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Volumn 284, Issue 2, 1998, Pages 385-400

A synthetic Holliday junction is sandwiched between two tetrameric Mycobacterium leprae RuvA structures in solution: New insights from neutron scattering contrast variation and modelling

Author keywords

Holliday junction; Molecular modelling; Neutron scattering; Recombination; RuvA

Indexed keywords

BACTERIAL PROTEIN; DEUTERIUM OXIDE; MAGNESIUM ION; TETRAMER;

EID: 0032573536     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2177     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses
    • Ashton A.W., Boehm M.K., Gallimore J.R., Pepys M.B., Perkins S.J. Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses. J. Mol. Biol. 272:1997;408-422
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 2
    • 0030596495 scopus 로고    scopus 로고
    • Extended glycoprotein structure of the seven domains in human carcinoembryonic antigen by X-ray and neutron solution scattering and an automated curve fitting procedure: Implications for cellular adhesion
    • Boehm M.K., Mayans M.O., Thornton J.D., Begent R.H.J., Keep P.A., Perkins S.J. Extended glycoprotein structure of the seven domains in human carcinoembryonic antigen by X-ray and neutron solution scattering and an automated curve fitting procedure implications for cellular adhesion. J. Mol. Biol. 259:1996;718-736
    • (1996) J. Mol. Biol. , vol.259 , pp. 718-736
    • Boehm, M.K.1    Mayans, M.O.2    Thornton, J.D.3    Begent, R.H.J.4    Keep, P.A.5    Perkins, S.J.6
  • 3
    • 0026640147 scopus 로고
    • HPLC purification of synthetic DNA
    • Brown T., Brown D.J.S. HPLC purification of synthetic DNA. Methods Enzymol. 211:1992;20-35
    • (1992) Methods Enzymol. , vol.211 , pp. 20-35
    • Brown, T.1    Brown, D.J.S.2
  • 4
    • 0026331068 scopus 로고
    • Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins
    • Dunderdale H.J., Benson F.E., Parsons C.A., Sharples G.J., Lloyd R.G., West S.C. Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins. Nature. 354:1991;506-510
    • (1991) Nature , vol.354 , pp. 506-510
    • Dunderdale, H.J.1    Benson, F.E.2    Parsons, C.A.3    Sharples, G.J.4    Lloyd, R.G.5    West, S.C.6
  • 5
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • Egelman E.H., Yu X., Wild R., Hingorani M.M., Patel S.S. Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases. Proc. Natl Acad. Sci. USA. 92:1995;3869-3873
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3869-3873
    • Egelman, E.H.1    Yu, X.2    Wild, R.3    Hingorani, M.M.4    Patel, S.S.5
  • 6
    • 0030727120 scopus 로고    scopus 로고
    • In vitro reconstitution of the late steps of genetic recombination in E. coli
    • Eggleston A.K., Mitchell A.H., West S.C. In vitro reconstitution of the late steps of genetic recombination in E. coli. Cell. 89:1997;607-617
    • (1997) Cell , vol.89 , pp. 607-617
    • Eggleston, A.K.1    Mitchell, A.H.2    West, S.C.3
  • 10
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522-524
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 12
    • 0026482604 scopus 로고
    • Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration
    • Iwasaki H., Takahagi M., Nakata A., Shinagawa H. Escherichia coli RuvA and RuvB proteins specifically interact with Holliday junctions and promote branch migration. Genes Dev. 6:1992;2214-2220
    • (1992) Genes Dev. , vol.6 , pp. 2214-2220
    • Iwasaki, H.1    Takahagi, M.2    Nakata, A.3    Shinagawa, H.4
  • 13
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • Jacrot B., Zaccai G. Determination of molecular weight by neutron scattering. Biopolymers. 20:1981;2413-2426
    • (1981) Biopolymers , vol.20 , pp. 2413-2426
    • Jacrot, B.1    Zaccai, G.2
  • 14
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure pattern recognition of hydrogen-bonded and geometrical features. Biopolymers. 22:1983;2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 17
    • 44049114919 scopus 로고
    • Upgrading of the SANS instrument D11 at the ILL
    • Lindner P., May R.P., Timmins P.A. Upgrading of the SANS instrument D11 at the ILL. Physica B. 180:1992;967-972
