메뉴 건너뛰기




Volumn 11, Issue 2, 2003, Pages 187-196

ATP-mediated conformational changes in the RecA filament

Author keywords

3D reconstruction; Electron microscopy; Homologous recombination; Image analysis; Rad51; UvsX

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA; NUCLEOTIDE; RECA PROTEIN;

EID: 0037313864     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00003-0     Document Type: Article
Times cited : (133)

References (73)
  • 2
    • 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
  • 3
    • 0024485568 scopus 로고
    • RecA-dependent DNA repair processes
    • Smith K.C., Wang T.C. recA-dependent DNA repair processes. Bioessays. 10:1989;12-16.
    • (1989) Bioessays , vol.10 , pp. 12-16
    • Smith, K.C.1    Wang, T.C.2
  • 4
    • 0017231681 scopus 로고
    • DNA synthesis inhibition and the induction of protein X in Escherichia coli
    • Gudas L.J., Pardee A.B. DNA synthesis inhibition and the induction of protein X in Escherichia coli. J. Mol. Biol. 101:1976;459-477.
    • (1976) J. Mol. Biol. , vol.101 , pp. 459-477
    • Gudas, L.J.1    Pardee, A.B.2
  • 5
    • 0023858526 scopus 로고
    • Function of cloned T4 recombination genes, uvsX and uvsY, in cells of Escherichia coli
    • Minagawa T., Fujisawa H., Yonesaki T., Ryo Y. Function of cloned T4 recombination genes, uvsX and uvsY, in cells of Escherichia coli. Mol. Gen. Genet. 211:1988;350-356.
    • (1988) Mol. Gen. Genet. , vol.211 , pp. 350-356
    • Minagawa, T.1    Fujisawa, H.2    Yonesaki, T.3    Ryo, Y.4
  • 6
    • 0023026267 scopus 로고
    • Purification and characterization of the T4 bacteriophage uvsX protein
    • Formosa T., Alberts B.M. Purification and characterization of the T4 bacteriophage uvsX protein. J. Biol. Chem. 261:1986;6107-6118.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6107-6118
    • Formosa, T.1    Alberts, B.M.2
  • 7
    • 0031034269 scopus 로고    scopus 로고
    • Construction and analysis of a recombination-deficient (radA) mutant of Haloferax volcanii
    • Woods W.G., Dyall-Smith M.L. Construction and analysis of a recombination-deficient (radA) mutant of Haloferax volcanii. Mol. Microbiol. 23:1997;791-797.
    • (1997) Mol. Microbiol. , vol.23 , pp. 791-797
    • Woods, W.G.1    Dyall-Smith, M.L.2
  • 9
    • 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
  • 10
    • 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
  • 11
    • 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
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0027325816 scopus 로고
    • Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA
    • Shinohara A., Ogawa H., Matsuda Y., Ushio N., Ikeo K., Ogawa T. Cloning of human, mouse and fission yeast recombination genes homologous to RAD51 and recA. Nat. Genet. 4:1993;239-243.
    • (1993) Nat. Genet. , vol.4 , pp. 239-243
    • Shinohara, A.1    Ogawa, H.2    Matsuda, Y.3    Ushio, N.4    Ikeo, K.5    Ogawa, T.6
  • 15
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • Abrahams J.P., Leslie A.G., Lutter R., Walker J.E. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria. Nature. 370:1994;621-628.
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.2    Lutter, R.3    Walker, J.E.4
  • 17
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev S., Hsieh J., Gauss G.H., Lohman T.M., Waksman G. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell. 90:1997;635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 18
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya M.R., Guo S., Tabor S., Richardson C.C., Ellenberger T. Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell. 99:1999;167-177.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 19
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M.R., Sawaya M.R., Ellenberger T., Wigley D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell. 101:2000;589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 20
    • 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. Nucleic Acid Res. Mol. Biol. 56:1997;129-223.
