메뉴 건너뛰기




Volumn 4, Issue September 2015, 2015, Pages

Imaging and energetics of single SSB-ssDNA molecules reveal intramolecular condensation and insight into RecOR function

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOPROTEIN; SINGLE STRANDED DNA BINDING PROTEIN; DNA BINDING PROTEIN; ESCHERICHIA COLI PROTEIN; PROTEIN BINDING; RECO PROTEIN, E COLI; RECR PROTEIN, E COLI; SINGLE STRANDED DNA; SSB PROTEIN, E COLI;

EID: 84949952959     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.08646     Document Type: Article
Times cited : (52)

References (66)
  • 1
    • 0021929046 scopus 로고
    • Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
    • Alatossava T, Jutte H, Kuhn A, Kellenberger E. 1985. Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187. Journal of Bacteriology 162:413-419.
    • (1985) Journal of Bacteriology , vol.162 , pp. 413-419
    • Alatossava, T.1    Jutte, H.2    Kuhn, A.3    Kellenberger, E.4
  • 4
    • 84868615392 scopus 로고    scopus 로고
    • Direct imaging of RecA nucleation and growth on single molecules of SSB-coated ssDNA
    • Bell JC, Plank JL, Dombrowski CC, Kowalczykowski SC. 2012. Direct imaging of RecA nucleation and growth on single molecules of SSB-coated ssDNA. Nature 491:274-278. doi: 10.1038/nature11598.
    • (2012) Nature , vol.491 , pp. 274-278
    • Bell, J.C.1    Plank, J.L.2    Dombrowski, C.C.3    Kowalczykowski, S.C.4
  • 5
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg OG, Winter RB, von Hippel PH. 1981. Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory. Biochemistry 20:6929-6948. doi: 10.1021/bi00527a028.
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 7
    • 84896701202 scopus 로고    scopus 로고
    • Elastic properties and secondary structure formation of single-stranded DNA at monovalent and divalent salt conditions
    • Bosco A, Camunas-Soler J, Ritort F. 2014. Elastic properties and secondary structure formation of single-stranded DNA at monovalent and divalent salt conditions. Nucleic Acids Research 42:2064-2074. doi: 10.1093/nar/gkt1089.
    • (2014) Nucleic Acids Research , vol.42 , pp. 2064-2074
    • Bosco, A.1    Camunas-Soler, J.2    Ritort, F.3
  • 8
    • 0023040461 scopus 로고
    • Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA
    • Bujalowski W, Lohman TM. 1986. Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA. Biochemistry 25:7799-7802. doi: 10.1021/bi00372a003.
    • (1986) Biochemistry , vol.25 , pp. 7799-7802
    • Bujalowski, W.1    Lohman, T.M.2
  • 9
    • 0023660486 scopus 로고
    • Limited co-operativity in protein-nucleic acid interactions. A thermodynamic model for the interactions of Escherichia coli single strand binding protein with single-stranded nucleic acids in the"beaded", (SSB)65 mode
    • Bujalowski W, Lohman TM. 1987. Limited co-operativity in protein-nucleic acid interactions. A thermodynamic model for the interactions of Escherichia coli single strand binding protein with single-stranded nucleic acids in the"beaded", (SSB)65 mode. Journal of Molecular Biology 195:897-907. doi: 10.1016/0022-2836(87)90493-1.
    • (1987) Journal of Molecular Biology , vol.195 , pp. 897-907
    • Bujalowski, W.1    Lohman, T.M.2
  • 10
    • 0024403429 scopus 로고
    • Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model
    • Bujalowski W, Lohman TM. 1989a. Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model. Journal of Molecular Biology 207:249-268. doi: 10.1016/0022-2836(89)90454-3.
    • (1989) Journal of Molecular Biology , vol.207 , pp. 249-268
    • Bujalowski, W.1    Lohman, T.M.2
  • 11
    • 0024356728 scopus 로고
    • Negative co-operativity in Escherichia coli single strand binding protein- oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effects
    • Bujalowski W, Lohman TM. 1989b. Negative co-operativity in Escherichia coli single strand binding protein- oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effects. Journal of Molecular Biology 207:269-288. doi: 10.1016/0022-2836(89)90455-5.
