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Volumn 25, Issue 4, 2000, Pages 183-184

A ubiquitous structural core

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; HELICASE; NUCLEOPROTEIN; PROTEIN SUBUNIT; RECA PROTEIN;

EID: 0034177084     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01570-X     Document Type: Review
Times cited : (7)

References (49)
  • 1
    • 0029654290 scopus 로고
    • Formation, translocation and resolution of Holliday junctions during homologous genetic recombination
    • S.C. West Formation, translocation and resolution of Holliday junctions during homologous genetic recombination Phil. Trans. Roy. Soc. B 347 1995 21 25
    • (1995) Phil. Trans. Roy. Soc. B , vol.347 , pp. 21-25
    • West, S.C.1
  • 2
    • 0028102267 scopus 로고
    • Biochemistry of homologous recombination in Escherichia coli
    • S.C. Kowalczykowski Biochemistry of homologous recombination in Escherichia coli Microbiol. Rev. 58 1994 401 465
    • (1994) Microbiol. Rev. , vol.58 , pp. 401-465
    • Kowalczykowski, S.C.1
  • 3
    • 0030633568 scopus 로고    scopus 로고
    • RecA protein: structure, function, and role in recombinational DNA repair
    • A.I. Roca M.M. Cox RecA protein structure, function, and role in recombinational DNA repair Prog. Nucleic Acids Res. Mol. Biol. 56 1997 129 223
    • (1997) Prog. Nucleic Acids Res. Mol. Biol. , vol.56 , pp. 129-223
    • Roca, A.I.1    Cox, M.M.2
  • 4
    • 0026095558 scopus 로고
    • Helical interactions in homologous pairing and strand exchange driven by RecA protein
    • C.M. Radding Helical interactions in homologous pairing and strand exchange driven by RecA protein J. Biol. Chem. 266 1991 5355 5358
    • (1991) J. Biol. Chem. , vol.266 , pp. 5355-5358
    • Radding, C.M.1
  • 5
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • A. Shinohara 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
  • 6
    • 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
    • A. Aboussekhra 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 1992 3224 3234
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3224-3234
    • Aboussekhra, A.1
  • 7
    • 0020478259 scopus 로고
    • The helicity of DNA in complexes with RecA protein
    • A. Stasiak E. DiCapua 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
  • 8
    • 0019888429 scopus 로고
    • Elongation of duplex DNA by RecA protein
    • A. Stasiak 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
  • 9
    • 0027167689 scopus 로고
    • Similarity of the yeast RAD51 filament to the bacterial RecA filament
    • T. Ogawa 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
  • 10
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • F.E. Benson 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
  • 11
    • 0029856618 scopus 로고    scopus 로고
    • Crystal structure of a DExx box DNA helicase
    • H.S. Subramanya Crystal structure of a DExx box DNA helicase Nature 384 1996 379 383
    • (1996) Nature , vol.384 , pp. 379-383
    • Subramanya, H.S.1
  • 12
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • R.M. Story 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
  • 13
    • 0027518667 scopus 로고
    • Helicase-catalysed DNA unwinding
    • T.M. Lohman Helicase-catalysed DNA unwinding J. Biol. Chem. 268 1993 2269 2272
    • (1993) J. Biol. Chem. , vol.268 , pp. 2269-2272
    • Lohman, T.M.1
  • 14
    • 0027950513 scopus 로고
    • DNA helicases: enzymes with essential roles in all aspects of DNA metabolism
    • S.W. Matson DNA helicases enzymes with essential roles in all aspects of DNA metabolism BioEssays 16 1994 13 22
    • (1994) BioEssays , vol.16 , pp. 13-22
    • Matson, S.W.1
  • 15
    • 0028953715 scopus 로고
    • DNA helicases in recombination and repair: construction of a ΔuvrD ΔhelD ΔrecQ mutant deficient in recombination and repair
    • V.M. Mendonca DNA helicases in recombination and repair construction of a ΔuvrD ΔhelD ΔrecQ mutant deficient in recombination and repair J. Bacteriol. 177 1995 1326 1335
    • (1995) J. Bacteriol. , vol.177 , pp. 1326-1335
    • Mendonca, V.M.1
  • 17
    • 0032942212 scopus 로고    scopus 로고
    • Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis
    • A. Shiratori Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis Yeast 15 1999 219 253
    • (1999) Yeast , vol.15 , pp. 219-253
    • Shiratori, A.1
  • 18
    • 0029911566 scopus 로고    scopus 로고
    • The RuvABC proteins and Holliday junction processing in Escherichia coli