    • (1997) Prog. Nucleic Acid Res. Mol. Biol. , vol.56 , pp. 129-223
    • Roca, A.I.1    Cox, M.M.2
  • 21
    • 0030949953 scopus 로고    scopus 로고
    • Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms
    • Brendel V., Brocchieri L., Sandler S.J., Clark A.J., Karlin S. Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms. J. Mol. Evol. 44:1997;528-541.
    • (1997) J. Mol. Evol. , vol.44 , pp. 528-541
    • Brendel, V.1    Brocchieri, L.2    Sandler, S.J.3    Clark, A.J.4    Karlin, S.5
  • 22
    • 0030664070 scopus 로고    scopus 로고
    • An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing
    • Aihara H., Ito Y., Kurumizaka H., Terada T., Yokoyama S., Shibata T. An interaction between a specified surface of the C-terminal domain of RecA protein and double-stranded DNA for homologous pairing. J. Mol. Biol. 274:1997;213-221.
    • (1997) J. Mol. Biol. , vol.274 , pp. 213-221
    • Aihara, H.1    Ito, Y.2    Kurumizaka, H.3    Terada, T.4    Yokoyama, S.5    Shibata, T.6
  • 24
    • 0033538424 scopus 로고    scopus 로고
    • The N-terminal domain of the human Rad51 protein binds DNA: Structure and a DNA binding surface as revealed by NMR
    • Aihara H., Ito Y., Kurumizaka H., Yokoyama S., Shibata T. The N-terminal domain of the human Rad51 protein binds DNA. structure and a DNA binding surface as revealed by NMR J. Mol. Biol. 290:1999;495-504.
    • (1999) J. Mol. Biol. , vol.290 , pp. 495-504
    • Aihara, H.1    Ito, Y.2    Kurumizaka, H.3    Yokoyama, S.4    Shibata, T.5
  • 25
    • 0035914418 scopus 로고    scopus 로고
    • DNA pairing and strand exchange by the Escherichia coli RecA and yeast Rad51 proteins without ATP hydrolysis: On the importance of not getting stuck
    • Rice K.P., Eggler A.L., Sung P., Cox M.M. DNA pairing and strand exchange by the Escherichia coli RecA and yeast Rad51 proteins without ATP hydrolysis. on the importance of not getting stuck J. Biol. Chem. 276:2001;38570-38581.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38570-38581
    • Rice, K.P.1    Eggler, A.L.2    Sung, P.3    Cox, M.M.4
  • 26
    • 0020478259 scopus 로고
    • The helicity of DNA in complexes with RecA protein
    • Stasiak A., DiCapua E. The helicity of DNA in complexes with RecA protein. Nature. 229:1982;185-186.
    • (1982) Nature , vol.229 , pp. 185-186
    • Stasiak, A.1    DiCapua, E.2
  • 27
    • 0019888429 scopus 로고
    • Elongation of duplex DNA by RecA protein
    • Stasiak A., DiCapua E., Koller T. Elongation of duplex DNA by RecA protein. J. Mol. Biol. 151:1981;557-564.
    • (1981) J. Mol. Biol. , vol.151 , pp. 557-564
    • Stasiak, A.1    DiCapua, E.2    Koller, T.3
  • 28
    • 0035812601 scopus 로고    scopus 로고
    • Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently
    • Yang S., VanLoock M.S., Yu X., Egelman E.H. Comparison of bacteriophage T4 UvsX and human Rad51 filaments suggests that RecA-like polymers may have evolved independently. J. Mol. Biol. 312:2001;999-1009.