    • (1989) Journal of Molecular Biology , vol.207 , pp. 269-288
    • Bujalowski, W.1    Lohman, T.M.2
  • 12
    • 0023916373 scopus 로고
    • Binding mode transitions of Escherichia coli single strand binding protein-single-stranded DNA complexes. Cation, anion, pH, and binding density effects
    • Bujalowski W, Overman LB, Lohman TM. 1988. Binding mode transitions of Escherichia coli single strand binding protein-single-stranded DNA complexes. Cation, anion, pH, and binding density effects. The Journal of Biological Chemistry 263:4629-4640.
    • (1988) The Journal of Biological Chemistry , vol.263 , pp. 4629-4640
    • Bujalowski, W.1    Overman, L.B.2    Lohman, T.M.3
  • 13
    • 13444282478 scopus 로고    scopus 로고
    • PriA helicase and SSB interact physically and functionally
    • Cadman CJ, McGlynn P. 2004. PriA helicase and SSB interact physically and functionally. Nucleic Acids Research 32:6378-6387. doi: 10.1093/nar/gkh980.
    • (2004) Nucleic Acids Research , vol.32 , pp. 6378-6387
    • Cadman, C.J.1    McGlynn, P.2
  • 14
    • 0343470642 scopus 로고
    • Escherichia coli single-strand binding protein organizes single-stranded DNA in nucleosome-like units
    • Chrysogelos S, Griffith J. 1982. Escherichia coli single-strand binding protein organizes single-stranded DNA in nucleosome-like units. Proceedings of the National Academy of Sciences of USA 79:5803-5807. doi: 10.1073/ pnas.79.19.5803.
    • (1982) Proceedings of the National Academy of Sciences of USA , vol.79 , pp. 5803-5807
    • Chrysogelos, S.1    Griffith, J.2
  • 15
    • 55949111485 scopus 로고    scopus 로고
    • Fluorescent single-stranded DNA binding protein as a probe for sensitive, real-time assays of helicase activity
    • Dillingham MS, Tibbles KL, Hunter JL, Bell JC, Kowalczykowski SC, Webb MR. 2008. Fluorescent single-stranded DNA binding protein as a probe for sensitive, real-time assays of helicase activity. Biophysical Journal 95:3330-3339. doi: 10.1529/biophysj.108.13351.
    • (2008) Biophysical Journal , vol.95 , pp. 3330-3339
    • Dillingham, M.S.1    Tibbles, K.L.2    Hunter, J.L.3    Bell, J.C.4    Kowalczykowski, S.C.5    Webb, M.R.6
  • 16
    • 85005627207 scopus 로고
    • Cation transport in Escherichia coli: V. Regulation of cation content
    • Epstein W, Schultz SG. 1965. Cation transport in Escherichia coli: V. Regulation of cation content. The Journal of General Physiology 49:221-234. doi: 10.1085/jgp.49.2.221.
    • (1965) The Journal of General Physiology , vol.49 , pp. 221-234
    • Epstein, W.1    Schultz, S.G.2
  • 17
    • 0013862077 scopus 로고
    • Cation transport in Escherichia coli. VI. K exchange
    • Epstein W, Schultz SG. 1966. Cation transport in Escherichia coli. VI. K exchange. The Journal of General Physiology 49:469-481. doi: 10.1085/jgp.49.3.469.
    • (1966) The Journal of General Physiology , vol.49 , pp. 469-481
    • Epstein, W.1    Schultz, S.G.2
  • 18
    • 0028175289 scopus 로고
    • Co-operative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB)35 binding mode
    • Ferrari ME, Bujalowski W, Lohman TM. 1994. Co-operative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB)35 binding mode. Journal of Molecular Biology 236:106-123. doi: 10.1006/jmbi.1994.1122.
