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Volumn 37, Issue 2, 2009, Pages 557-567

Inter-subunit interactions that coordinate Rad51's activities

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; RAD51 PROTEIN;

EID: 59649118705     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn973     Document Type: Article
Times cited : (9)

References (58)
  • 1
    • 33845604556 scopus 로고    scopus 로고
    • DNA double-strand break repair: All's well that ends well
    • Wyman,C. and Kanaar,R. (2006) DNA double-strand break repair: All's well that ends well. Annu. Rev. Genet., 40, 363-383.
    • (2006) Annu. Rev. Genet , vol.40 , pp. 363-383
    • Wyman, C.1    Kanaar, R.2
  • 2
    • 0033614034 scopus 로고    scopus 로고
    • The DNA binding properties of Saccharomyces cerevisiae Rad51 protein
    • Zaitseva,E.M., Zaitsev,E.N. and Kowalczykowski,S.C. (1999) The DNA binding properties of Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem., 274, 2907-2915.
    • (1999) J. Biol. Chem , vol.274 , pp. 2907-2915
    • Zaitseva, E.M.1    Zaitsev, E.N.2    Kowalczykowski, S.C.3
  • 3
    • 0032513226 scopus 로고    scopus 로고
    • Binding of Rad51p to DNA. Interaction of Rad51p with single- and double-stranded DNA
    • Namsaraev,E.A. and Berg,P. (1998) Binding of Rad51p to DNA. Interaction of Rad51p with single- and double-stranded DNA. J. Biol. Chem., 273, 6177-6182.
    • (1998) J. Biol. Chem , vol.273 , pp. 6177-6182
    • Namsaraev, E.A.1    Berg, P.2
  • 4
    • 0030850017 scopus 로고    scopus 로고
    • Characterization of strand exchange activity of yeast Rad51 protein
    • Namsaraev,E. and Berg,P. (1997) Characterization of strand exchange activity of yeast Rad51 protein. Mol. Cell Biol., 17, 5359-5368.
    • (1997) Mol. Cell Biol , vol.17 , pp. 5359-5368
    • Namsaraev, E.1    Berg, P.2
  • 5
    • 0034161571 scopus 로고    scopus 로고
    • Tailed duplex DNA is the preferred substrate for Rad51 proteinmediated homologous pairing
    • Mazin,A.V., Zaitseva,E., Sung,P. and Kowalczykowski,S.C. (2000) Tailed duplex DNA is the preferred substrate for Rad51 proteinmediated homologous pairing. EMBO J., 19, 1148-1156.
    • (2000) EMBO J , vol.19 , pp. 1148-1156
    • Mazin, A.V.1    Zaitseva, E.2    Sung, P.3    Kowalczykowski, S.C.4
  • 6
    • 0027978039 scopus 로고    scopus 로고
    • Sung,P. (1994) Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science, 265, 1241-1243.
    • Sung,P. (1994) Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein. Science, 265, 1241-1243.
  • 9
    • 0026751113 scopus 로고
    • Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein
    • Shinohara,A., Ogawa,H. and Ogawa,T. (1992) Rad51 protein involved in repair and recombination in S. cerevisiae is a RecA-like protein. Cell, 69, 457-470.
    • (1992) Cell , vol.69 , pp. 457-470
    • Shinohara, A.1    Ogawa, H.2    Ogawa, T.3
  • 10
    • 0028072098 scopus 로고
    • Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA
    • Benson,F.E., Stasiak,A. and West,S.C. (1994) Purification and characterization of the human Rad51 protein, an analogue of E. coli RecA. EMBO J., 13, 5764-5771.
    • (1994) EMBO J , vol.13 , pp. 5764-5771
    • Benson, F.E.1    Stasiak, A.2    West, S.C.3
  • 12
    • 0029112483 scopus 로고
    • DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA
    • Sung,P. and Robberson,D.L. (1995) DNA strand exchange mediated by a RAD51-ssDNA nucleoprotein filament with polarity opposite to that of RecA. Cell, 82, 453-461.
    • (1995) Cell , vol.82 , pp. 453-461
    • Sung, P.1    Robberson, D.L.2
  • 13
    • 0031449639 scopus 로고    scopus 로고
    • Mammalian Rad51 protein: A RecA homologue with pleiotropic functions
    • Vispe,S. and Defais,M. (1997) Mammalian Rad51 protein: A RecA homologue with pleiotropic functions. Biochimie, 79, 587-592.