    • (2001) J. Mol. Biol. , vol.312 , pp. 999-1009
    • Yang, S.1    VanLoock, M.S.2    Yu, X.3    Egelman, E.H.4
  • 29
    • 0027199391 scopus 로고
    • DNA conformation induced by the bacteriophage T4 UvsX protein appears identical to the conformation induced by the Escherichia coli RecA protein
    • Yu X., Egelman E.H. DNA conformation induced by the bacteriophage T4 UvsX protein appears identical to the conformation induced by the Escherichia coli RecA protein. J. Mol. Biol. 232:1993;1-4.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1-4
    • Yu, X.1    Egelman, E.H.2
  • 30
    • 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. 259:1993;1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 32
    • 0028892745 scopus 로고
    • Structural polymorphism of the RecA protein from the thermophilic bacterium Thermus aquaticus
    • Yu X., Angov E., Camerini-Otero R.D., Egelman E.H. Structural polymorphism of the RecA protein from the thermophilic bacterium Thermus aquaticus. Biophys. J. 69:1995;2728-2738.
    • (1995) Biophys. J. , vol.69 , pp. 2728-2738
    • Yu, X.1    Angov, E.2    Camerini-Otero, R.D.3    Egelman, E.H.4
  • 33
    • 0032079749 scopus 로고    scopus 로고
    • RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
    • Seitz E.M., Brockman J.P., Sandler S.J., Clark A.J., Kowalczykowski S.C. RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange. Genes Dev. 12:1998;1248-1253.
    • (1998) Genes Dev. , vol.12 , pp. 1248-1253
    • Seitz, E.M.1    Brockman, J.P.2    Sandler, S.J.3    Clark, A.J.4    Kowalczykowski, S.C.5
  • 34
    • 0032514675 scopus 로고    scopus 로고
    • RecA binding to a single double-stranded DNA molecule: A possible role of DNA conformational fluctuations
    • Leger J.F., Robert J., Bourdieu L., Chatenay D., Marko J.F. RecA binding to a single double-stranded DNA molecule. a possible role of DNA conformational fluctuations Proc. Natl. Acad. Sci. USA. 95:1998;12295-12299.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12295-12299
    • Leger, J.F.1    Robert, J.2    Bourdieu, L.3    Chatenay, D.4    Marko, J.F.5
  • 35
    • 0035827144 scopus 로고    scopus 로고
    • Does a stretched DNA structure dictate the helical geometry of RecA-like filaments?
    • Egelman E.H. Does a stretched DNA structure dictate the helical geometry of RecA-like filaments? J. Mol. Biol. 309:2001;539-542.
    • (2001) J. Mol. Biol. , vol.309 , pp. 539-542
    • Egelman, E.H.1
  • 36
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story R.M., Weber I.T., Steitz T.A. The structure of the E. coli recA protein monomer and polymer. Nature. 355:1992;318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 37
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy. 85:2000;225-234.
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 38
    • 0000668797 scopus 로고
    • Reconstruction of three-dimensional structures from electron micrographs
    • DeRosier D.J., Klug A. Reconstruction of three-dimensional structures from electron micrographs. Nature. 217:1968;130-134.
    • (1968) Nature , vol.217 , pp. 130-134
    • DeRosier, D.J.1    Klug, A.2
  • 39
    • 0035861994 scopus 로고    scopus 로고
    • Archaeal RadA protein binds DNA as both helical filaments and octameric rings
    • Yang S., Yu X., Seitz E.M., Kowalczykowski S.C., Egelman E.H. Archaeal RadA protein binds DNA as both helical filaments and octameric rings. J. Mol. Biol. 314:2001;1077-1085.
    • (2001) J. Mol. Biol. , vol.314 , pp. 1077-1085
    • Yang, S.1    Yu, X.2    Seitz, E.M.3    Kowalczykowski, S.C.4    Egelman, E.H.5
  • 40
    • 0035795407 scopus 로고    scopus 로고
    • Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits
    • Galkin V.E., Orlova A., Lukoyanova N., Wriggers W., Egelman E.H. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J. Cell Biol. 153:2001;75-86.
    • (2001) J. Cell Biol. , vol.153 , pp. 75-86
    • Galkin, V.E.1    Orlova, A.2    Lukoyanova, N.3    Wriggers, W.4    Egelman, E.H.5
  • 41
    • 0037092046 scopus 로고    scopus 로고
    • The utrophin actin-binding domain binds F-actin in two different modes: Implications for the spectrin superfamily of proteins
    • Galkin V.E., Orlova A., VanLoock M.S., Rybakova I.N., Ervasti J.M., Egelman E.H. The utrophin actin-binding domain binds F-actin in two different modes. implications for the spectrin superfamily of proteins J. Cell Biol. 157:2002;243-251.
