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Volumn 117, Issue 1, 2004, Pages 47-56

Saccharomyces cerevisiae Mer3 helicase stimulates 3′-5′ heteroduplex extension by Rad51: Implications for crossover control in meiotic recombination

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED DNA; HELICASE; RAD51 PROTEIN; SINGLE STRANDED DNA;

EID: 1842816528     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(04)00294-6     Document Type: Article
Times cited : (90)

References (72)
  • 1
    • 0034697965 scopus 로고    scopus 로고
    • Zip3 provides a link between recombination enzymes and synaptonemal complex proteins
    • Agarwal S., Roeder G.S. Zip3 provides a link between recombination enzymes and synaptonemal complex proteins. Cell. 102:2000;245-255.
    • (2000) Cell , vol.102 , pp. 245-255
    • Agarwal, S.1    Roeder, G.S.2
  • 2
    • 0037334946 scopus 로고    scopus 로고
    • Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein filament
    • Alexeev A., Mazin A., Kowalczykowski S.C. Rad54 protein possesses chromatin-remodeling activity stimulated by the Rad51-ssDNA nucleoprotein filament. Nat. Struct. Biol. 10:2003;182-186.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 182-186
    • Alexeev, A.1    Mazin, A.2    Kowalczykowski, S.C.3
  • 3
    • 0035854342 scopus 로고    scopus 로고
    • Differential timing and control of noncrossover and crossover recombination during meiosis
    • Allers T., Lichten M. Differential timing and control of noncrossover and crossover recombination during meiosis. Cell. 106:2001;47-57.
    • (2001) Cell , vol.106 , pp. 47-57
    • Allers, T.1    Lichten, M.2
  • 4
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco P.R., Tracy R.B., Kowalczykowski S.C. DNA strand exchange proteins. A biochemical and physical comparison Front. Biosci. 3:1998;D570-D603.
    • (1998) Front. Biosci. , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 5
    • 0026697166 scopus 로고
    • DMC1: A meiosis-specific yeast homolog of e. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression
    • Bishop D.K., Park D., Xu L., Kleckner N. DMC1. a meiosis-specific yeast homolog of e. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression Cell. 69:1992;439-456.
    • (1992) Cell , vol.69 , pp. 439-456
    • Bishop, D.K.1    Park, D.2    Xu, L.3    Kleckner, N.4
  • 6
    • 4344582144 scopus 로고    scopus 로고
    • Crossover/noncrossover differentiation, synaptonemal complex formation and regulatory surveillance at the leptotene/zygotene transition of meiosis
    • , this issue
    • Börner G.V., Kleckner N., Hunter N. Crossover/noncrossover differentiation, synaptonemal complex formation and regulatory surveillance at the leptotene/zygotene transition of meiosis. Cell. 117:2004;29-45., this issue.
    • (2004) Cell , vol.117 , pp. 29-45
    • Börner, G.V.1    Kleckner, N.2    Hunter, N.3
  • 7
    • 0032076484 scopus 로고    scopus 로고
    • Zip2, a meiosis-specific protein required for the initiation of chromosome synapsis
    • Chua P.R., Roeder G.S. Zip2, a meiosis-specific protein required for the initiation of chromosome synapsis. Cell. 93:1998;349-359.
    • (1998) Cell , vol.93 , pp. 349-359
    • Chua, P.R.1    Roeder, G.S.2
  • 8
    • 0030910889 scopus 로고    scopus 로고
    • Recombinational repair in yeast: Functional interactions between Rad51 and Rad54 proteins
    • Clever B., Interthal H., Schmuckli-Maurer J., King J., Sigrist M., Heyer W.D. Recombinational repair in yeast. functional interactions between Rad51 and Rad54 proteins EMBO J. 16:1997;2535-2544.