    • (1997) Biochimie , vol.79 , pp. 587-592
    • Vispe, S.1    Defais, M.2
  • 14
    • 0027167689 scopus 로고
    • Similarity of the yeast RAD51 filament to the bacterial RecA filament
    • Ogawa,T., Yu,X., Shinohara,A. and Egelman,E.H. (1993) Similarity of the yeast RAD51 filament to the bacterial RecA filament. Science, 259, 1896-1899.
    • (1993) Science , vol.259 , pp. 1896-1899
    • Ogawa, T.1    Yu, X.2    Shinohara, A.3    Egelman, E.H.4
  • 15
    • 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. and Egelman,E.H. (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
  • 16
    • 0024339718 scopus 로고
    • The location of DNA in RecADNA helical filaments
    • Egelman,E.H. and Yu,X. (1989) The location of DNA in RecADNA helical filaments. Science, 245, 404-407.
    • (1989) Science , vol.245 , pp. 404-407
    • Egelman, E.H.1    Yu, X.2
  • 17
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger,J.P. and Berger,J.M. (2006) Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct., 35, 93-114.
    • (2006) Annu. Rev. Biophys. Biomol. Struct , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 18
    • 0029829561 scopus 로고    scopus 로고
    • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
    • Scheffzek,K., Lautwein,A., Kabsch,W., Ahmadian,M.R. and Wittinghofer,A. (1996) Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature, 384, 591-596.
    • (1996) Nature , vol.384 , pp. 591-596
    • Scheffzek, K.1    Lautwein, A.2    Kabsch, W.3    Ahmadian, M.R.4    Wittinghofer, A.5
  • 19
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • Story,R.M., Weber,I.T. and Steitz,T.A. (1992) The structure of the E. coli recA protein monomer and polymer. Nature, 355, 318-325.
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 20
    • 0037441480 scopus 로고    scopus 로고
    • Structural studies on MtRecA-nucleotide complexes: Insights into DNA and nucleotide binding and the structural signature of NTP recognition
    • Datta,S., Ganesh,N., Chandra,N.R., Muniyappa,K. and Vijayan,M. (2003) Structural studies on MtRecA-nucleotide complexes: Insights into DNA and nucleotide binding and the structural signature of NTP recognition. Proteins, 50, 474-485.
    • (2003) Proteins , vol.50 , pp. 474-485
    • Datta, S.1    Ganesh, N.2    Chandra, N.R.3    Muniyappa, K.4    Vijayan, M.5
  • 22
    • 27144526413 scopus 로고    scopus 로고
    • Crystal structure of Methanococcus voltae RadA in complex with ADP: Hydrolysis-induced conformational change
    • Qian,X., Wu,Y., He,Y. and Luo,Y. (2005) Crystal structure of Methanococcus voltae RadA in complex with ADP: Hydrolysis-induced conformational change. Biochemistry, 44, 13753-13761.
    • (2005) Biochemistry , vol.44 , pp. 13753-13761
    • Qian, X.1    Wu, Y.2    He, Y.3    Luo, Y.4
  • 23
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RADA: A snapshot of its extended conformation
    • Wu,Y., He,Y., Moya,I.A., Qian,X. and Luo,Y. (2004) Crystal structure of archaeal recombinase RADA: A snapshot of its extended conformation. Mol. Cell, 15, 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
  • 24
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • Chen,Z., Yang,H. and Pavletich,N.P. (2008) Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature, 453 489-484.
    • (2008) Nature , vol.453 , pp. 489-484
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 25
    • 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. and Shibata,T. (1999) 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, 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
  • 26
    • 33847795537 scopus 로고    scopus 로고
    • Regulation of bacterial RecA protein function
    • Cox,M.M. (2007) Regulation of bacterial RecA protein function. Crit. Rev. Biochem. Mol. Biol., 42, 41-63.
    • (2007) Crit. Rev. Biochem. Mol. Biol , vol.42 , pp. 41-63
    • Cox, M.M.1
  • 27
    • 4444308700 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in a compressed helical filament
    • Xing,X. and Bell,C.E. (2004) Crystal structures of Escherichia coli RecA in a compressed helical filament. J. Mol. Biol., 342, 1471-1485.