    • (1994) Journal of Molecular Biology , vol.236 , pp. 106-123
    • Ferrari, M.E.1    Bujalowski, W.2    Lohman, T.M.3
  • 19
    • 77952545470 scopus 로고    scopus 로고
    • Single-molecule imaging brings Rad51 nucleoprotein filaments into focus
    • Forget AL, Kowalczykowski SC. 2010. Single-molecule imaging brings Rad51 nucleoprotein filaments into focus. Trends in Cell Biology 20:269-276. doi: 10.1016/j.tcb.2010.02.004.
    • (2010) Trends in Cell Biology , vol.20 , pp. 269-276
    • Forget, A.L.1    Kowalczykowski, S.C.2
  • 20
    • 84857118715 scopus 로고    scopus 로고
    • Single-molecule imaging of DNA pairing by RecA reveals a three-dimensional homology search
    • Forget AL, Kowalczykowski SC. 2012. Single-molecule imaging of DNA pairing by RecA reveals a three-dimensional homology search. Nature 482:423-427. doi: 10.1038/nature10782.
    • (2012) Nature , vol.482 , pp. 423-427
    • Forget, A.L.1    Kowalczykowski, S.C.2
  • 21
    • 84896873779 scopus 로고    scopus 로고
    • Concentration-dependent exchange of replication protein A on single-stranded DNA revealed by single-molecule imaging
    • Gibb B, Ye LF, Gergoudis SC, Kwon Y, Niu H, Sung P, Greene EC. 2014. Concentration-dependent exchange of replication protein A on single-stranded DNA revealed by single-molecule imaging. PLOS ONE 9:e87922. doi: 10.1371/journal.pone.0087922.
    • (2014) PLOS ONE , vol.9
    • Gibb, B.1    Ye, L.F.2    Gergoudis, S.C.3    Kwon, Y.4    Niu, H.5    Sung, P.6    Greene, E.C.7
  • 22
    • 0036111913 scopus 로고    scopus 로고
    • Magnetic tweezers: Micromanipulation and force measurement at the molecular level
    • Gosse C, Croquette V. 2002. Magnetic tweezers: micromanipulation and force measurement at the molecular level. Biophysical Journal 82:3314-3329. doi: 10.1016/S0006-3495(02)75672-5.
    • (2002) Biophysical Journal , vol.82 , pp. 3314-3329
    • Gosse, C.1    Croquette, V.2
  • 25
    • 66149130735 scopus 로고    scopus 로고
    • Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. Coli
    • Handa N, Morimatsu K, Lovett ST, Kowalczykowski SC. 2009. Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli. Genes & Development 23:1234-1245. doi: 10.1101/gad. 1780709.
    • (2009) Genes & Development , vol.23 , pp. 1234-1245
    • Handa, N.1    Morimatsu, K.2    Lovett, S.T.3    Kowalczykowski, S.C.4
  • 26
    • 0037180443 scopus 로고    scopus 로고
    • Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: A common step in genetic recombination
    • Kantake N, Madiraju MV, Sugiyama T, Kowalczykowski SC. 2002. Escherichia coli RecO protein anneals ssDNA complexed with its cognate ssDNA-binding protein: a common step in genetic recombination. Proceedings of the National Academy of Sciences of USA 99:15327-15332. doi: 10.1073/pnas.252633399.
    • (2002) Proceedings of the National Academy of Sciences of USA , vol.99 , pp. 15327-15332
    • Kantake, N.1    Madiraju, M.V.2    Sugiyama, T.3    Kowalczykowski, S.C.4
  • 27
    • 84862945756 scopus 로고    scopus 로고
    • Direct characterization of protein oligomers and their quaternary structures by single-molecule FRET
    • Kim C, Kim JY, Kim SH, Lee BI, Lee NK. 2012. Direct characterization of protein oligomers and their quaternary structures by single-molecule FRET. Chemical Communications 48:1138-1140. doi: 10.1039/c2cc16528g.
    • (2012) Chemical Communications , vol.48 , pp. 1138-1140
    • Kim, C.1    Kim, J.Y.2    Kim, S.H.3    Lee, B.I.4    Lee, N.K.5
  • 28
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • Kowalczykowski SC, Lonberg N, Newport JW, von Hippel PH. 1981. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions. Journal of Molecular Biology 145:75-104. doi: 10.1016/0022-2836(81)90335-1.