    • (1997) EMBO J. , vol.16 , pp. 2535-2544
    • Clever, B.1    Interthal, H.2    Schmuckli-Maurer, J.3    King, J.4    Sigrist, M.5    Heyer, W.D.6
  • 9
    • 0019853508 scopus 로고
    • Directionality and polarity in recA protein-promoted branch migration
    • Cox M.M., Lehman I.R. Directionality and polarity in recA protein-promoted branch migration. Proc. Natl. Acad. Sci. USA. 78:1981;6018-6022.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6018-6022
    • Cox, M.M.1    Lehman, I.R.2
  • 10
    • 0037131257 scopus 로고    scopus 로고
    • The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein a
    • Eggler A.L., Inman R.B., Cox M.M. The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A. J. Biol. Chem. 277:2002;39280-39288.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39280-39288
    • Eggler, A.L.1    Inman, R.B.2    Cox, M.M.3
  • 11
    • 0021944555 scopus 로고
    • RecA protein rapidly crystallizes in the presence of spermidine: A valuable step in its purification and physical characterization
    • Griffith J., Shores C.G. RecA protein rapidly crystallizes in the presence of spermidine. A valuable step in its purification and physical characterization Biochemistry. 24:1985;158-162.
    • (1985) Biochemistry , vol.24 , pp. 158-162
    • Griffith, J.1    Shores, C.G.2
  • 12
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • Harmon F.G., Kowalczykowski S.C. RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination. Genes Dev. 12:1998;1134-1144.
    • (1998) Genes Dev. , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 13
    • 0029119967 scopus 로고
    • Complex formation in yeast double-strand break repair: Participation of Rad51, Rad52, Rad55, and Rad57 proteins
    • Hays S.L., Firmenich A.A., Berg P. Complex formation in yeast double-strand break repair. participation of Rad51, Rad52, Rad55, and Rad57 proteins Proc. Natl. Acad. Sci. USA. 92:1995;6925-6929.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6925-6929
    • Hays, S.L.1    Firmenich, A.A.2    Berg, P.3
  • 14
    • 0029145505 scopus 로고
    • MSH5, a novel MutS homolog, facilitates meiotic reciprocal recombination between homologs in Saccharomyces cerevisiae but not mismatch repair
    • Hollingsworth N.M., Ponte L., Halsey C. MSH5, a novel MutS homolog, facilitates meiotic reciprocal recombination between homologs in Saccharomyces cerevisiae but not mismatch repair. Genes Dev. 9:1995;1728-1739.
    • (1995) Genes Dev. , vol.9 , pp. 1728-1739
    • Hollingsworth, N.M.1    Ponte, L.2    Halsey, C.3
  • 15
    • 0035834743 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA
    • Hong E.L., Shinohara A., Bishop D.K. Saccharomyces cerevisiae Dmc1 protein promotes renaturation of single-strand DNA (ssDNA) and assimilation of ssDNA into homologous super-coiled duplex DNA. J. Biol. Chem. 276:2001;41906-41912.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41906-41912
    • Hong, E.L.1    Shinohara, A.2    Bishop, D.K.3
  • 16
    • 0030906684 scopus 로고    scopus 로고
    • Mlh1 is unique among mismatch repair proteins in its ability to promote crossing-over during meiosis
    • Hunter N., Borts R.H. Mlh1 is unique among mismatch repair proteins in its ability to promote crossing-over during meiosis. Genes Dev. 11:1997;1573-1582.
    • (1997) Genes Dev. , vol.11 , pp. 1573-1582
    • Hunter, N.1    Borts, R.H.2
  • 17
    • 0035854362 scopus 로고    scopus 로고
    • The single-end invasion: An asymmetric intermediate at the double-strand break to double-holliday junction transition of meiotic recombination
    • Hunter N., Kleckner N. The single-end invasion. an asymmetric intermediate at the double-strand break to double-holliday junction transition of meiotic recombination Cell. 106:2001;59-70.