    • (2004) J. Mol. Biol , vol.342 , pp. 1471-1485
    • Xing, X.1    Bell, C.E.2
  • 28
    • 8544258063 scopus 로고    scopus 로고
    • Crystal structure of RecA from Deinococcus radiodurans: Insights into the structural basis of extreme radioresistance
    • Rajan,R. and Bell,C.E. (2004) Crystal structure of RecA from Deinococcus radiodurans: Insights into the structural basis of extreme radioresistance. J. Mol. Biol., 344, 951-963.
    • (2004) J. Mol. Biol , vol.344 , pp. 951-963
    • Rajan, R.1    Bell, C.E.2
  • 29
    • 11144255128 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP
    • Xing,X. and Bell,C.E. (2004) Crystal structures of Escherichia coli RecA in complex with MgADP and MnAMP-PNP. Biochemistry, 43, 16142-16152.
    • (2004) Biochemistry , vol.43 , pp. 16142-16152
    • Xing, X.1    Bell, C.E.2
  • 30
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story,R.M. and Steitz,T.A. (1992) Structure of the recA protein-ADP complex. Nature, 355, 374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 31
    • 0028129812 scopus 로고
    • Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli
    • Skiba,M.C. and Knight,K.L. (1994) Functionally important residues at a subunit interface site in the RecA protein from Escherichia coli. J. Biol. Chem., 269, 3823-3828.
    • (1994) J. Biol. Chem , vol.269 , pp. 3823-3828
    • Skiba, M.C.1    Knight, K.L.2
  • 32
    • 1642463787 scopus 로고    scopus 로고
    • Molecular design and functional organization of the RecA protein
    • McGrew,D.A. and Knight,K.L. (2003) Molecular design and functional organization of the RecA protein. Crit. Rev. Biochem. Mol. Biol., 38, 385-432.
    • (2003) Crit. Rev. Biochem. Mol. Biol , vol.38 , pp. 385-432
    • McGrew, D.A.1    Knight, K.L.2
  • 33
    • 0035157386 scopus 로고    scopus 로고
    • Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament
    • Kelley De Zutter,J., Forget,A.L., Logan,K.M. and Knight,K.L. (2001) Phe217 regulates the transfer of allosteric information across the subunit interface of the RecA protein filament. Structure (Camb.), 9, 47-55.
    • (2001) Structure (Camb.) , vol.9 , pp. 47-55
    • Kelley De Zutter, J.1    Forget, A.L.2    Logan, K.M.3    Knight, K.L.4
  • 35
    • 0037124355 scopus 로고    scopus 로고
    • Mutations in yeast Rad51 that partially bypass the requirement for Rad55 and Rad57 in DNA repair by increasing the stability of Rad51-DNA complexes
    • Fortin,G.S. and Symington,L.S. (2002) Mutations in yeast Rad51 that partially bypass the requirement for Rad55 and Rad57 in DNA repair by increasing the stability of Rad51-DNA complexes. EMBO J., 21 3160-3170.
    • (2002) EMBO J , vol.21 , pp. 3160-3170
    • Fortin, G.S.1    Symington, L.S.2
  • 36
    • 12844272179 scopus 로고    scopus 로고
    • Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence
    • Wu,Y., Qian,X., He,Y., Moya,I.A. and Luo,Y. (2005) Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence. J. Biol. Chem., 280, 722-728.
    • (2005) J. Biol. Chem , vol.280 , pp. 722-728
    • Wu, Y.1    Qian, X.2    He, Y.3    Moya, I.A.4    Luo, Y.5
  • 39
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong,I. and Lohman,T.M. (1993) A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions. Proc. Natl Acad. Sci. USA, 90, 5428-5432.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.M.2
  • 40
    • 0020971304 scopus 로고
    • Escherichia coli phage T4 topoisomerase
    • Kreuzer,K.N. and Jongeneel,C.V. (1983) Escherichia coli phage T4 topoisomerase. Methods Enzymol., 100, 144-160.
    • (1983) Methods Enzymol , vol.100 , pp. 144-160
    • Kreuzer, K.N.1    Jongeneel, C.V.2
  • 41
    • 0023135142 scopus 로고
    • Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
    • Kowalczykowski,S.C. and Krupp,R.A. (1987) Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA. J. Mol. Biol., 193, 97-113.
    • (1987) J. Mol. Biol , vol.193 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 42
    • 0141737560 scopus 로고    scopus 로고
    • NADH-coupled microplate photometric assay for kinetic studies of ATPhydrolyzing enzymes with low and high specific activities
    • Kiianitsa,K., Solinger,J.A. and Heyer,W.D. (2003) NADH-coupled microplate photometric assay for kinetic studies of ATPhydrolyzing enzymes with low and high specific activities. Anal. Biochem., 321, 266-271.
