메뉴 건너뛰기




Volumn 106, Issue 31, 2009, Pages 12688-12693

Structural transitions within human Rad51 nucleoprotein filaments

Author keywords

DNA curtain; Homologous recombination; Single molecule imaging

Indexed keywords

ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLYLIMIDODIPHOSPHATE; DNA; DOUBLE STRANDED DNA; NUCLEOPROTEIN; NUCLEOTIDE; OLIGOMER; RAD51 PROTEIN; CALCIUM; RAD51 PROTEIN, HUMAN; SODIUM CHLORIDE;

EID: 69149089856     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0811465106     Document Type: Article
Times cited : (38)

References (31)
  • 1
    • 0036900120 scopus 로고    scopus 로고
    • Role of RAD52 Epistasis group of genes in homologous recombination and double-strand break repair
    • Symington LS (2002) Role of RAD52 Epistasis group of genes in homologous recombination and double-strand break repair. Microbiol Mol Biol Rev 66:630-670.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 630-670
    • Symington, L.S.1
  • 2
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo J, Sung P, Klein H (2008) Mechanism of eukaryotic homologous recombination. Annu Rev Biochem 77:229-257.
    • (2008) Annu Rev Biochem , vol.77 , pp. 229-257
    • San Filippo, J.1    Sung, P.2    Klein, H.3
  • 3
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West SC (2003) Molecular views of recombination proteins and their control. Nat Rev 4:1-11.
    • (2003) Nat Rev , vol.4 , pp. 1-11
    • West, S.C.1
  • 4
    • 0242384946 scopus 로고    scopus 로고
    • Rad51 recombinase and recombination mediators
    • Sung P, Krejci L, Van Komen S, Sehorn MG (2003) Rad51 recombinase and recombination mediators. J Biol Chem 278:42729-42732.
    • (2003) J Biol Chem , vol.278 , pp. 42729-42732
    • Sung, P.1    Krejci, L.2    Van Komen, S.3    Sehorn, M.G.4
  • 5
    • 0030584084 scopus 로고    scopus 로고
    • Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro
    • Baumann P, Benson FE, West SC (1996) Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 87:757-766.
    • (1996) Cell , vol.87 , pp. 757-766
    • Baumann, P.1    Benson, F.E.2    West, S.C.3
  • 6
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco PR, Tracy RB, Kowalczykowski SC (1998) DNA strand exchange proteins: A biochemical and physical comparison. Front Biosci 3:d530-603.
    • (1998) Front Biosci , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 7
    • 0037131257 scopus 로고    scopus 로고
    • The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A
    • Oct 18
    • Eggler A, Inman R, Cox M (2002) Oct 18) The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A. J Biol Chem 277:39280-39288.
    • (2002) J Biol Chem , vol.277 , pp. 39280-39288
    • Eggler, A.1    Inman, R.2    Cox, M.3
  • 8
    • 2342527027 scopus 로고    scopus 로고
    • DNA damage checkpoint and repair centers
    • Jun
    • Lisby M, Rothstein R (2004 Jun) DNA damage checkpoint and repair centers. Curr Opin Cell Biol 16:328-334.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 328-334
    • Lisby, M.1    Rothstein, R.2
  • 9
    • 33748681302 scopus 로고    scopus 로고
    • Some disassembly required: Role of DNA translocases in the disruption of recombination intermediates and dead-end complexes
    • Symington LS, Heyer WD (2006) Some disassembly required: Role of DNA translocases in the disruption of recombination intermediates and dead-end complexes. Genes Dev 20:2479-2486.
    • (2006) Genes Dev , vol.20 , pp. 2479-2486
    • Symington, L.S.1    Heyer, W.D.2
  • 10
    • 0032127849 scopus 로고    scopus 로고