    • (2001) Cell , vol.106 , pp. 59-70
    • Hunter, N.1    Kleckner, N.2
  • 19
  • 20
    • 0030893115 scopus 로고    scopus 로고
    • Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family
    • Keeney S., Giroux C.N., Kleckner N. Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family. Cell. 88:1997;375-384.
    • (1997) Cell , vol.88 , pp. 375-384
    • Keeney, S.1    Giroux, C.N.2    Kleckner, N.3
  • 21
    • 0033918538 scopus 로고    scopus 로고
    • EXO1 and MSH4 differentially affect crossing-over and segregation
    • Khazanehdari K.A., Borts R.H. EXO1 and MSH4 differentially affect crossing-over and segregation. Chromosoma. 109:2000;94-102.
    • (2000) Chromosoma , vol.109 , pp. 94-102
    • Khazanehdari, K.A.1    Borts, R.H.2
  • 22
    • 0034533703 scopus 로고    scopus 로고
    • Decreased meiotic intergenic recombination and increased meiosis I nondisjunction in exo1 mutants of Saccharomyces cerevisiae
    • Kirkpatrick D.T., Ferguson J.R., Petes T.D., Symington L.S. Decreased meiotic intergenic recombination and increased meiosis I nondisjunction in exo1 mutants of Saccharomyces cerevisiae. Genetics. 156:2000;1549-1557.
    • (2000) Genetics , vol.156 , pp. 1549-1557
    • Kirkpatrick, D.T.1    Ferguson, J.R.2    Petes, T.D.3    Symington, L.S.4
  • 23
    • 0029775620 scopus 로고    scopus 로고
    • Meiosis: How could it work?
    • Kleckner N. Meiosis. how could it work? Proc. Natl. Acad. Sci. USA. 93:1996;8167-8174.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8167-8174
    • Kleckner, N.1
  • 24
    • 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
    • Kowalczykowski S.C., Clow J.C., Somani R., Varghese A. 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. 193:1987;81-95.
    • (1987) J. Mol. Biol. , vol.193 , pp. 81-95
    • Kowalczykowski, S.C.1    Clow, J.C.2    Somani, R.3    Varghese, A.4
  • 27
    • 0032493889 scopus 로고    scopus 로고
    • Saccharomyces Ku70, mre11/rad50 and RPA proteins regulate adaptation to G2/M arrest after DNA damage
    • Lee S.E., Moore J.K., Holmes A., Umezu K., Kolodner R.D., Haber J.E. Saccharomyces Ku70, mre11/rad50 and RPA proteins regulate adaptation to G2/M arrest after DNA damage. Cell. 94:1998;399-409.
    • (1998) Cell , vol.94 , pp. 399-409
    • Lee, S.E.1    Moore, J.K.2    Holmes, A.3    Umezu, K.4    Kolodner, R.D.5    Haber, J.E.6
  • 29
    • 0034161571 scopus 로고    scopus 로고
    • Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing
    • b
    • Mazin A.V., Zaitseva E., Sung P., Kowalczykowski S.C. Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing. EMBO J. 19:2000;1148-1156. b.
    • (2000) EMBO J. , vol.19 , pp. 1148-1156
    • Mazin, A.V.1    Zaitseva, E.2    Sung, P.3    Kowalczykowski, S.C.4
  • 30
    • 0037900075 scopus 로고    scopus 로고
    • A novel function of Rad54 protein. Stabilization of the Rad51 nucleoprotein filament
    • Mazin A.V., Alexeev A.A., Kowalczykowski S.C. A novel function of Rad54 protein. Stabilization of the Rad51 nucleoprotein filament. J. Biol. Chem. 278:2003;14029-14036.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14029-14036
    • Mazin, A.V.1    Alexeev, A.A.2    Kowalczykowski, S.C.3
  • 31
    • 0038628984 scopus 로고    scopus 로고
    • Biochemical basis of the constitutive coprotease activity of RecA P67W protein
    • Mirshad J.K., Kowalczykowski S.C. Biochemical basis of the constitutive coprotease activity of RecA P67W protein. Biochemistry. 42:2003;5937-5944.