    • (1992) Physica B , vol.180 , pp. 967-972
    • Lindner, P.1    May, R.P.2    Timmins, P.A.3
  • 18
    • 0029871788 scopus 로고    scopus 로고
    • Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82
    • Mahdi A.A., Sharples G.J., Mandal T.N., Lloyd R.G. Holliday junction resolvases encoded by homologous rusA genes in Escherichia coli K-12 and phage 82. J. Mol. Biol. 257:1996;561-573
    • (1996) J. Mol. Biol. , vol.257 , pp. 561-573
    • Mahdi, A.A.1    Sharples, G.J.2    Mandal, T.N.3    Lloyd, R.G.4
  • 19
    • 0027236687 scopus 로고
    • Resolution of Holliday intermediates in recombination and DNA repair: Indirect suppression of ruvA, ruvB, and ruvC mutations
    • Mandal T.N., Mahdi A.A., Sharples G.J., Lloyd R.G. Resolution of Holliday intermediates in recombination and DNA repair indirect suppression of ruvA, ruvB, and ruvC mutations. J. Bacteriol. 175:1993;4325-4334
    • (1993) J. Bacteriol. , vol.175 , pp. 4325-4334
    • Mandal, T.N.1    Mahdi, A.A.2    Sharples, G.J.3    Lloyd, R.G.4
  • 20
    • 0024550638 scopus 로고
    • ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication
    • Mastrangelo I.A., Hough P.V.C., Wall J.S., Dobson M., Dean F.B., Hurwitz J. ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication. Nature. 338:1989;658-662
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1    Hough, P.V.C.2    Wall, J.S.3    Dobson, M.4    Dean, F.B.5    Hurwitz, J.6
  • 21
    • 0029131402 scopus 로고
    • Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar
    • Mayans M.O., Coadwell W.J., Beale D., Symons D.B.A., Perkins S.J. Demonstration by pulsed neutron scattering that the arrangement of the Fab and Fc fragments in the overall structures of bovine IgG1 and IgG2 in solution is similar. Biochem. J. 311:1995;283-291
    • (1995) Biochem. J. , vol.311 , pp. 283-291
    • Mayans, M.O.1    Coadwell, W.J.2    Beale, D.3    Symons, D.B.A.4    Perkins, S.J.5
  • 22
    • 0028170790 scopus 로고
    • Hexameric rings of Escherichia coli RuvB protein: Cooperative assembly, processivity and ATPase activity
    • Mitchell A.H., West S.C. Hexameric rings of Escherichia coli RuvB protein cooperative assembly, processivity and ATPase activity. J. Mol. Biol. 243:1994;208-215
    • (1994) J. Mol. Biol. , vol.243 , pp. 208-215
    • Mitchell, A.H.1    West, S.C.2
  • 23
    • 0027184479 scopus 로고
    • Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins: II. Interaction of RuvB with DNA
    • Muller B., Tsaneva I.R., West S.C. Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins II. Interaction of RuvB with DNA. J. Biol. Chem. 268:1993;17185-17189
    • (1993) J. Biol. Chem. , vol.268 , pp. 17185-17189
    • Muller, B.1    Tsaneva, I.R.2    West, S.C.3
  • 24
    • 0032518238 scopus 로고    scopus 로고
    • Functional analysis of the domain structure in the Holliday junction binding protein RuvA
    • Nishino T., Ariyoshi M., Iwasaki H., Shinagawa H., Morikawa K. Functional analysis of the domain structure in the Holliday junction binding protein RuvA. Structure. 6:1998;11-21
    • (1998) Structure , vol.6 , pp. 11-21
    • Nishino, T.1    Ariyoshi, M.2    Iwasaki, H.3    Shinagawa, H.4    Morikawa, K.5
  • 25
    • 0032518183 scopus 로고    scopus 로고
    • Holliday junction resolvase in Schizosaccharomyces pombe has identical endonuclease activity to the CCE1 homologue YDC2
    • Oram M., Keeley A., Tsaneva I.R. Holliday junction resolvase in Schizosaccharomyces pombe has identical endonuclease activity to the CCE1 homologue YDC2. Nucl. Acids Res. 26:1998;594-601
    • (1998) Nucl. Acids Res. , vol.26 , pp. 594-601
    • Oram, M.1    Keeley, A.2    Tsaneva, I.R.3
  • 26
    • 0027261464 scopus 로고
    • Formation of a RuvAB-Holliday junction complex in vitro
    • Parsons C.A., West S.C. Formation of a RuvAB-Holliday junction complex in vitro. J. Mol. Biol. 232:1993;397-405
    • (1993) J. Mol. Biol. , vol.232 , pp. 397-405
    • Parsons, C.A.1    West, S.C.2
  • 27
    • 0026741832 scopus 로고
    • Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday juctions