    • (2003) Anal. Biochem , vol.321 , pp. 266-271
    • Kiianitsa, K.1    Solinger, J.A.2    Heyer, W.D.3
  • 43
    • 0035902524 scopus 로고    scopus 로고
    • The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA
    • Ristic,D., Wyman,C., Paulusma,C. and Kanaar,R. (2001) The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA. Proc. Natl Acad. Sci. USA, 98, 8454-8460.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8454-8460
    • Ristic, D.1    Wyman, C.2    Paulusma, C.3    Kanaar, R.4
  • 44
    • 0029953512 scopus 로고    scopus 로고
    • Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis
    • Sung,P. and Stratton,S.A. (1996) Yeast Rad51 recombinase mediates polar DNA strand exchange in the absence of ATP hydrolysis. J. Biol. Chem. 271, 27983-27986.
    • (1996) J. Biol. Chem , vol.271 , pp. 27983-27986
    • Sung, P.1    Stratton, S.A.2
  • 46
    • 32644466860 scopus 로고    scopus 로고
    • Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function
    • Chi,P., Van Komen,S., Sehorn,M.G., Sigurdsson,S. and Sung,P. (2006) Roles of ATP binding and ATP hydrolysis in human Rad51 recombinase function. DNA Repair (Amst.), 5, 381-391.
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 381-391
    • Chi, P.1    Van Komen, S.2    Sehorn, M.G.3    Sigurdsson, S.4    Sung, P.5
  • 47
    • 0027397313 scopus 로고
    • Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation
    • Rehrauer,W.M. and Kowalczykowski,S.C. (1993) Alteration of the nucleoside triphosphate (NTP) catalytic domain within Escherichia coli recA protein attenuates NTP hydrolysis but not joint molecule formation. J. Biol. Chem., 268, 1292-1297.
    • (1993) J. Biol. Chem , vol.268 , pp. 1292-1297
    • Rehrauer, W.M.1    Kowalczykowski, S.C.2
  • 48
    • 0029961677 scopus 로고    scopus 로고
    • DNA strand exchange promoted by RecA K72R. Two reaction phases with different Mg2+ requirements
    • Shan,Q., Cox,M.M. and Inman,R.B. (1996) DNA strand exchange promoted by RecA K72R. Two reaction phases with different Mg2+ requirements. J. Biol. Chem., 271, 5712-5724.
    • (1996) J. Biol. Chem , vol.271 , pp. 5712-5724
    • Shan, Q.1    Cox, M.M.2    Inman, R.B.3
  • 49
    • 0036724688 scopus 로고    scopus 로고
    • The requirement for ATP hydrolysis by Saccharomyces cerevisiae Rad51 is bypassed by mating-type heterozygosity or RAD54 in high copy
    • Morgan,E.A., Shah,N. and Symington,L.S. (2002) The requirement for ATP hydrolysis by Saccharomyces cerevisiae Rad51 is bypassed by mating-type heterozygosity or RAD54 in high copy. Mol. Cell Biol., 22, 6336-6343.
    • (2002) Mol. Cell Biol , vol.22 , pp. 6336-6343
    • Morgan, E.A.1    Shah, N.2    Symington, L.S.3
  • 50
    • 0035053510 scopus 로고    scopus 로고
    • Effect of ions and nucleotides on the interactions of yeast Rad51 protein with single-stranded oligonucleotides
    • Kim,J.M., Maraboeuf,F., Kim,S.K., Shinohara,A. and Takahashi,M. (2001) Effect of ions and nucleotides on the interactions of yeast Rad51 protein with single-stranded oligonucleotides. J. Biochem. (Tokyo) 129, 469-475.
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 469-475
    • Kim, J.M.1    Maraboeuf, F.2    Kim, S.K.3    Shinohara, A.4    Takahashi, M.5
  • 51
    • 20844461121 scopus 로고    scopus 로고
    • Human Rad51 filaments on double- and single-stranded DNA: Correlating regular and irregular forms with recombination function
    • Ristic,D., Modesti,M., van der Heijden,T., van Noort,J., Dekker,C., Kanaar,R. and Wyman,C. (2005) Human Rad51 filaments on double- and single-stranded DNA: Correlating regular and irregular forms with recombination function. Nucleic Acids Res., 33, 3292-3302.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3292-3302
    • Ristic, D.1    Modesti, M.2    van der Heijden, T.3    van Noort, J.4    Dekker, C.5    Kanaar, R.6    Wyman, C.7
  • 52
    • 33745567940 scopus 로고    scopus 로고
    • Asp302 determines potassium dependence of a RadA recombinase from Methanococcus voltae
    • Qian,X., He,Y., Wu,Y. and Luo,Y. (2006) Asp302 determines potassium dependence of a RadA recombinase from Methanococcus voltae. J. Mol. Biol., 360, 537-547.