    • (2003) Biochemistry , vol.42 , pp. 5937-5944
    • Mirshad, J.K.1    Kowalczykowski, S.C.2
  • 32
    • 0030623351 scopus 로고    scopus 로고
    • Involvement of the MRE2 gene of yeast in formation of meiosis-specific double-strand breaks and crossover recombination through RNA splicing
    • Nakagawa T., Ogawa H. Involvement of the MRE2 gene of yeast in formation of meiosis-specific double-strand breaks and crossover recombination through RNA splicing. Genes Cells. 2:1997;65-79.
    • (1997) Genes Cells , vol.2 , pp. 65-79
    • Nakagawa, T.1    Ogawa, H.2
  • 33
    • 0033569945 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae MER3 gene, encoding a novel helicase-like protein, is required for crossover control in meiosis
    • Nakagawa T., Ogawa H. The Saccharomyces cerevisiae MER3 gene, encoding a novel helicase-like protein, is required for crossover control in meiosis. EMBO J. 18:1999;5714-5723.
    • (1999) EMBO J. , vol.18 , pp. 5714-5723
    • Nakagawa, T.1    Ogawa, H.2
  • 34
    • 0037008675 scopus 로고    scopus 로고
    • The MER3 DNA helicase catalyzes the unwinding of Holliday junctions
    • a
    • Nakagawa T., Kolodner R.D. The MER3 DNA helicase catalyzes the unwinding of Holliday junctions. J. Biol. Chem. 277:2002;28019-28024. a.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28019-28024
    • Nakagawa, T.1    Kolodner, R.D.2
  • 35
    • 0036240334 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Mer3 is a DNA helicase involved in meiotic crossing over
    • b
    • Nakagawa T., Kolodner R.D. Saccharomyces cerevisiae Mer3 is a DNA helicase involved in meiotic crossing over. Mol. Cell. Biol. 22:2002;3281-3291. b.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3281-3291
    • Nakagawa, T.1    Kolodner, R.D.2
  • 36
    • 0033453220 scopus 로고    scopus 로고
    • Multiple functions of MutS- and MutL-related heterocomplexes
    • Nakagawa T., Datta A., Kolodner R.D. Multiple functions of MutS- and MutL-related heterocomplexes. Proc. Natl. Acad. Sci. USA. 96:1999;14186-14188.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14186-14188
    • Nakagawa, T.1    Datta, A.2    Kolodner, R.D.3
  • 37
    • 0035943723 scopus 로고    scopus 로고
    • The MER3 helicase involved in meiotic crossing over is stimulated by single-stranded DNA-binding proteins and unwinds DNA in the 3′ to 5′ direction
    • Nakagawa T., Flores-Rozas H., Kolodner R.D. The MER3 helicase involved in meiotic crossing over is stimulated by single-stranded DNA-binding proteins and unwinds DNA in the 3′ to 5′ direction. J. Biol. Chem. 276:2001;31487-31493.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31487-31493
    • Nakagawa, T.1    Flores-Rozas, H.2    Kolodner, R.D.3
  • 38
    • 0030850017 scopus 로고    scopus 로고
    • Characterization of strand exchange activity of yeast Rad51 protein
    • Namsaraev E., Berg P. Characterization of strand exchange activity of yeast Rad51 protein. Mol. Cell. Biol. 17:1997;5359-5368.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5359-5368
    • Namsaraev, E.1    Berg, P.2
  • 39
    • 0032169410 scopus 로고    scopus 로고
    • Branch migration during Rad51-promoted strand exchange proceeds in either direction
    • Namsaraev E.A., Berg P. Branch migration during Rad51-promoted strand exchange proceeds in either direction. Proc. Natl. Acad. Sci. USA. 95:1998;10477-10481.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10477-10481
    • Namsaraev, E.A.1    Berg, P.2
  • 40
    • 0034635469 scopus 로고    scopus 로고
