.1
  • 40
    • 0029112483 scopus 로고
    • DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA
    • Sung, P., and D. L. Robberson. 1995. DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA. Cell 82:453-461.
    • (1995) Cell , vol.82 , pp. 453-461
    • Sung, P.1    Robberson, D.L.2
  • 41
    • 0029953512 scopus 로고    scopus 로고
    • Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis
    • Sung, P., and S. A. Stratton. 1996. Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis. J. Biol. Chem. 271:27983-27986.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27983-27986
    • Sung, P.1    Stratton, S.A.2
  • 42
    • 0020541955 scopus 로고
    • The double-strand-break repair model for recombination
    • Szostak, J. W., T. L. Orr-Weaver, R. J. Rothstein, and F. W. Stahl. 1983. The double-strand-break repair model for recombination. Cell 33:25-35.
    • (1983) Cell , vol.33 , pp. 25-35
    • Szostak, J.W.1    Orr-Weaver, T.L.2    Rothstein, R.J.3    Stahl, F.W.4
  • 43
    • 0024494344 scopus 로고
    • Binding stoichiometry and structure of RecA-DNA complexes studied by flow linear dichroism and fluorescence spectroscopy. Evidence for multiple heterogeneous DNA coordination
    • Takahashi, M., M. Kubista, and B. Norden. 1989. Binding stoichiometry and structure of RecA-DNA complexes studied by flow linear dichroism and fluorescence spectroscopy. Evidence for multiple heterogeneous DNA coordination. J. Mol. Biol. 205:137-147.
    • (1989) J. Mol. Biol. , vol.205 , pp. 137-147
    • Takahashi, M.1    Kubista, M.2    Norden, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.