    • (1981) Journal of Molecular Biology , vol.145 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.H.4
  • 29
    • 77952783935 scopus 로고    scopus 로고
    • Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein
    • Kozlov AG, Cox MM, Lohman TM. 2010a. Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein. The Journal of Biological Chemistry 285:17246-17252. doi: 10.1074/jbc.M110.118273.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 17246-17252
    • Kozlov, A.G.1    Cox, M.M.2    Lohman, T.M.3
  • 30
    • 77951690386 scopus 로고    scopus 로고
    • Binding specificity of Escherichia coli single-stranded DNA binding protein for the chi subunit of DNA pol III holoenzyme and PriA helicase
    • Kozlov AG, Jezewska MJ, Bujalowski W, Lohman TM. 2010b. Binding specificity of Escherichia coli single-stranded DNA binding protein for the chi subunit of DNA pol III holoenzyme and PriA helicase. Biochemistry 49:3555-3566. doi: 10.1021/bi100069s.
    • (2010) Biochemistry , vol.49 , pp. 3555-3566
    • Kozlov, A.G.1    Jezewska, M.J.2    Bujalowski, W.3    Lohman, T.M.4
  • 31
    • 0036786227 scopus 로고    scopus 로고
    • Kinetic mechanism of direct transfer of Escherichia coli SSB tetramers between single-stranded DNA molecules
    • Kozlov AG, Lohman TM. 2002a. Kinetic mechanism of direct transfer of Escherichia coli SSB tetramers between single-stranded DNA molecules. Biochemistry 41:11611-11627. doi: 10.1021/bi020361m.
    • (2002) Biochemistry , vol.41 , pp. 11611-11627
    • Kozlov, A.G.1    Lohman, T.M.2
  • 32
    • 0037076536 scopus 로고    scopus 로고
    • Stopped-flow studies of the kinetics of single-stranded DNA binding and wrapping around the Escherichia coli SSB tetramer
    • Kozlov AG, Lohman TM. 2002b. Stopped-flow studies of the kinetics of single-stranded DNA binding and wrapping around the Escherichia coli SSB tetramer. Biochemistry 41:6032-6044. doi: 10.1021/bi020122z.
    • (2002) Biochemistry , vol.41 , pp. 6032-6044
    • Kozlov, A.G.1    Lohman, T.M.2
  • 34
    • 84901768289 scopus 로고    scopus 로고
    • Ultrafast redistribution of E. Coli SSB along long single-stranded DNA via intersegment transfer
    • Lee KS, Marciel AB, Kozlov AG, Schroeder CM, Lohman TM, Ha T. 2014. Ultrafast redistribution of E. coli SSB along long single-stranded DNA via intersegment transfer. Journal of Molecular Biology 426:2413-2421. doi: 10.1016/j.jmb.2014.04.023.
    • (2014) Journal of Molecular Biology , vol.426 , pp. 2413-2421
    • Lee, K.S.1    Marciel, A.B.2    Kozlov, A.G.3    Schroeder, C.M.4    Lohman, T.M.5    Ha, T.6
  • 35
    • 0037036070 scopus 로고    scopus 로고
    • Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski’s equality
    • Liphardt J, Dumont S, Smith SB, Tinoco I Jr, Bustamante C. 2002. Equilibrium information from nonequilibrium measurements in an experimental test of Jarzynski’s equality. Science 296:1832-1835. doi: 10.1126/science.1071152.
    • (2002) Science , vol.296 , pp. 1832-1835
    • Liphardt, J.1    Dumont, S.2    Smith, S.B.3    Tinoco, I.4    Bustamante, C.5
  • 36
    • 0024278440 scopus 로고
    • Negative cooperativity within individual tetramers of Escherichia coli single strand binding protein is responsible for the transition between the (SSB)35 and (SSB)56 DNA binding modes
    • Lohman TM, Bujalowski W. 1988. Negative cooperativity within individual tetramers of Escherichia coli single strand binding protein is responsible for the transition between the (SSB)35 and (SSB)56 DNA binding modes. Biochemistry 27:2260-2265. doi: 10.1021/bi00407a002.