    • Rad51 uses one mechanism to drive DNA strand exchange in both directions
    • Namsaraev E.A., Berg P. Rad51 uses one mechanism to drive DNA strand exchange in both directions. J. Biol. Chem. 275:2000;3970-3976.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3970-3976
    • Namsaraev, E.A.1    Berg, P.2
  • 41
    • 0037135538 scopus 로고    scopus 로고
    • Rad52 protein has a second stimulatory role in DNA strand exchange that complements replication protein-A function
    • New J.H., Kowalczykowski S.C. Rad52 protein has a second stimulatory role in DNA strand exchange that complements replication protein-A function. J. Biol. Chem. 277:2002;26171-26176.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26171-26176
    • New, J.H.1    Kowalczykowski, S.C.2
  • 42
    • 0032556870 scopus 로고    scopus 로고
    • Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein a
    • New J.H., Sugiyama T., Zaitseva 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    Zaitseva, E.3    Kowalczykowski, S.C.4
  • 44
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae
    • Pâques F., Haber J.E. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63:1999;349-404.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 349-404
    • Pâques, F.1    Haber, J.E.2
  • 45
    • 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
  • 46
    • 0032832810 scopus 로고    scopus 로고
    • Yeast Rad54 promotes Rad51-dependent homologous DNA pairing via ATP hydrolysis-driven change in DNA double helix conformation
    • Petukhova G., Van Komen S., Vergano S., Klein H., Sung P. Yeast Rad54 promotes Rad51-dependent homologous DNA pairing via ATP hydrolysis-driven change in DNA double helix conformation. J. Biol. Chem. 274:1999;29453-29462.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29453-29462
    • Petukhova, G.1    Van Komen, S.2    Vergano, S.3    Klein, H.4    Sung, P.5
  • 47
    • 0030767256 scopus 로고    scopus 로고
    • Meiotic chromosomes: It takes two to tango
    • Roeder G.S. Meiotic chromosomes. it takes two to tango Genes Dev. 11:1997;2600-2621.
    • (1997) Genes Dev. , vol.11 , pp. 2600-2621
    • Roeder, G.S.1
  • 48
    • 0028560427 scopus 로고
    • Mutation of a meiosis-specific MutS homolog decreases crossing over but not mismatch correction
    • Ross-Macdonald P., Roeder G.S. Mutation of a meiosis-specific MutS homolog decreases crossing over but not mismatch correction. Cell. 79:1994;1069-1080.
    • (1994) Cell , vol.79 , pp. 1069-1080
    • Ross-Macdonald, P.1    Roeder, G.S.2
  • 49
    • 0029048915 scopus 로고
    • Phage T4 homologous strand exchange: A DNA helicase, not the strand transferase, drives polar branch migration
    • Salinas F., Kodadek T. Phage T4 homologous strand exchange. a DNA helicase, not the strand transferase, drives polar branch migration Cell. 82:1995;111-119.
    • (1995) Cell , vol.82 , pp. 111-119
    • Salinas, F.1    Kodadek, T.2
  • 50
    • 0028178793 scopus 로고
    • Identification of joint molecules that form frequently between homologs but rarely between sister chromatids during yeast meiosis
    • Schwacha A., Kleckner N. Identification of joint molecules that form frequently between homologs but rarely between sister chromatids during yeast meiosis. Cell. 76:1994;51-63.
    • (1994) Cell , vol.76 , pp. 51-63
    • Schwacha, A.1    Kleckner, N.2
  • 51
    • 0032556898 scopus 로고    scopus 로고
    • Stimulation by Rad52 of yeast Rad51-mediated recombination
    • Shinohara A., Ogawa T. Stimulation by Rad52 of yeast Rad51-mediated recombination. Nature. 391:1998;404-407.