    • (2002) J. Cell Biol. , vol.157 , pp. 243-251
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Rybakova, I.N.4    Ervasti, J.M.5    Egelman, E.H.6
  • 42
    • 0037006805 scopus 로고    scopus 로고
    • A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure
    • Galkin V.E., VanLoock M.S., Orlova A., Egelman E.H. A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure. Curr. Biol. 12:2002;570-575.
    • (2002) Curr. Biol. , vol.12 , pp. 570-575
    • Galkin, V.E.1    VanLoock, M.S.2    Orlova, A.3    Egelman, E.H.4
  • 45
    • 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
  • 46
    • 0035902614 scopus 로고    scopus 로고
    • Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
    • Yu X., Jacobs S.A., West S.C., Ogawa T., Egelman E.H. Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc. Natl. Acad. Sci. USA. 98:2001;8419-8424.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8419-8424
    • Yu, X.1    Jacobs, S.A.2    West, S.C.3    Ogawa, T.4    Egelman, E.H.5
  • 47
    • 0025783415 scopus 로고
    • Removal of the RecA C-terminus results in a conformational change in the RecA-DNA filament
    • Yu X., Egelman E.H. Removal of the RecA C-terminus results in a conformational change in the RecA-DNA filament. J. Struct. Biol. 106:1991;243-254.
    • (1991) J. Struct. Biol. , vol.106 , pp. 243-254
    • Yu, X.1    Egelman, E.H.2
  • 48
    • 0026527367 scopus 로고
    • C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- and double-stranded DNAs
    • Tateishi S., Horii T., Ogawa T., Ogawa H. C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- and double-stranded DNAs. J. Mol. Biol. 223:1992;115-129.
    • (1992) J. Mol. Biol. , vol.223 , pp. 115-129
    • Tateishi, S.1    Horii, T.2    Ogawa, T.3    Ogawa, H.4
  • 49
    • 0014153487 scopus 로고
    • Prophage induction and filament formation in a mutant strain of Escherichia coli
    • Kirby E.P., Jacob F., Goldthwait D.A. Prophage induction and filament formation in a mutant strain of Escherichia coli. Proc. Natl. Acad. Sci. USA. 58:1967;1903-1910.
    • (1967) Proc. Natl. Acad. Sci. USA , vol.58 , pp. 1903-1910
    • Kirby, E.P.1    Jacob, F.2    Goldthwait, D.A.3
  • 50
    • 0023797024 scopus 로고
    • Biochemical basis of the temperature-inducible constitutive protease activity of the RecA441 protein of Escherichia coli
    • Lavery P.E., Kowalczykowski S.C. Biochemical basis of the temperature-inducible constitutive protease activity of the RecA441 protein of Escherichia coli. J. Mol. Biol. 203:1988;861-874.
    • (1988) J. Mol. Biol. , vol.203 , pp. 861-874
    • Lavery, P.E.1    Kowalczykowski, S.C.2
  • 52
    • 0035949640 scopus 로고    scopus 로고
    • ATP-mediated changes in cross-subunit interactions in the RecA protein
    • Logan K.M., Forget A.L., Verderese J.P., Knight K.L. ATP-mediated changes in cross-subunit interactions in the RecA protein. Biochemistry. 40:2001;11382-11389.