    • S.C. West 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
  • 19
    • 0028050051 scopus 로고
    • The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA
    • A. Stasiak The Escherichia coli RuvB branch migration protein forms double hexameric rings around DNA Proc. Natl. Acad. Sci. U. S. A. 91 1994 7618 7622
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 7618-7622
    • Stasiak, A.1
  • 20
    • 0031581811 scopus 로고    scopus 로고
    • Structure and subunit composition of the RuvAB–Holliday junction complex
    • X. Yu 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
  • 21
    • 0028968305 scopus 로고
    • Structure of a multisubunit complex that promotes DNA branch migration
    • C.A. Parsons 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
  • 22
    • 0029762774 scopus 로고    scopus 로고
    • DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase
    • X. Yu DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase Nat. Struct. Biol. 3 1996 740 743
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 740-743
    • Yu, X.1
  • 23
    • 0030670510 scopus 로고    scopus 로고
    • A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding
    • K.J. Hacker K.A. Johnson A hexameric helicase encircles one DNA strand and excludes the other during DNA unwinding Biochemistry 36 1997 14080 14087
    • (1997) Biochemistry , vol.36 , pp. 14080-14087
    • Hacker, K.J.1    Johnson, K.A.2
  • 24
    • 0027182114 scopus 로고
    • Helicases: amino acid sequence comparisons and structure–function relationships
    • A.E. Gorbalenya E.V. Koonin Helicases amino acid sequence comparisons and structure–function relationships Curr. Opin. Struct. Biol. 3 1993 419 429
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 25
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • A.E. Gorbalenya Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes Nucleic Acids Res. 17 1989 4713 4730
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1
  • 26
    • 0031911760 scopus 로고    scopus 로고
    • Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases
    • S. Korolev Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases Protein Sci. 7 1998 605 610
    • (1998) Protein Sci. , vol.7 , pp. 605-610
    • Korolev, S.1
  • 27
    • 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
    • S. Korolev 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
  • 28
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • M.R. Sawaya 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
  • 29
    • 0028114231 scopus 로고
    • Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria
    • 1-ATPase from bovine heart mitochondria Nature 370 1994 621 628
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1
  • 30
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III
    • B. Guenther Crystal structure of the δ′ subunit of the clamp-loader complex of E. coli DNA polymerase III Cell 91 1997 335 345
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1
  • 31
    • 0031013231 scopus 로고    scopus 로고
    • The RecA hexamer is a structural homologue of ring helicases
    • X. Yu E.H. Egelman 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
  • 32
    • 0029039925 scopus 로고
    • Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases
    • E.H. Egelman Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases Proc. Natl. Acad. Sci. U. S. A. 92 1995 3869 3873
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3869-3873
    • Egelman, E.H.1
  • 33
    • 0031585985 scopus 로고    scopus 로고
    • Six molecules of SV40 large T antigen assemble in a propeller-shaped particle around a channel
    • M.C. San Martin Six molecules of SV40 large T antigen assemble in a propeller-shaped particle around a channel J. Mol. Biol. 268 1997 15 20
    • (1997) J. Mol. Biol. , vol.268 , pp. 15-20
    • San Martin, M.C.1
  • 34
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • M.C. San Martin A structural model for the Escherichia coli DnaB helicase based on electron microscopy data J. Struct. Biol. 114 1995 167 176
    • (1995) J. Struct. Biol. , vol.114 , pp. 167-176
    • San Martin, M.C.1
  • 35
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different quaternary hexameric states
    • X. Yu The hexameric E. coli DnaB helicase can exist in different quaternary hexameric states J. Mol. Biol. 259 1996 7 14
    • (1996) J. Mol. Biol. , vol.259 , pp. 7-14
    • Yu, X.1
  • 36
    • 0032491563 scopus 로고    scopus 로고