    • (1998) Nature , vol.391 , pp. 404-407
    • Shinohara, A.1    Ogawa, T.2
  • 52
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • Shinohara A., Ogawa H., Ogawa T. Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell. 69:1992;457-470.
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 53
    • 0031242008 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae recA homologues RAD51 and DMC1 have both distinct and overlapping roles in meiotic recombination
    • Shinohara A., Gasior S., Ogawa T., Kleckner N., Bishop D.K. Saccharomyces cerevisiae recA homologues RAD51 and DMC1 have both distinct and overlapping roles in meiotic recombination. Genes Cells. 2:1997;615-629.
    • (1997) Genes Cells , vol.2 , pp. 615-629
    • Shinohara, A.1    Gasior, S.2    Ogawa, T.3    Kleckner, N.4    Bishop, D.K.5
  • 54
    • 0031902872 scopus 로고    scopus 로고
    • Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing
    • Shinohara A., Shinohara M., Ohta T., Matsuda S., Ogawa T. Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing. Genes Cells. 3:1998;145-156.
    • (1998) Genes Cells , vol.3 , pp. 145-156
    • Shinohara, A.1    Shinohara, M.2    Ohta, T.3    Matsuda, S.4    Ogawa, T.5
  • 55
    • 0035937811 scopus 로고    scopus 로고
    • Basis for avid homologous DNA strand exchange by human Rad51 and RPA
    • Sigurdsson S., Trujillo K., Song B., Stratton S., Sung P. Basis for avid homologous DNA strand exchange by human Rad51 and RPA. J. Biol. Chem. 276:2001;8798-8806.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8798-8806
    • Sigurdsson, S.1    Trujillo, K.2    Song, B.3    Stratton, S.4    Sung, P.5
  • 56
    • 0035902510 scopus 로고    scopus 로고
    • Rad54 protein stimulates the postsynaptic phase of Rad51 protein-mediated DNA strand exchange
    • Solinger J.A., Heyer W.D. Rad54 protein stimulates the postsynaptic phase of Rad51 protein-mediated DNA strand exchange. Proc. Natl. Acad. Sci. USA. 98:2001;8447-8453.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8447-8453
    • Solinger, J.A.1    Heyer, W.D.2
  • 57
    • 0035853277 scopus 로고    scopus 로고
    • Rad54 protein stimulates heteroduplex DNA formation in the synaptic phase of DNA strand exchange via specific interactions with the presynaptic Rad51 nucleoprotein filament
    • Solinger J.A., Lutz G., Sugiyama T., Kowalczykowski S.C., Heyer W.D. Rad54 protein stimulates heteroduplex DNA formation in the synaptic phase of DNA strand exchange via specific interactions with the presynaptic Rad51 nucleoprotein filament. J. Mol. Biol. 307:2001;1207-1221.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1207-1221
    • Solinger, J.A.1    Lutz, G.2    Sugiyama, T.3    Kowalczykowski, S.C.4    Heyer, W.D.5
  • 58
    • 0036864703 scopus 로고    scopus 로고
    • Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments
    • Solinger J.A., Kiianitsa K., Heyer W.D. Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments. Mol. Cell. 10:2002;1175-1188.
    • (2002) Mol. Cell , vol.10 , pp. 1175-1188
    • Solinger, J.A.1    Kiianitsa, K.2    Heyer, W.D.3
  • 59
    • 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., Zaitseva 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    Zaitseva, E.M.2    Kowalczykowski, S.C.3
  • 60
    • 0032568595 scopus 로고    scopus 로고
    • DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein a and single-stranded DNA
    • Sugiyama T., New J.H., Kowalczykowski S.C. DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA. Proc. Natl. Acad. Sci. USA. 95:1998;6049-6054.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6049-6054
    • Sugiyama, T.1    New, J.H.2    Kowalczykowski, S.C.3
  • 61
    • 0026019344 scopus 로고
    • Extensive 3′-overhanging, single-stranded DNA associated with the meiosis-specific double-strand breaks at the ARG4 recombination initiation site
    • Sun H., Treco D., Szostak J.W. Extensive 3′-overhanging, single-stranded DNA associated with the meiosis-specific double-strand breaks at the ARG4 recombination initiation site. Cell. 64:1991;1155-1161.
