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Volumn 33, Issue 12, 2005, Pages 3942-3952

Bacillus subtilis RecU Holliday-junction resolvase modulates RecA activities

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL DNA; CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE; DOUBLE STRANDED DNA; RECA PROTEIN; RECU PROTEIN; SINGLE STRANDED DNA; SINGLE STRANDED DNA BINDING PROTEIN; UNCLASSIFIED DRUG; 2'-DEOXYADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; DEOXYADENOSINE PHOSPHATE; DEOXYADENOSINE TRIPHOSPHATE; DNA BINDING PROTEIN;

EID: 22444436777     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gki713     Document Type: Article
Times cited : (54)

References (55)
  • 1
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • Kowalczykowski,S.C. (2000) Initiation of genetic recombination and recombination-dependent replication. Trends Biochem. Sci., 25 156-165.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 2
    • 0036228220 scopus 로고    scopus 로고
    • A novel family of regulated helicases/nucleases from Gram-positive bacteria: Insights into the initiation of DNA recombination
    • Chedin,F. and Kowalczykowski,S.C. (2002) A novel family of regulated helicases/nucleases from Gram-positive bacteria: Insights into the initiation of DNA recombination. Mol. Microbiol., 43, 823-834.
    • (2002) Mol. Microbiol. , vol.43 , pp. 823-834
    • Chedin, F.1    Kowalczykowski, S.C.2
  • 3
    • 0037126613 scopus 로고    scopus 로고
    • The RecOR proteins modulate RecA protein function at 5′ ends of single-stranded DNA
    • Bork,J.M., Cox,M.M. and Inman,R.B. (2001) The RecOR proteins modulate RecA protein function at 5′ ends of single-stranded DNA. EMBO J. 20, 7313-7322.
    • (2001) EMBO J. , vol.20 , pp. 7313-7322
    • Bork, J.M.1    Cox, M.M.2    Inman, R.B.3
  • 4
    • 0038392868 scopus 로고    scopus 로고
    • RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair
    • Morimatsu,K. and Kowalczykowski,S.C. (2003) RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair. Mol. Cell, 11, 1337-1347.
    • (2003) Mol. Cell , vol.11 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 6
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda
    • Kuzminov,A. (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda. Microbiol. Mol. Biol. Rev., 63, 751-813.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 7
    • 0033637253 scopus 로고    scopus 로고
    • Control of crossing over
    • Cromie,G.A. and Leach,D.R. (2000) Control of crossing over. Mol. Cell 6, 815-826.
    • (2000) Mol. Cell , vol.6 , pp. 815-826
    • Cromie, G.A.1    Leach, D.R.2
  • 8
    • 0029911725 scopus 로고    scopus 로고
    • Evidence for the coupling of ATP hydrolysis to the final (extension) phase of RecA protein-mediated DNA strand exchange
    • Bedale,W.A. and Cox,M. (1996) Evidence for the coupling of ATP hydrolysis to the final (extension) phase of RecA protein-mediated DNA strand exchange. J. Biol. Chem., 271, 5725-5732.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5725-5732
    • Bedale, W.A.1    Cox, M.2
  • 9
    • 0035902453 scopus 로고    scopus 로고
    • RecA protein promotes the regression of stalled replication forks in vitro
    • Robu,M.E., Inman,R.B. and Cox,M.M. (2001) RecA protein promotes the regression of stalled replication forks in vitro. Proc. Natl Acad. Sci. USA, 98, 8211-8218.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8211-8218
    • Robu, M.E.1    Inman, R.B.2    Cox, M.M.3
  • 10