    • (1988) Biochemistry , vol.27 , pp. 2260-2265
    • Lohman, T.M.1    Bujalowski, W.2
  • 37
    • 0028246888 scopus 로고
    • Escherichia coli single-stranded DNA-binding protein: Multiple DNA-binding modes and cooperativities
    • Lohman TM, Ferrari ME. 1994. Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities. Annual Review of Biochemistry 63:527-570. doi: 10.1146/annurev.bi.63.070194.002523.
    • (1994) Annual Review of Biochemistry , vol.63 , pp. 527-570
    • Lohman, T.M.1    Ferrari, M.E.2
  • 38
    • 0021920551 scopus 로고
    • Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration
    • Lohman TM, Overman LB. 1985. Two binding modes in Escherichia coli single strand binding protein-single stranded DNA complexes. Modulation by NaCl concentration. The Journal of Biological Chemistry 260:3594-3603.
    • (1985) The Journal of Biological Chemistry , vol.260 , pp. 3594-3603
    • Lohman, T.M.1    Overman, L.B.2
  • 39
    • 0022542165 scopus 로고
    • Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein
    • Lohman TM, Overman LB, Datta S. 1986. Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein. Journal of Molecular Biology 187:603-615. doi: 10.1016/0022-2836(86)90338-4.
    • (1986) Journal of Molecular Biology , vol.187 , pp. 603-615
    • Lohman, T.M.1    Overman, L.B.2    Datta, S.3
  • 40
    • 48249095036 scopus 로고    scopus 로고
    • Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I
    • Lu D, Keck JL. 2008. Structural basis of Escherichia coli single-stranded DNA-binding protein stimulation of exonuclease I. Proceedings of the National Academy of Sciences of USA 105:9169-9174. doi: 10.1073/pnas.0800741105.
    • (2008) Proceedings of the National Academy of Sciences of USA , vol.105 , pp. 9169-9174
    • Lu, D.1    Keck, J.L.2
  • 42
    • 34147224324 scopus 로고
    • The single-stranded DNA-binding protein of Escherichia coli
    • Meyer RR, Laine PS. 1990. The single-stranded DNA-binding protein of Escherichia coli. Microbiological Reviews 54:342-380.
    • (1990) Microbiological Reviews , vol.54 , pp. 342-380
    • Meyer, R.R.1    Laine, P.S.2
  • 43
    • 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, Kowalczykowski SC. 2003. RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: a universal step of recombinational repair. Molecular Cell 11:1337-1347. doi: 10.1016/S1097-2765(03)00188-6.
    • (2003) Molecular Cell , vol.11 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 44
    • 84867406977 scopus 로고    scopus 로고
    • RecFOR proteins target RecA protein to a DNA gap with either DNA or RNA at the 5’ terminus: Implication for repair of stalled replication forks
    • Morimatsu K, Wu Y, Kowalczykowski SC. 2012. RecFOR proteins target RecA protein to a DNA gap with either DNA or RNA at the 5’ terminus: implication for repair of stalled replication forks. The Journal of Biological Chemistry 287:35621-35630. doi: 10.1074/jbc.M112.397034.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 35621-35630
    • Morimatsu, K.1    Wu, Y.2    Kowalczykowski, S.C.3
  • 46
    • 0019349524 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA
    • Newport JW, Lonberg N, Kowalczykowski SC, von Hippel PH. 1981. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. II. Specificity of binding to DNA and RNA. Journal of Molecular Biology 145:105-121. doi: 10.1016/0022-2836(81)90336-3.