    • Parsons C.A., Tsaneva I., Lloyd R.G., West S.C. Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday juctions. Proc. Natl Acad. Sci. USA. 89:1992;5452-5456
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5452-5456
    • Parsons, C.A.1    Tsaneva, I.2    Lloyd, R.G.3    West, S.C.4
  • 28
    • 0028968305 scopus 로고
    • Structure of a multisubunit complex that promotes DNA branch migration
    • Parsons C.A., Stasiak A., Bennet R.J., West S.C. Structure of a multisubunit complex that promotes DNA branch migration. Nature. 374:1995;375-378
    • (1995) Nature , vol.374 , pp. 375-378
    • Parsons, C.A.1    Stasiak, A.2    Bennet, R.J.3    West, S.C.4
  • 29
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: The calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins S.J. Protein volumes and hydration effects the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:1986;169-180
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 30
    • 77956826381 scopus 로고
    • X-ray and neutron solution scattering
    • Perkins S.J. X-ray and neutron solution scattering. New Compr. Biochem. ser. B. 11:1988;143-265
    • (1988) New Compr. Biochem. Ser. B , vol.11 , pp. 143-265
    • Perkins, S.J.1
  • 31
    • 0021112502 scopus 로고
    • Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering
    • Perkins S.J., Weiss H. Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering. J. Mol. Biol. 168:1983;847-866
    • (1983) J. Mol. Biol. , vol.168 , pp. 847-866
    • Perkins, S.J.1    Weiss, H.2
  • 32
    • 0027377159 scopus 로고
    • Modelling of the serine protease fold by X-ray and neutron scattering and sedimentation analyses: Its occurrence in factor D of the complement system
    • Perkins S.J., Smith K.F., Kilpatrick J.M., Volanakis J.E., Sim R.B. Modelling of the serine protease fold by X-ray and neutron scattering and sedimentation analyses its occurrence in factor D of the complement system. Biochem. J. 295:1993;87-99
    • (1993) Biochem. J. , vol.295 , pp. 87-99
    • Perkins, S.J.1    Smith, K.F.2    Kilpatrick, J.M.3    Volanakis, J.E.4    Sim, R.B.5
  • 37
    • 0026244044 scopus 로고
    • GNOM - A program package for small-angle scattering data processing
    • Semenyuk A.V., Svergun D.I. GNOM - a program package for small-angle scattering data processing. J. Appl. Crystallog. 24:1991;537-540
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 38
    • 0028590083 scopus 로고
    • Processing of intermediates in recombination and DNA repair: Identification of a new endonuclease that specifically cleaves Holliday junctions
    • Sharples G.J., Chan S.N., Mahdi A.A., Whitby M.C., Lloyd R.G. Processing of intermediates in recombination and DNA repair identification of a new endonuclease that specifically cleaves Holliday junctions. EMBO J. 13:1994;6133-6142
    • (1994) EMBO J. , vol.13 , pp. 6133-6142
    • Sharples, G.J.1    Chan, S.N.2    Mahdi, A.A.3    Whitby, M.C.4    Lloyd, R.G.5
  • 39
    • 0026058539 scopus 로고
    • SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli: Functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA
    • Shiba T., Iwasaki H., Nakata A., Shinagawa H. SOS-inducible DNA repair proteins, RuvA and RuvB, of Escherichia coli functional interactions between RuvA and RuvB for ATP hydrolysis and renaturation of the cruciform structure in supercoiled DNA. Proc. Natl Acad. Sci. USA. 88:1991;8445-8449
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8445-8449
    • Shiba, T.1    Iwasaki, H.2    Nakata, A.3    Shinagawa, H.4
  • 40
    • 0027413084 scopus 로고
    • Escherichia coli RuvA and RuvB proteins involved in recombination repair: Physical properties and interactions with DNA
    • Shiba T., Iwasaki H., Nakata A., Shinagawa H. Escherichia coli RuvA and RuvB proteins involved in recombination repair Physical properties and interactions with DNA. Mol. Gen. Genet. 237:1993;395-399
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 395-399
    • Shiba, T.1    Iwasaki, H.2    Nakata, A.3    Shinagawa, H.4
  • 41
    • 0029995337 scopus 로고    scopus 로고
    • Processing the Holliday juction in homologous recombination