    • (2001) Biochemistry , vol.40 , pp. 11382-11389
    • Logan, K.M.1    Forget, A.L.2    Verderese, J.P.3    Knight, K.L.4
  • 53
    • 0031013231 scopus 로고    scopus 로고
    • The RecA hexamer is a structural homologue of ring helicases
    • Yu X., Egelman E.H. The RecA hexamer is a structural homologue of ring helicases. Nat. Struct. Biol. 4:1997;101-104.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 101-104
    • Yu, X.1    Egelman, E.H.2
  • 54
    • 0030780649 scopus 로고    scopus 로고
    • Local folding of the N-terminal domain of Escherichia coli RecA controls protein-protein interaction
    • Masui R., Mikawa T., Kuramitsu S. Local folding of the N-terminal domain of Escherichia coli RecA controls protein-protein interaction. J. Biol. Chem. 272:1997;27707-27715.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27707-27715
    • Masui, R.1    Mikawa, T.2    Kuramitsu, S.3
  • 55
    • 0035936698 scopus 로고    scopus 로고
    • Crystal structure of the hexameric replicative helicase RepA of plasmid RSF1010
    • Niedenzu T., Roleke D., Bains G., Scherzinger E., Saenger W. Crystal structure of the hexameric replicative helicase RepA of plasmid RSF1010. J. Mol. Biol. 306:2001;479-487.
    • (2001) J. Mol. Biol. , vol.306 , pp. 479-487
    • Niedenzu, T.1    Roleke, D.2    Bains, G.3    Scherzinger, E.4    Saenger, W.5
  • 56
    • 0036671363 scopus 로고    scopus 로고
    • Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form
    • Kagawa W., Kurumizaka H., Ishitani R., Fukai S., Nureki O., Shibata T., Yokoyama S. Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form. Mol. Cell. 10:2002;359-371.
    • (2002) Mol. Cell , vol.10 , pp. 359-371
    • Kagawa, W.1    Kurumizaka, H.2    Ishitani, R.3    Fukai, S.4    Nureki, O.5    Shibata, T.6    Yokoyama, S.7
  • 57
    • 0037015051 scopus 로고    scopus 로고
    • Arrangement of RecA protein in its active filament determined by polarized-light spectroscopy
    • Morimatsu K., Takahashi M., Norden B. Arrangement of RecA protein in its active filament determined by polarized-light spectroscopy. Proc. Natl. Acad. Sci. USA. 99:2002;11688-11693.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11688-11693
    • Morimatsu, K.1    Takahashi, M.2    Norden, B.3
  • 58
    • 0025273606 scopus 로고
    • Image analysis reveals that Escherichia coli RecA protein consists of two domains
    • Yu X., Egelman E.H. Image analysis reveals that Escherichia coli RecA protein consists of two domains. Biophys. J. 57:1990;555-566.
    • (1990) Biophys. J. , vol.57 , pp. 555-566
    • Yu, X.1    Egelman, E.H.2
  • 59
    • 0024999088 scopus 로고
    • Inhibition of recA protein promoted ATP hydrolysis. 1. ATP γ S and ADP are antagonistic inhibitors
    • Lee J.W., Cox M.M. Inhibition of recA protein promoted ATP hydrolysis. 1. ATP γ 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
  • 60
    • 0035838982 scopus 로고    scopus 로고
    • Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites: Implications for the mechanism of rotary catalysis
    • Menz R.I., Walker J.E., Leslie A.G. Structure of bovine mitochondrial F(1)-ATPase with nucleotide bound to all three catalytic sites. implications for the mechanism of rotary catalysis Cell. 106:2001;331-341.
    • (2001) Cell , vol.106 , pp. 331-341
    • Menz, R.I.1    Walker, J.E.2    Leslie, A.G.3
  • 61
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
    • Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell. 94:1998;525-536.
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 62
    • 0028129812 scopus 로고
    • Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli
    • Skiba M.C., Knight K.L. Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli. J. Biol. Chem. 269:1994;3823-3828.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3823-3828
    • Skiba, M.C.1    Knight, K.L.2
  • 63
    • 0033554419 scopus 로고    scopus 로고
    • Intersubunit proximity of residues in the RecA protein as shown by engineered disulfide cross-links
    • Skiba M.C., Logan K.M., Knight K.L. Intersubunit proximity of residues in the RecA protein as shown by engineered disulfide cross-links. Biochemistry. 38:1999;11933-11941.