    • 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. and Lloyd,R.G. (1993) Resolution of Holliday intermediates in recombination and DNA repair: Indirect suppression of ruvA, ruvB, and ruvC mutations. J. Bacteriol., 175, 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
  • 11
    • 4143135445 scopus 로고    scopus 로고
    • Single-molecule study of RuvAB-mediated Holliday-junction migration
    • Dawid,A., Croquette,V., Grigoriev,M. and Heslot,F. (2004) Single-molecule study of RuvAB-mediated Holliday-junction migration. Proc. Natl Acad. Sci. USA, 101, 11611-11616.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11611-11616
    • Dawid, A.1    Croquette, V.2    Grigoriev, M.3    Heslot, F.4
  • 12
    • 4143070381 scopus 로고    scopus 로고
    • Direct observation of RuvAB-catalyzed branch migration of single Holliday junctions
    • Amit,R., Gileadi,O. and Stavans,J. (2004) Direct observation of RuvAB-catalyzed branch migration of single Holliday junctions. Proc. Natl Acad. Sci. USA, 101, 11605-11610.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11605-11610
    • Amit, R.1    Gileadi, O.2    Stavans, J.3
  • 13
    • 0346374827 scopus 로고    scopus 로고
    • Bacillus subtilis RecU protein cleaves Holliday junctions and anneals single-stranded DNA
    • Ayora,S., Carrasco,B., Doncel,E., Lurz,R. and Alonso,J.C. (2004) Bacillus subtilis RecU protein cleaves Holliday junctions and anneals single-stranded DNA. Proc. Natl Acad. Sci. USA, 101, 452-457.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 452-457
    • Ayora, S.1    Carrasco, B.2    Doncel, E.3    Lurz, R.4    Alonso, J.C.5
  • 14
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • West,S.C. (1997) Processing of recombination intermediates by the RuvABC proteins. Annu. Rev. Genet., 31, 213-244.
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 15
    • 11244255422 scopus 로고    scopus 로고
    • The DinI and RecX proteins are competing modulators of RecA function
    • Lusetti,S.L., Drees,J.C., Stohl,E.A., Seifert,H.S. and Cox,M.M. (2004) The DinI and RecX proteins are competing modulators of RecA function. J. Biol. Chem., 279, 55073-55079.
    • (2004) J. Biol. Chem. , vol.279 , pp. 55073-55079
    • Lusetti, S.L.1    Drees, J.C.2    Stohl, E.A.3    Seifert, H.S.4    Cox, M.M.5
  • 16
    • 0037125994 scopus 로고    scopus 로고
    • RecX protein abrogates ATP hydrolysis and strand exchange promoted by RecA: Insights into negative regulation of homologous recombination
    • Venkatesh,R., Ganesh,N., Guhan,N., Reddy,M.S., Chandrasekhar,T. and Muniyappa,K. (2002) RecX protein abrogates ATP hydrolysis and strand exchange promoted by RecA: Insights into negative regulation of homologous recombination. Proc. Natl Acad. Sci. USA, 99, 12091-12096.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12091-12096
    • Venkatesh, R.1    Ganesh, N.2    Guhan, N.3    Reddy, M.S.4    Chandrasekhar, T.5    Muniyappa, K.6
  • 20
    • 0035112201 scopus 로고    scopus 로고
    • A model for the abrogation of the SOS response by an SOS protein: A negatively charged helix in DinI mimics DNA in its interaction with RecA
    • Voloshin,O.N., Ramirez,B.E., Bax,A. and Camerini-Otero,R.D. (2001) A model for the abrogation of the SOS response by an SOS protein: A negatively charged helix in DinI mimics DNA in its interaction with RecA. Genes Dev., 15, 415-427.
    • (2001) Genes Dev. , vol.15 , pp. 415-427
    • Voloshin, O.N.1    Ramirez, B.E.2    Bax, A.3    Camerini-Otero, R.D.4
  • 21
    • 0033119260 scopus 로고    scopus 로고
    • The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation
    • Churchill,J.J., Anderson,D.G. and Kowalczykowski,S.C. (1999) The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation. Genes Dev. 13, 901-911.