    • Shinagawa H., Iwasaki H. Processing the Holliday juction in homologous recombination. Trends Biochem. Sci. 21:1996;107-111
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 107-111
    • Shinagawa, H.1    Iwasaki, H.2
  • 44
    • 0026633047 scopus 로고
    • ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli
    • Tsaneva I.R., Müller B., West S.C. ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli. Cell. 69:1992;1171-1180
    • (1992) Cell , vol.69 , pp. 1171-1180
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 45
    • 0026444104 scopus 로고
    • Purification and properties of the RuvA and RuvB proteins of Escherichia coli
    • Tsaneva I.R., Illing G.T., Lloyd R.G., West S.C. Purification and properties of the RuvA and RuvB proteins of Escherichia coli. Mol. Gen. Genet. 235:1992;1-10
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 1-10
    • Tsaneva, I.R.1    Illing, G.T.2    Lloyd, R.G.3    West, S.C.4
  • 46
    • 0027476446 scopus 로고
    • RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
    • Tsaneva I.R., Müller B., West S.C. RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro. Proc. Natl Acad. Sci. USA. 90:1993;1315-1319
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1315-1319
    • Tsaneva, I.R.1    Müller, B.2    West, S.C.3
  • 47
    • 0032536901 scopus 로고    scopus 로고
    • Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli
    • van Gool A.J., Shah R., Mezard C., West S.C. Functional interactions between the Holliday junction resolvase and the branch migration motor of Escherichia coli. EMBO J. 17:1997;1838-1845
    • (1997) EMBO J. , vol.17 , pp. 1838-1845
    • Van Gool, A.J.1    Shah, R.2    Mezard, C.3    West, S.C.4
  • 48
    • 0029911566 scopus 로고    scopus 로고
    • The RuvABC proteins and Holliday junction processing in Escherichia coli
    • West S.C. The RuvABC proteins and Holliday junction processing in Escherichia coli. J. Bacteriol. 178:1996;1237-1241
    • (1996) J. Bacteriol. , vol.178 , pp. 1237-1241
    • West, S.C.1
  • 49
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • West S.C. Processing of recombination intermediates by the RuvABC proteins. Annu. Rev. Genet. 31:1997;213-244
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 50
    • 0030596061 scopus 로고    scopus 로고
    • Interactions between RuvA and RuvC at Holliday junctions: Inhibition of junction cleavage and formation of a RuvC-RuvC-DNA complex
    • Whitby M.C., Bolt E.L., Chan S.N., Lloyd R.G. Interactions between RuvA and RuvC at Holliday junctions Inhibition of junction cleavage and formation of a RuvC-RuvC-DNA complex. J. Mol. Biol. 264:1996;878-890
    • (1996) J. Mol. Biol. , vol.264 , pp. 878-890
    • Whitby, M.C.1    Bolt, E.L.2    Chan, S.N.3    Lloyd, R.G.4
  • 51
    • 0031588022 scopus 로고    scopus 로고
    • Recognition and manipulation of branched DNA structure by junction-resolving enzymes
    • White M.F., Giraud-Panis M.J.E., Pöhler R.G., Lilley D.J.M. Recognition and manipulation of branched DNA structure by junction-resolving enzymes. J. Mol. Biol. 269:1997;647-664
    • (1997) J. Mol. Biol. , vol.269 , pp. 647-664
    • White, M.F.1    Giraud-Panis, M.J.E.2    Pöhler, R.G.3    Lilley, D.J.M.4
  • 52
    • 85055706702 scopus 로고
    • Absolute calibration of small angle neutron scattering data
    • Wignall G.D., Bates F.S. Absolute calibration of small angle neutron scattering data. J. Appl. Crystallog. 20:1987;28-40
    • (1987) J. Appl. Crystallog. , vol.20 , pp. 28-40
    • Wignall, G.D.1    Bates, F.S.2
  • 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. Nature Struct. Biol. 4:1997;101-104
    • (1997) Nature Struct. Biol. , vol.4 , pp. 101-104
    • Yu, X.1    Egelman, E.H.2
  • 54
    • 0031581811 scopus 로고    scopus 로고
    • Structure and subunit composition of the RuvAB-Holliday junction complex
    • Yu X., West S.C., Egelman E.H. Structure and subunit composition of the RuvAB-Holliday junction complex. J. Mol. Biol. 266:1997;217-222
    • (1997) J. Mol. Biol. , vol.266 , pp. 217-222
    • Yu, X.1    West, S.C.2    Egelman, E.H.3


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