    • (1999) Biochemistry , vol.38 , pp. 11933-11941
    • Skiba, M.C.1    Logan, K.M.2    Knight, K.L.3
  • 64
    • 0035157386 scopus 로고    scopus 로고
    • Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament
    • De Zutter J.K., Forget A.L., Logan K.M., Knight K.L. Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament. Structure. 9:2001;47-55.
    • (2001) Structure , vol.9 , pp. 47-55
    • De Zutter, J.K.1    Forget, A.L.2    Logan, K.M.3    Knight, K.L.4
  • 65
    • 0027457534 scopus 로고
    • Inactivation of the recA protein by mutation of histidine 97 or lysine 248 at the subunit interface
    • Nguyen T.T., Muench K.A., Bryant F.R. Inactivation of the recA protein by mutation of histidine 97 or lysine 248 at the subunit interface. J. Biol. Chem. 268:1993;3107-3113.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3107-3113
    • Nguyen, T.T.1    Muench, K.A.2    Bryant, F.R.3
  • 66
    • 17544384169 scopus 로고    scopus 로고
    • The DNA binding site(s) of the Escherichia coli RecA protein
    • Rehrauer W.M., Kowalczykowski S.C. The DNA binding site(s) of the Escherichia coli RecA protein. J. Biol. Chem. 271:1996;11996-12002.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11996-12002
    • Rehrauer, W.M.1    Kowalczykowski, S.C.2
  • 67
    • 0033134192 scopus 로고    scopus 로고
    • The mutant RecA proteins, RecAR243Q and RecAK245N, exhibit defective DNA binding in homologous pairing
    • Kurumizaka H., Ikawa S., Sarai A., Shibata T. The mutant RecA proteins, RecAR243Q and RecAK245N, exhibit defective DNA binding in homologous pairing. Arch. Biochem. Biophys. 365:1999;83-91.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 83-91
    • Kurumizaka, H.1    Ikawa, S.2    Sarai, A.3    Shibata, T.4
  • 68
    • 0037177811 scopus 로고    scopus 로고
    • Biochemical characterization of the human RAD51 protein. I. ATP hydrolysis
    • Tombline G., Fishel R. Biochemical characterization of the human RAD51 protein. I. ATP hydrolysis. J. Biol. Chem. 277:2002;14417-14425.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14417-14425
    • Tombline, G.1    Fishel, R.2
  • 69
    • 0033527668 scopus 로고    scopus 로고
    • The hRad51 and RecA proteins show significant differences in cooperative binding to single-stranded DNA
    • De Zutter J.K., Knight K.L. The hRad51 and RecA proteins show significant differences in cooperative binding to single-stranded DNA. J. Mol. Biol. 293:1999;769-780.
    • (1999) J. Mol. Biol. , vol.293 , pp. 769-780
    • De Zutter, J.K.1    Knight, K.L.2
  • 70
    • 0026560474 scopus 로고
    • Direct visualization of dynamics and co-operative conformational changes within RecA filaments that appear to be associated with the hydrolysis of adenosine 5′-O-(3-thiotriphosphate)
    • Yu X., Egelman E.H. Direct visualization of dynamics and co-operative conformational changes within RecA filaments that appear to be associated with the hydrolysis of adenosine 5′-O-(3-thiotriphosphate). J. Mol. Biol. 225:1992;193-216.
    • (1992) J. Mol. Biol. , vol.225 , pp. 193-216
    • Yu, X.1    Egelman, E.H.2
  • 71
    • 0029975088 scopus 로고    scopus 로고
    • Spider and web: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. Spider and web. processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116:1996;190-199.
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 72
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 73
    • 0033119938 scopus 로고    scopus 로고
    • Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
    • Esnouf R.M. Further additions to MolScript version 1.4, including reading and contouring of electron-density maps. Acta Crystallogr. D Biol. Crystallogr. 55:1999;938-940.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 938-940
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.