    • (1981) Journal of Molecular Biology , vol.145 , pp. 105-121
    • Newport, J.W.1    Lonberg, N.2    Kowalczykowski, S.C.3    Von Hippel, P.H.4
  • 47
    • 84930632519 scopus 로고    scopus 로고
    • Interaction with single-stranded DNA-binding protein stimulates Escherichia coli Ribonuclease HI enzymatic activity
    • Petzold C, Marceau AH, Miller KH, Marqusee S, Keck JL. 2015. Interaction with single-stranded DNA-binding protein stimulates Escherichia coli Ribonuclease HI enzymatic activity. The Journal of Biological Chemistry 290:14626-14636. doi: 10.1074/jbc.M115.655134.
    • (2015) The Journal of Biological Chemistry , vol.290 , pp. 14626-14636
    • Petzold, C.1    Marceau, A.H.2    Miller, K.H.3    Marqusee, S.4    Keck, J.L.5
  • 48
    • 84887275455 scopus 로고    scopus 로고
    • An’open’ structure of the RecOR complex supports ssDNA binding within the core of the complex
    • Radzimanowski J, Dehez F, Round A, Bidon-Chanal A, McSweeney S, Timmins J. 2013. An’open’ structure of the RecOR complex supports ssDNA binding within the core of the complex. Nucleic Acids Research 41:7972-7986. doi: 10.1093/nar/gkt572.
    • (2013) Nucleic Acids Research , vol.41 , pp. 7972-7986
    • Radzimanowski, J.1    Dehez, F.2    Round, A.3    Bidon-Chanal, A.4    McSweeney, S.5    Timmins, J.6
  • 49
    • 0023664450 scopus 로고
    • Variability of the intracellular ionic environment of Escherichia coli. Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression
    • Richey B, Cayley DS, Mossing MC, Kolka C, Anderson CF, Farrar TC, Record MT Jr. 1987. Variability of the intracellular ionic environment of Escherichia coli. Differences between in vitro and in vivo effects of ion concentrations on protein-DNA interactions and gene expression. The Journal of Biological Chemistry 262:7157-7164.
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 7157-7164
    • Richey, B.1    Cayley, D.S.2    Mossing, M.C.3    Kolka, C.4    Erson, C.F.5    Farrar, T.C.6    Record, M.T.7
  • 51
    • 70350488396 scopus 로고    scopus 로고
    • SSB protein diffusion on single-stranded DNA stimulates RecA filament formation
    • Roy R, Kozlov AG, Lohman TM, Ha T. 2009. SSB protein diffusion on single-stranded DNA stimulates RecA filament formation. Nature 461:1092-1097. doi: 10.1038/nature08442.
    • (2009) Nature , vol.461 , pp. 1092-1097
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 52
    • 79960790784 scopus 로고    scopus 로고
    • Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein
    • Ryzhikov M, Koroleva O, Postnov D, Tran A, Korolev S. 2011. Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein. Nucleic Acids Research 39:6305-6314. doi: 10.1093/nar/gkr199.
    • (2011) Nucleic Acids Research , vol.39 , pp. 6305-6314
    • Ryzhikov, M.1    Koroleva, O.2    Postnov, D.3    Tran, A.4    Korolev, S.5
  • 54
    • 0026179448 scopus 로고
    • Structure and dynamics of the complex of single stranded DNA binding protein of Escherichia coli with circular single stranded DNA of filamentous phages
    • Schaper A, Urbanke C, Kohring GW, Maass G. 1991. Structure and dynamics of the complex of single stranded DNA binding protein of Escherichia coli with circular single stranded DNA of filamentous phages. Journal of Biomolecular Structure & Dynamics 8:1233-1250. doi: 10.1080/07391102.1991.10507880.
    • (1991) Journal of Biomolecular Structure & Dynamics , vol.8 , pp. 1233-1250
    • Schaper, A.1    Urbanke, C.2    Kohring, G.W.3    Maass, G.4
  • 55
    • 0000218405 scopus 로고
    • Linear cooperative binding of large ligands involving mutual exclusion of different binding modes
    • Schwarz G, Stankowski S. 1979. Linear cooperative binding of large ligands involving mutual exclusion of different binding modes. Biophysical Chemistry 10:173-181. doi: 10.1016/0301-4622(79)85037-1.
