메뉴 건너뛰기




Volumn 323, Issue 3, 2004, Pages 845-851

Self-polymerization of archaeal RadA protein into long and fine helical filaments

Author keywords

AFM; Dmc1; Homologous recombination; Rad51; RadA; RecA

Indexed keywords

BACTERIAL PROTEIN; CARBON NANOTUBE; DNA; NUCLEOPROTEIN; NUCLEOTIDE; RADA PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 4544289542     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.163     Document Type: Article
Times cited : (17)

References (25)
  • 1
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • S.C. Kowalczykowski Initiation of genetic recombination and recombination-dependent replication Trends Biochem. Sci. 25 2000 156 165
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 2
    • 0242692609 scopus 로고    scopus 로고
    • The bacterial RecA protein as a motor protein
    • M.M. Cox The bacterial RecA protein as a motor protein Annu. Rev. Microbiol. 57 2003 551 577
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 551-577
    • Cox, M.M.1
  • 3
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is aRecA-like protein
    • A. Shinohara, H. Ogawa, and T. Ogawa Rad51 protein involved in repair and recombination in S. cerevisiae is aRecA-like protein Cell 69 1992 457 470
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 4
    • 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, D. Park, L. Xu, and N. Kleckner 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
  • 5
    • 0029946142 scopus 로고    scopus 로고
    • RecA-like genes from three archaean species with putative protein products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces cerevisiae
    • S.J. Sandler, L.H. Satin, H.S. Samra, and A.J. Clark recA-like genes from three archaean species with putative protein products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces cerevisiae Nucleic Acids Res. 24 1996 2125 2132
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2125-2132
    • Sandler, S.J.1    Satin, L.H.2    Samra, H.S.3    Clark, A.J.4
  • 6
    • 0032079749 scopus 로고    scopus 로고
    • RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
    • E.M. Seitz, J.P. Brockman, S.J. Sandler, A.J. Clark, and S.C. Kowalczykowski 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
  • 7
    • 0035890601 scopus 로고    scopus 로고
    • RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination
    • M.J. McIlwraith, D.R. Hall, A.Z. Stasiak, A. Stasiak, D.B. Wigley, and S.C. West RadA protein from Archaeoglobus fulgidus forms rings, nucleoprotein filaments and catalyses homologous recombination Nucleic Acids Res. 29 2001 4509 4517
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4509-4517
    • McIlwraith, M.J.1    Hall, D.R.2    Stasiak, A.Z.3    Stasiak, A.4    Wigley, D.B.5    West, S.C.6
  • 8
    • 0035861994 scopus 로고    scopus 로고
    • Archaeal RadA protein binds DNA as both helical filaments and octameric rings
    • S. Yang, X. Yu, E.M. Seitz, S.C. Kowalczykowski, and E.H. Egelman 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
  • 9
    • 0027167689 scopus 로고
    • Similarity of the yeast RAD51 filament to the bacterial RecA filament
    • T. Ogawa, X. Yu, A. Shinohara, and E.H. Egelman 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
  • 12
    • 0031013231 scopus 로고    scopus 로고
    • The RecA hexamer is a structural homologue of ring helicases
    • X. Yu, and 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
  • 13
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • R.M. Story, I.T. Weber, and T.A. Steitz 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
  • 14
    • 0030811492 scopus 로고    scopus 로고
    • Purification of human Rad51 protein by selective spermidine precipitation
    • P. Baumann, F.E. Benson, N. Hajibagheri, and S.C. West Purification of human Rad51 protein by selective spermidine precipitation Mutat. Res. 384 1997 65 72
    • (1997) Mutat. Res. , vol.384 , pp. 65-72
    • Baumann, P.1    Benson, F.E.2    Hajibagheri, N.3    West, S.C.4
  • 16
    • 4544257906 scopus 로고    scopus 로고
    • High-throughput screening of soluble recombinant proteins
    • R.J. Simpson Cold Spring Harbor Laboratory Cold Spring Harbor, NY
    • T.F. Wang, and A.H.J. Wang High-throughput screening of soluble recombinant proteins R.J. Simpson Purifying Proteins for Proteomics: A Laboratory Manual 2004 Cold Spring Harbor Laboratory Cold Spring Harbor, NY Chapter 5
    • (2004) Purifying Proteins for Proteomics: A Laboratory Manual
    • Wang, T.F.1    Wang, A.H.J.2
  • 17
    • 0031059866 scopus 로고    scopus 로고
    • Processing of the X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of the X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 18
    • 0031058884 scopus 로고    scopus 로고
    • Rotation function calculations with GLRF program
    • L. Tong, and M. Rossmann Rotation function calculations with GLRF program Methods Enzymol. 276 1997 594 611
    • (1997) Methods Enzymol. , vol.276 , pp. 594-611
    • Tong, L.1    Rossmann, M.2
  • 19
    • 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
    • T.F. Wang, N. Kleckner, and N. Hunter 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
  • 20
    • 0019053474 scopus 로고
    • Genetic recombination of bacterial plasmid DNA: Electron microscopic analysis of in vitro intramolecular recombination
    • R. Kolodner Genetic recombination of bacterial plasmid DNA: electron microscopic analysis of in vitro intramolecular recombination Proc. Natl. Acad. Sci. USA 77 1980 4847 4851
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4847-4851
    • Kolodner, R.1
  • 22
    • 0031807387 scopus 로고    scopus 로고
    • Isolation and characterization of a DnaJ-like protein in rats: The C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein
    • C.H. Leng, J.L. Brodsky, and C. Wang Isolation and characterization of a DnaJ-like protein in rats: the C-terminal 10-kDa domain of hsc70 is not essential for stimulating the ATP-hydrolytic activity of hsc70 by a DnaJ-like protein Protein Sci. 7 1998 1186 1194
    • (1998) Protein Sci. , vol.7 , pp. 1186-1194
    • Leng, C.H.1    Brodsky, J.L.2    Wang, C.3
  • 23
    • 0037981459 scopus 로고    scopus 로고
    • Easy method to adjust the angle of the carbon nanotube probe of an atomic force microscope
    • Y.C. Chang, D.C. Wang, C.S. Chang, and T.T. Tsong Easy method to adjust the angle of the carbon nanotube probe of an atomic force microscope Appl. Phys. Lett. 82 2003 3541 3543
    • (2003) Appl. Phys. Lett. , vol.82 , pp. 3541-3543
    • Chang, Y.C.1    Wang, D.C.2    Chang, C.S.3    Tsong, T.T.4
  • 24
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RADA; A snapshot of its extended conformation
    • Y. Wu, Y. He, I.A. Moya, X. Qian, and Y. Luo Crystal structure of archaeal recombinase RADA; a snapshot of its extended conformation Mol. Cell 15 2004 423 435
    • (2004) Mol. Cell , vol.15 , pp. 423-435
    • Wu, Y.1    He, Y.2    Moya, I.A.3    Qian, X.4    Luo, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.