    • Polymorphic quaternary organization of the Bacillus subtilis bacteriophage SPP1 replicative helicase (G40 P).
    • M. Barcena Polymorphic quaternary organization of the Bacillus subtilis bacteriophage SPP1 replicative helicase (G40 P). J. Mol. Biol. 283 1998 809 819
    • (1998) J. Mol. Biol. , vol.283 , pp. 809-819
    • Barcena, M.1
  • 37
    • 0033548196 scopus 로고    scopus 로고
    • Biochemical and electron microscopic image analysis of the hexameric E1 helicase
    • E.T. Fouts Biochemical and electron microscopic image analysis of the hexameric E1 helicase J. Biol. Chem. 274 1999 4447 4458
    • (1999) J. Biol. Chem. , vol.274 , pp. 4447-4458
    • Fouts, E.T.1
  • 38
    • 0028892745 scopus 로고
    • Structural polymorphism of the RecA protein from the thermophilic bacterium Thermus aquaticus
    • X. Yu 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
  • 39
    • 0026697166 scopus 로고
    • DMC1: a meiosis-specific yeast homolog of E. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression
    • D.K. Bishop 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
  • 40
    • 0030764984 scopus 로고    scopus 로고
    • Recombination activities of HsDmc1 protein, the meiotic human homolog of RecA protein
    • Z. Li Recombination activities of HsDmc1 protein, the meiotic human homolog of RecA protein Proc. Natl. Acad. Sci. U. S. A. 94 1997 11221 11226
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11221-11226
    • Li, Z.1
  • 41
    • 0033571226 scopus 로고    scopus 로고
    • The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51
    • J.Y. Masson The meiosis-specific recombinase hDmc1 forms ring structures and interacts with hRad51 EMBO J. 18 1999 6552 6560
    • (1999) EMBO J. , vol.18 , pp. 6552-6560
    • Masson, J.Y.1
  • 42
    • 0032828490 scopus 로고    scopus 로고
    • Human Dmc1 protein binds DNA as an octameric ring
    • S.I. Passy Human Dmc1 protein binds DNA as an octameric ring Proc. Natl. Acad. Sci. U. S. A. 96 1999 10684 10688
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 10684-10688
    • Passy, S.I.1
  • 43
    • 0026443726 scopus 로고
    • Activity of the purified mutagenesis proteins UmuC, UmuD′, and RecA in replicative bypass of an abasic DNA lesion by DNA polymerase III
    • M. Rajagopalan Activity of the purified mutagenesis proteins UmuC, UmuD′, and RecA in replicative bypass of an abasic DNA lesion by DNA polymerase III Proc. Natl. Acad. Sci. U. S. A. 89 1992 10777 10781
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 10777-10781
    • Rajagopalan, M.1
  • 44
    • 0033529763 scopus 로고    scopus 로고
    • UmuD′(2)C is an error-prone DNA polymerase, Escherichia coli pol V
    • M. Tang UmuD′(2)C is an error-prone DNA polymerase, Escherichia coli pol V Proc. Natl. Acad. Sci. U. S. A. 96 1999 8919 8924
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 8919-8924
    • Tang, M.1
  • 45
    • 0032484207 scopus 로고    scopus 로고
    • Modulation of RecA nucleoprotein function by the mutagenic UmuD′C protein complex
    • W.M. Rehrauer Modulation of RecA nucleoprotein function by the mutagenic UmuD′C protein complex J. Biol. Chem. 273 1998 32384 32387
    • (1998) J. Biol. Chem. , vol.273 , pp. 32384-32387
    • Rehrauer, W.M.1
  • 46
    • 0030933762 scopus 로고    scopus 로고
    • Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2
    • S.K. Sharan Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2 Nature 386 1997 804 810
    • (1997) Nature , vol.386 , pp. 804-810
    • Sharan, S.K.1
  • 47
    • 0029909565 scopus 로고    scopus 로고
    • A mutation in mouse rad51 results in an early embryonic lethal that is suppressed by a mutation in p53
    • D.S. Lim P. Hasty A mutation in mouse rad51 results in an early embryonic lethal that is suppressed by a mutation in p53 Mol. Cell Biol. 16 1996 7133 7143
    • (1996) Mol. Cell Biol. , vol.16 , pp. 7133-7143
    • Lim, D.S.1    Hasty, P.2
  • 48
    • 15844409553 scopus 로고    scopus 로고
    • Positional cloning of the Werner’s syndrome gene
    • C.-E. Yu Positional cloning of the Werner’s syndrome gene Science 272 1996 258 262
    • (1996) Science , vol.272 , pp. 258-262
    • Yu, C.-E.1
  • 49
    • 0028785586 scopus 로고
    • The Bloom’s syndrome gene product is homologous to RecQ helicases
    • N.A. Ellis The Bloom’s syndrome gene product is homologous to RecQ helicases Cell 83 1995 655 666
    • (1995) Cell , vol.83 , pp. 655-666
    • Ellis, N.A.1


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