    • (1979) Biophysical Chemistry , vol.10 , pp. 173-181
    • Schwarz, G.1    Stankowski, S.2
  • 56
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in Escherichia coli RecQ DNA helicase function
    • Shereda RD, Bernstein DA, Keck JL. 2007. A central role for SSB in Escherichia coli RecQ DNA helicase function. The Journal of Biological Chemistry 282:19247-19258. doi: 10.1074/jbc.M608011200.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 58
    • 0030024985 scopus 로고    scopus 로고
    • Overstretching B-DNA: The elastic response of individual double-stranded and single-stranded DNA molecules
    • Smith SB, Cui Y, Bustamante C. 1996. Overstretching B-DNA: the elastic response of individual double-stranded and single-stranded DNA molecules. Science 271:795-799. doi: 10.1126/science.271.5250.795.
    • (1996) Science , vol.271 , pp. 795-799
    • Smith, S.B.1    Cui, Y.2    Bustamante, C.3
  • 60
    • 84928967106 scopus 로고    scopus 로고
    • Remodeling of RecG helicase at the DNA replication Fork by SSB protein
    • Sun Z, Tan HY, Bianco PR, Lyubchenko YL. 2015. Remodeling of RecG helicase at the DNA replication Fork by SSB protein. Scientific Reports 5:9625. doi: 10.1038/srep09625.
    • (2015) Scientific Reports , vol.5 , pp. 9625
    • Sun, Z.1    Tan, H.Y.2    Bianco, P.R.3    Lyubchenko, Y.L.4
  • 61
    • 0027238208 scopus 로고
    • Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein
    • Umezu K, Chi NW, Kolodner RD. 1993. Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein. Proceedings of the National Academy of Sciences of USA 90:3875-3879. doi: 10.1073/pnas.90.9.3875.
    • (1993) Proceedings of the National Academy of Sciences of USA , vol.90 , pp. 3875-3879
    • Umezu, K.1    Chi, N.W.2    Kolodner, R.D.3
  • 62
    • 0028034452 scopus 로고
    • Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein
    • Umezu K, Kolodner RD. 1994. Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein. The Journal of Biological Chemistry 269:30005-30013.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 30005-30013
    • Umezu, K.1    Kolodner, R.D.2
  • 63
    • 84879034275 scopus 로고    scopus 로고
    • PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein
    • Wessel SR, Marceau AH, Massoni SC, Zhou R, Ha T, Sandler SJ, Keck JL. 2013. PriC-mediated DNA replication restart requires PriC complex formation with the single-stranded DNA-binding protein. The Journal of Biological Chemistry 288:17569-17578. doi: 10.1074/jbc.M113.478156.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 17569-17578
    • Wessel, S.R.1    Marceau, A.H.2    Massoni, S.C.3    Zhou, R.4    Ha, T.5    Sandler, S.J.6    Keck, J.L.7
  • 65
    • 0034901419 scopus 로고    scopus 로고
    • Stretching single-stranded DNA: Interplay of electrostatic, base-pairing, and base-pair stacking interactions
    • Zhang Y, Zhou H, Ou-Yang ZC. 2001. Stretching single-stranded DNA: interplay of electrostatic, base-pairing, and base-pair stacking interactions. Biophysical Journal 81:1133-1143. doi: 10.1016/S0006-3495(01)75770-0.
    • (2001) Biophysical Journal , vol.81 , pp. 1133-1143
    • Zhang, Y.1    Zhou, H.2    Ou-Yang, Z.C.3
  • 66
    • 79960804204 scopus 로고    scopus 로고
    • SSB functions as a sliding platform that migrates on DNA via reptation
    • Zhou R, Kozlov AG, Roy R, Zhang J, Korolev S, Lohman TM, Ha T. 2011. SSB functions as a sliding platform that migrates on DNA via reptation. Cell 146:222-232. doi: 10.1016/j.cell.2011.06.036.
    • (2011) Cell , vol.146 , pp. 222-232
    • Zhou, R.1    Kozlov, A.G.2    Roy, R.3    Zhang, J.4    Korolev, S.5    Lohman, T.M.6    Ha, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.