    • (1999) Genes Dev. , vol.13 , pp. 901-911
    • Churchill, J.J.1    Anderson, D.G.2    Kowalczykowski, S.C.3
  • 22
    • 0242384946 scopus 로고    scopus 로고
    • Rad51 recombinase and recombination mediators
    • Sung,P., Krejci,L., Van Komen,S. and Sehorn,M.G. (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
  • 23
    • 0000410142 scopus 로고
    • Homologous pairing in genetic recombination: Formation of D loops by combined action of RecA protein and a helix-destabilizing protein
    • Shibata,T., DasGupta,C., Cunningham,R.P. and Radding,C.M. (1990) Homologous pairing in genetic recombination: Formation of D loops by combined action of RecA protein and a helix-destabilizing protein. Proc. Natl Acad. Sci. USA, 77, 2606-2610.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2606-2610
    • Shibata, T.1    DasGupta, C.2    Cunningham, R.P.3    Radding, C.M.4
  • 24
    • 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
  • 25
    • 0028043495 scopus 로고
    • Dissociation of RecA filaments from duplex DNA by the RuvA and RuvB DNA repair proteins
    • Adams,D.E., Tsaneva,I.R. and West,S.C. (1994) Dissociation of RecA filaments from duplex DNA by the RuvA and RuvB DNA repair proteins. Proc. Natl Acad. Sci. USA, 91, 9901-9905.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9901-9905
    • Adams, D.E.1    Tsaneva, I.R.2    West, S.C.3
  • 26
    • 0029098812 scopus 로고
    • Blocked RecA protein-mediated DNA strand exchange reactions are reversed by the RuvA and RuvB proteins
    • Iype,L.E., Inman,R.B. and Cox,M.M. (1995) Blocked RecA protein-mediated DNA strand exchange reactions are reversed by the RuvA and RuvB proteins. J. Biol. Chem., 270, 19473-19480.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19473-19480
    • Iype, L.E.1    Inman, R.B.2    Cox, M.M.3
  • 27
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute,X., Jeusset,J., Soustelle,C., Kowalczykowski,S.C., Le Cam,E. and Fabre,F. (2003) The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments. Nature, 423, 309-312.
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 29
    • 13244252309 scopus 로고    scopus 로고
    • UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli
    • Veaute,X., Delmas,S., Selva,M., Jeusset,J., Le Cam,E., Matic,I., Fabre,F. and Petit,M.A. (2005) UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli. EMBO J. 24, 180-189.
    • (2005) EMBO J. , vol.24 , pp. 180-189
    • Veaute, X.1    Delmas, S.2    Selva, M.3    Jeusset, J.4    Le Cam, E.5    Matic, I.6    Fabre, F.7    Petit, M.A.8
  • 30
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco,P.R., Tracy,R.B. and Kowalczykowski,S.C. (1998) DNA strand exchange proteins: A biochemical and physical comparison. Front. Biosci., 3, D570-D603.
    • (1998) Front. Biosci. , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 31
    • 0038700698 scopus 로고    scopus 로고
    • Molecular views of recombination proteins and their control
    • West,S.C. (2003) Molecular views of recombination proteins and their control. Nature Rev. Mol. Cell Biol., 4, 435-445.
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 435-445
    • West, S.C.1
  • 33
    • 0035893241 scopus 로고    scopus 로고
    • Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange
    • Sigurdsson,S., Van Komen,S., Bussen,W., Schild,D., Albala,J.S. and Sung,P. (2001) Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange. Genes Dev., 15, 3308-3318.