    • (2006) J. Mol. Biol , vol.360 , pp. 537-547
    • Qian, X.1    He, Y.2    Wu, Y.3    Luo, Y.4
  • 53
    • 33744965295 scopus 로고    scopus 로고
    • Complementation of one RecA protein point mutation by another. Evidence for trans catalysis of ATP hydrolysis
    • Cox,J.M., Abbott,S.N., Chitteni-Pattu,S., Inman,R.B. and Cox,M.M. (2006) Complementation of one RecA protein point mutation by another. Evidence for trans catalysis of ATP hydrolysis. J. Biol. Chem., 281, 12968-12975.
    • (2006) J. Biol. Chem , vol.281 , pp. 12968-12975
    • Cox, J.M.1    Abbott, S.N.2    Chitteni-Pattu, S.3    Inman, R.B.4    Cox, M.M.5
  • 54
    • 0034634390 scopus 로고    scopus 로고
    • The homologous pairing domain of RecA also mediates the allosteric regulation of DNA binding and ATP hydrolysis: A remarkable concentration of functional residues
    • Voloshin,O.N., Wang,L. and Camerini-Otero,R.D. (2000) The homologous pairing domain of RecA also mediates the allosteric regulation of DNA binding and ATP hydrolysis: A remarkable concentration of functional residues. J. Mol. Biol., 303, 709-720.
    • (2000) J. Mol. Biol , vol.303 , pp. 709-720
    • Voloshin, O.N.1    Wang, L.2    Camerini-Otero, R.D.3
  • 55
    • 0344097427 scopus 로고    scopus 로고
    • Saturation mutagenesis of the E. coli RecA loop L2 homologous DNA pairing region reveals residues essential for recombination and recombinational repair
    • Hortnagel,K., Voloshin,O.N., Kinal,H.H., Ma,N., Schaffer-Judge, C. and Camerini-Otero,R.D. (1999) Saturation mutagenesis of the E. coli RecA loop L2 homologous DNA pairing region reveals residues essential for recombination and recombinational repair. J. Mol. Biol., 286 1097-1106.
    • (1999) J. Mol. Biol , vol.286 , pp. 1097-1106
    • Hortnagel, K.1    Voloshin, O.N.2    Kinal, H.H.3    Ma, N.4    Schaffer-Judge, C.5    Camerini-Otero, R.D.6
  • 56
    • 14844355639 scopus 로고    scopus 로고
    • Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA
    • Ariza,A., Richard,D.J., White,M.F. and Bond,C.S. (2005) Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA. Nucleic Acids Res., 33, 1465-1473.
    • (2005) Nucleic Acids Res , vol.33 , pp. 1465-1473
    • Ariza, A.1    Richard, D.J.2    White, M.F.3    Bond, C.S.4
  • 57
    • 34247869930 scopus 로고    scopus 로고
    • Crystal structure of the left-handed archaeal RadA helical filament: Identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
    • Chen,L.T., Ko,T.P., Chang,Y.C., Lin,K.A., Chang,C.S., Wang,A.H. and Wang,T.F. (2007) Crystal structure of the left-handed archaeal RadA helical filament: Identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins. Nucleic Acids Res., 35, 1787-1801.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1787-1801
    • Chen, L.T.1    Ko, T.P.2    Chang, Y.C.3    Lin, K.A.4    Chang, C.S.5    Wang, A.H.6    Wang, T.F.7
  • 58
    • 0030633568 scopus 로고    scopus 로고
    • RecA protein: Structure, function, and role in recombinational DNA repair
    • Roca,A.I. and Cox,M.M. (1997) RecA protein: Structure, function, and role in recombinational DNA repair. Prog. Nucleic Acid. Res. Mol. Biol., 56, 129-223.
    • (1997) Prog. Nucleic Acid. Res. Mol. Biol , vol.56 , pp. 129-223
    • Roca, A.I.1    Cox, M.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.