    • Role of the human Rad51 protein in homologous recombination and double-stranded-break repair
    • Baumann P, West SC (1998) Role of the human Rad51 protein in homologous recombination and double-stranded-break repair. Trends Biochem Sci 23:247-251.
    • (1998) Trends Biochem Sci , vol.23 , pp. 247-251
    • Baumann, P.1    West, S.C.2
  • 11
    • 0035902614 scopus 로고    scopus 로고
    • Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
    • Yu X, Jacobs SA, West SC, Ogawa T, Egelman EH (2001) Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc Natl Acad Sci USA 98:8419-8424.
    • (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
  • 12
    • 47249132575 scopus 로고    scopus 로고
    • A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments
    • Sheridan SD, et al. (2008) A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments. Nucleic Acids Res 36:4057-4066.
    • (2008) Nucleic Acids Res , vol.36 , pp. 4057-4066
    • Sheridan, S.D.1
  • 13
    • 2342466755 scopus 로고    scopus 로고
    • Structural basis for octomeric ring formation and DNA interaction of the human homologous-pairing protein Dmc1
    • Kinebuchi T, et al. (2004) Structural basis for octomeric ring formation and DNA interaction of the human homologous-pairing protein Dmc1. Mol Cell 14:363-374.
    • (2004) Mol Cell , vol.14 , pp. 363-374
    • Kinebuchi, T.1
  • 15
    • 0031013231 scopus 로고    scopus 로고
    • The RecA hexamer is a structural homologue of ring helicases
    • Yu X, Egelman EH (1997) The RecA hexamer is a structural homologue of ring helicases. Nat Struct Biol 4:101-104.
    • (1997) Nat Struct Biol , vol.4 , pp. 101-104
    • Yu, X.1    Egelman, E.H.2
  • 16
    • 0035861994 scopus 로고    scopus 로고
    • Archaeal RadA protein binds DNA as both helical filaments and octameric rings
    • Yang S, Yu X, Seitz EM, Kowalczykowski SC, Egelman EH (2001) Archaeal RadA protein binds DNA as both helical filaments and octameric rings. J Mol Biol 314:1077-1085.
    • (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
  • 17
    • 33749327819 scopus 로고    scopus 로고
    • Visualizing the assembly of human Rad51 filaments on double-stranded DNA
    • Prasad TK, Yeykal CC, Greene EC (2006) Visualizing the assembly of human Rad51 filaments on double-stranded DNA. J Mol Biol 363:713-728.
    • (2006) J Mol Biol , vol.363 , pp. 713-728
    • Prasad, T.K.1    Yeykal, C.C.2    Greene, E.C.3
  • 18
    • 30344473311 scopus 로고    scopus 로고
    • Organized arrays of individual DNA molecules tethered to supported lipid bilayers
    • Graneli A, Yeykal CC, Prasad TK, Greene EC (2006) Organized arrays of individual DNA molecules tethered to supported lipid bilayers. Langmuir 22:292-299.
    • (2006) Langmuir , vol.22 , pp. 292-299
    • Graneli, A.1    Yeykal, C.C.2    Prasad, T.K.3    Greene, E.C.4
  • 19
  • 21
    • 3042791448 scopus 로고    scopus 로고
    • 2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity
    • 2+ activates human homologous recombination protein Rad51 by modulating its ATPase activity. Proc Natl Acad Sci USA 101:9988-9993.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9988-9993
    • Bugreev, D.V.1    Mazin, A.V.2
  • 22
    • 0037036354 scopus 로고    scopus 로고
    • ATP hydrolysis by mammalian Rad51 has a key role during homology-directed DNA repair
    • Stark JM, Hu P, Pierce AJ, Moynahan ME, Ellis N, Jasin M (2002) ATP hydrolysis by mammalian Rad51 has a key role during homology-directed DNA repair. J Biol Chem 277:20185-20194.
    • (2002) J Biol Chem , vol.277 , pp. 20185-20194