    • (2001) Genes Dev. , vol.15 , pp. 3308-3318
    • Sigurdsson, S.1    Van Komen, S.2    Bussen, W.3    Schild, D.4    Albala, J.S.5    Sung, P.6
  • 35
    • 0037462657 scopus 로고    scopus 로고
    • Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro
    • Lio,Y.C., Mazin,A.V., Kowalczykowski,S.C. and Chen,D.J. (2003) Complex formation by the human Rad51B and Rad51C DNA repair proteins and their activities in vitro. J. Biol. Chem., 278, 2469-2478.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2469-2478
    • Lio, Y.C.1    Mazin, A.V.2    Kowalczykowski, S.C.3    Chen, D.J.4
  • 36
    • 3042676518 scopus 로고    scopus 로고
    • Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex
    • Yokoyama,H., Sarai,N., Kagawa,W., Enomoto,R., Shibata,T., Kurumizaka,H. and Yokoyama,S. (2004) Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex. Nucleic Acids Res., 32, 2556-2565.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2556-2565
    • Yokoyama, H.1    Sarai, N.2    Kagawa, W.3    Enomoto, R.4    Shibata, T.5    Kurumizaka, H.6    Yokoyama, S.7
  • 38
    • 0346850823 scopus 로고    scopus 로고
    • Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D)
    • Braybrooke,J.P., Li,J.L., Wu,L., Caple,F., Benson,F.E. and Hickson,I.D. (2003) Functional interaction between the Bloom's syndrome helicase and the RAD51 paralog, RAD51L3 (RAD51D). J. Biol. Chem., 278, 48357-48366.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48357-48366
    • Braybrooke, J.P.1    Li, J.L.2    Wu, L.3    Caple, F.4    Benson, F.E.5    Hickson, I.D.6
  • 39
    • 0346340054 scopus 로고    scopus 로고
    • RAD51C is required for Holliday junction processing in mammalian cells
    • Liu,Y., Masson,J.Y., Shah,R., O'Regan,P. and West,S.C. (2004) RAD51C is required for Holliday junction processing in mammalian cells. Science 303, 243-246.
    • (2004) Science , vol.303 , pp. 243-246
    • Liu, Y.1    Masson, J.Y.2    Shah, R.3    O'Regan, P.4    West, S.C.5
  • 40
    • 7044232011 scopus 로고    scopus 로고
    • Homologous recombination generates T-loop-sized deletions at human telomeres
    • Wang,R.C., Smogorzewska,A. and de Lange,T. (2004) Homologous recombination generates T-loop-sized deletions at human telomeres. Cell, 119, 355-368.
    • (2004) Cell , vol.119 , pp. 355-368
    • Wang, R.C.1    Smogorzewska, A.2    de Lange, T.3
  • 41
    • 24344457115 scopus 로고    scopus 로고
    • The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage
    • in press
    • McGregor,N., Ayora,S., Sedelnikova,S., Carrasco,B., Alonso,J.C., Thaw,P. and Rafferty,J.B. (2005) The structure of Bacillus subtilis RecU Holliday junction resolvase and its role in substrate selection and sequence specific cleavage. Structure, in press.
    • (2005) Structure
    • McGregor, N.1    Ayora, S.2    Sedelnikova, S.3    Carrasco, B.4    Alonso, J.C.5    Thaw, P.6    Rafferty, J.B.7
  • 42
    • 0037184023 scopus 로고    scopus 로고
    • Homologous-pairing activity of the Bacillus subtilis bacteriophage SPP1 replication protein G35P
    • Ayora,S., Missich,R., Mesa,P., Lurz,R., Yang,S., Egelman,E.H. and Alonso,J.C. (2002) Homologous-pairing activity of the Bacillus subtilis bacteriophage SPP1 replication protein G35P. J. Biol. Chem., 277, 35969-35979.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35969-35979
    • Ayora, S.1    Missich, R.2    Mesa, P.3    Lurz, R.4    Yang, S.5    Egelman, E.H.6    Alonso, J.C.7
  • 43
    • 0024724761 scopus 로고
    • Expression of the recE gene during induction of the SOS response in Bacillus subtilis recombination-deficient strains
    • Gassel,M. and Alonso,J.C. (1989) Expression of the recE gene during induction of the SOS response in Bacillus subtilis recombination-deficient strains. Mol. Microbiol., 3, 1269-1276.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1269-1276
    • Gassel, M.1    Alonso, J.C.2
  • 44
    • 0027968224 scopus 로고
    • Nucleotide sequence and complementation studies of the gene 35 region of the Bacillus subtilis bacteriophage SPP1
    • Weise,F., Chai,S., Luder,G. and Alonso,J.C. (1994) Nucleotide sequence and complementation studies of the gene 35 region of the Bacillus subtilis bacteriophage SPP1. Virology, 202, 1046-1049.