    • (1991) Cell , vol.64 , pp. 1155-1161
    • Sun, H.1    Treco, D.2    Szostak, J.W.3
  • 62
    • 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
  • 63
    • 0030995362 scopus 로고    scopus 로고
    • Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein a to promote DNA strand exchange by Rad51 recombinase
    • Sung P. Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein A to promote DNA strand exchange by Rad51 recombinase. Genes Dev. 11:1997;1111-1121.
    • (1997) Genes Dev. , vol.11 , pp. 1111-1121
    • Sung, P.1
  • 64
    • 0034733599 scopus 로고    scopus 로고
    • Recombination factors of Saccharomyces cerevisiae
    • Sung P., Trujillo K.M., Van Komen S. Recombination factors of Saccharomyces cerevisiae. Mutat. Res. 451:2000;257-275.
    • (2000) Mutat. Res. , vol.451 , pp. 257-275
    • Sung, P.1    Trujillo, K.M.2    Van Komen, S.3
  • 65
    • 0027502061 scopus 로고
    • ZIP1 is a synaptonemal complex protein required for meiotic chromosome synapsis
    • Sym M., Engebrecht J.A., Roeder G.S. ZIP1 is a synaptonemal complex protein required for meiotic chromosome synapsis. Cell. 72:1993;365-378.
    • (1993) Cell , vol.72 , pp. 365-378
    • Sym, M.1    Engebrecht, J.A.2    Roeder, G.S.3
  • 67
    • 0033915812 scopus 로고    scopus 로고
    • Exo1 roles for repair of DNA double-strand breaks and meiotic crossing over in Saccharomyces cerevisiae
    • Tsubouchi H., Ogawa H. Exo1 roles for repair of DNA double-strand breaks and meiotic crossing over in Saccharomyces cerevisiae. Mol. Biol. Cell. 11:2000;2221-2233.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2221-2233
    • Tsubouchi, H.1    Ogawa, H.2
  • 68
    • 0037113947 scopus 로고    scopus 로고
    • Functional cross-talk among Rad51, Rad54, and replication protein a in heteroduplex DNA joint formation
    • Van Komen S., Petukhova G., Sigurdsson S., Sung P. Functional cross-talk among Rad51, Rad54, and replication protein A in heteroduplex DNA joint formation. J. Biol. Chem. 277:2002;43578-43587.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43578-43587
    • Van Komen, S.1    Petukhova, G.2    Sigurdsson, S.3    Sung, P.4
  • 69
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute X., Jeusset J., Soustelle C., Kowalczykowski S.C., Le Cam E., Fabre F. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments. Nature. 423:2003;309-312.
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 70
    • 0033598817 scopus 로고    scopus 로고
    • Functional specificity of MutL homologs in yeast: Evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction
    • Wang T.F., Kleckner N., Hunter N. Functional specificity of MutL homologs in yeast. evidence for three Mlh1-based heterocomplexes with distinct roles during meiosis in recombination and mismatch correction Proc. Natl. Acad. Sci. USA. 96:1999;13914-13919.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13914-13919
    • Wang, T.F.1    Kleckner, N.2    Hunter, N.3
  • 71
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West S.C. Molecular views of recombination proteins and their control. Nat. Rev. Mol. Cell Biol. 4:2003;435-445.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 435-445
    • West, S.C.1
  • 72
    • 0033614034 scopus 로고    scopus 로고
    • The DNA binding properties of Saccharomyces cerevisiae Rad51 protein
    • Zaitseva 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
    • Zaitseva, E.M.1    Zaitsev, E.N.2    Kowalczykowski, S.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.