    • Stark, J.M.1    Hu, P.2    Pierce, A.J.3    Moynahan, M.E.4    Ellis, N.5    Jasin, M.6
  • 23
    • 32644466860 scopus 로고    scopus 로고
    • Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function
    • Chi P, Van Komen S, Sehorn MG, Sigurdsson S, Sung P (2006) Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function. DNA Repair 5:381-391.
    • (2006) DNA Repair , vol.5 , pp. 381-391
    • Chi, P.1    Van Komen, S.2    Sehorn, M.G.3    Sigurdsson, S.4    Sung, P.5
  • 24
    • 34250160539 scopus 로고    scopus 로고
    • Elastic behavior of RecA-DNA helical filaments
    • Nishinaka T, Doi Y, Hara R, Yashima E (2007) Elastic behavior of RecA-DNA helical filaments. J Mol Biol 370:837-845.
    • (2007) J Mol Biol , vol.370 , pp. 837-845
    • Nishinaka, T.1    Doi, Y.2    Hara, R.3    Yashima, E.4
  • 25
    • 59649116344 scopus 로고    scopus 로고
    • Counting Rad51 proteins disassembling from nucleoprotein filaments under tension
    • van Mameren J, Modesti M, Kanaar R, Wyman C, Peterman EJ, Wuite GJ (2009) Counting Rad51 proteins disassembling from nucleoprotein filaments under tension. Nature 457:745-748.
    • (2009) Nature , vol.457 , pp. 745-748
    • van Mameren, J.1    Modesti, M.2    Kanaar, R.3    Wyman, C.4    Peterman, E.J.5    Wuite, G.J.6
  • 26
    • 33744781613 scopus 로고    scopus 로고
    • The Rad51/RadA N-terminal domain activates nucleoprotein filament ATPase activity
    • Galkin VE, et al. (2006) The Rad51/RadA N-terminal domain activates nucleoprotein filament ATPase activity. Structure 14:983-992.
    • (2006) Structure , vol.14 , pp. 983-992
    • Galkin, V.E.1
  • 28
    • 34249878748 scopus 로고    scopus 로고
    • Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2
    • Esashi F, Galkin VE, Yu X, Egelman EH, West SC (2007) Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2. Nat Struct Mol Biol 14:468-474.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 468-474
    • Esashi, F.1    Galkin, V.E.2    Yu, X.3    Egelman, E.H.4    West, S.C.5
  • 29
    • 34249892132 scopus 로고    scopus 로고
    • Stabilization of RAD-51-DNA filaments via an interaction domain in Caenorhabditis elegans BRCA2
    • Petalcorin MI, Galkin VE, Yu X, Egelman EH, Boulton SJ (2007) Stabilization of RAD-51-DNA filaments via an interaction domain in Caenorhabditis elegans BRCA2. Proc Natl Acad Sci USA 104:8299-8304.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8299-8304
    • Petalcorin, M.I.1    Galkin, V.E.2    Yu, X.3    Egelman, E.H.4    Boulton, S.J.5
  • 30
    • 57349128865 scopus 로고    scopus 로고
    • A chemical compound that stimulates the human homologous recombination protein RAD51
    • Jayathilaka K, et al. (2008) A chemical compound that stimulates the human homologous recombination protein RAD51. Proc Natl Acad Sci USA 105:15848-15853.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15848-15853
    • Jayathilaka, K.1
  • 31
    • 34248512303 scopus 로고    scopus 로고
    • A DNA-translocating Snf2 molecular motor: Saccharomyces cerevisiae Rdh54 displays processive translocation and extrudes DNA loops
    • Prasad TK, Robertson RB, Visnapuu ML, Chi P, Sung P, Greene EC (2007) A DNA-translocating Snf2 molecular motor: Saccharomyces cerevisiae Rdh54 displays processive translocation and extrudes DNA loops. J Mol Biol 369:940-953.
    • (2007) J Mol Biol , vol.369 , pp. 940-953
    • Prasad, T.K.1    Robertson, R.B.2    Visnapuu, M.L.3    Chi, P.4    Sung, P.5    Greene, E.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.