    • (1994) Virology , vol.202 , pp. 1046-1049
    • Weise, F.1    Chai, S.2    Luder, G.3    Alonso, J.C.4
  • 45
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill,S.C. and von Hippel,P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem., 182 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 48
    • 0028308710 scopus 로고
    • Homologous pairing and DNA strand-exchange proteins
    • Kowalczykowski,S.C. and Eggleston,A.K. (1994) Homologous pairing and DNA strand-exchange proteins. Annu. Rev. Biochem., 63, 991-1043.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 991-1043
    • Kowalczykowski, S.C.1    Eggleston, A.K.2
  • 49
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
    • Lusetti,S.L. and Cox,M.M. (2002) The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. Annu. Rev. Biochem., 71, 71-100.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2
  • 50
    • 0021970138 scopus 로고
    • Purification of a RecA protein analogue from Bacillus subtilis
    • Lovett,C.M.,Jr and Roberts,J.W. (1985) Purification of a RecA protein analogue from Bacillus subtilis. J. Biol. Chem., 260, 3305-3313.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3305-3313
    • Lovett Jr., C.M.1    Roberts, J.W.2
  • 51
    • 0033543543 scopus 로고    scopus 로고
    • Reevaluation of the nucleotide cofactor specificity of the RecA protein from Bacillus subtilis
    • Steffen,S.E. and Bryant,F.R. (1999) Reevaluation of the nucleotide cofactor specificity of the RecA protein from Bacillus subtilis. J. Biol. Chem., 274, 25990-25994.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25990-25994
    • Steffen, S.E.1    Bryant, F.R.2
  • 52
    • 26444464002 scopus 로고    scopus 로고
    • Caracterización de la proteína RecU de Bacillus subtilis 168
    • Estudio de su papel en la recombinación y segregación cromosómica, PhD, Thesis Universidad Autónoma de Madrid, Madrid, Spain
    • Doncel-Pérez,E. (2002) Caracterización de la proteína RecU de Bacillus subtilis 168. Estudio de su papel en la recombinación y segregación cromosómica, PhD, Thesis Universidad Autónoma de Madrid, Madrid, Spain.
    • (2002)
    • Doncel-Pérez, E.1
  • 53
    • 0031004885 scopus 로고    scopus 로고
    • A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein
    • Sugiyama,T., Zaitseva,E.M. and Kowalczykowski,S.C. (1997) A single-stranded DNA-binding protein is needed for efficient presynaptic complex formation by the Saccharomyces cerevisiae Rad51 protein. J. Biol. Chem., 272, 7940-7945.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7940-7945
    • Sugiyama, T.1    Zaitseva, E.M.2    Kowalczykowski, S.C.3
  • 54
    • 0024378045 scopus 로고
    • Enhancement of Escherichia coli RecA protein enzymatic function by dATP
    • Menetski,J.P. and Kowalczykowski,S.C. (1989) Enhancement of Escherichia coli RecA protein enzymatic function by dATP. Biochemistry, 28, 5871-5881.
    • (1989) Biochemistry , vol.28 , pp. 5871-5881
    • Menetski, J.P.1    Kowalczykowski, S.C.2
  • 55
    • 0034714309 scopus 로고    scopus 로고
    • Cleavage of Holliday junctions by the Escherichia coli RuvABC complex
    • Eggleston,A.K. and West,S.C. (2000) Cleavage of Holliday junctions by the Escherichia coli RuvABC complex. J. Biol. Chem., 275 26467-26476.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26467-26476
    • Eggleston, A.K.1    West, S.C.2


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