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Volumn 353, Issue 4, 2005, Pages 822-837

Determinants of specific binding of HMGB1 protein to hemicatenated DNA loops

Author keywords

Alternative DNA conformations; DNA knot and hemicatenane; DNA topoisomers fractionation in chloroquine gels; High mobility group proteins; HMG box domain

Indexed keywords

DNA; DNA Z; EXODEOXYRIBONUCLEASE III; HIGH MOBILITY GROUP B1 PROTEIN; MAGNESIUM;

EID: 26844469813     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.08.073     Document Type: Article
Times cited : (36)

References (76)
  • 1
    • 0035282078 scopus 로고    scopus 로고
    • Revised nomenclature for high mobility group (HMG) chromosomal proteins
    • M. Bustin Revised nomenclature for high mobility group (HMG) chromosomal proteins Trends Biochem. Sci. 26 2001 152 153
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 152-153
    • Bustin, M.1
  • 2
    • 0029070956 scopus 로고
    • The HMG-1 box protein family: Classification and functional relationships
    • A.D. Baxevanis, and D. Landsman The HMG-1 box protein family: classification and functional relationships Nucl. Acids Res. 23 1995 1604 1613
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Landsman, D.2
  • 3
    • 0033559518 scopus 로고    scopus 로고
    • From head to toes: The multiple facets of Sox proteins
    • M. Wegner From head to toes: the multiple facets of Sox proteins Nucl. Acids Res. 27 1999 1409 1420
    • (1999) Nucl. Acids Res. , vol.27 , pp. 1409-1420
    • Wegner, M.1
  • 4
    • 0032471965 scopus 로고    scopus 로고
    • Flexing DNA: HMG-box proteins and their partners
    • M.E. Bianchi, and M. Beltrame Flexing DNA: HMG-box proteins and their partners Am. J. Hum. Genet. 63 1998 1573 1577
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 1573-1577
    • Bianchi, M.E.1    Beltrame, M.2
  • 6
    • 0033982040 scopus 로고    scopus 로고
    • Recognition of distorted DNA structures by HMG domains
    • A. Travers Recognition of distorted DNA structures by HMG domains Curr. Opin. Struct. Biol. 10 2000 102 109
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 102-109
    • Travers, A.1
  • 7
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related "architectural" DNA-binding proteins
    • J.O. Thomas, and A.A. Travers HMG1 and 2, and related "architectural" DNA-binding proteins Trends Biochem. Sci. 26 2001 167 174
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 8
    • 0034741833 scopus 로고    scopus 로고
    • HMG1 and 2: Architectural DNA-binding proteins
    • J.O. Thomas HMG1 and 2: architectural DNA-binding proteins Biochem. Soc. Trans. 29 2001 395 401
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 395-401
    • Thomas, J.O.1
  • 9
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins
    • M. Bustin Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins Mol. Cell. Biol. 19 1999 5237 5246
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5237-5246
    • Bustin, M.1
  • 10
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • T. Bonaldi, G. Langst, R. Strohner, P.B. Becker, and M.E. Bianchi The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding EMBO J. 21 2002 6865 6873
    • (2002) EMBO J. , vol.21 , pp. 6865-6873
    • Bonaldi, T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 11
    • 0037295617 scopus 로고    scopus 로고
    • Priming the nucleosome: A role for HMGB proteins?
    • A.A. Travers Priming the nucleosome: a role for HMGB proteins? EMBO Rep. 4 2003 131 136
    • (2003) EMBO Rep. , vol.4 , pp. 131-136
    • Travers, A.A.1
  • 13
    • 0034682315 scopus 로고    scopus 로고
    • Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
    • A. Taguchi, D.C. Blood, G. del Toro, A. Canet, D.C. Lee, and W. Qu Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases Nature 405 2000 354 360
    • (2000) Nature , vol.405 , pp. 354-360
    • Taguchi, A.1    Blood, D.C.2    Del Toro, G.3    Canet, A.4    Lee, D.C.5    Qu, W.6
  • 14
    • 17144376810 scopus 로고    scopus 로고
    • High-mobility group box 1 protein (HMGB1): Nuclear weapon in the immune arsenal
    • M.T. Lotze, and K.J. Tracey High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal Nature Rev. Immunol. 5 2005 331 342
    • (2005) Nature Rev. Immunol. , vol.5 , pp. 331-342
    • Lotze, M.T.1    Tracey, K.J.2
  • 15
    • 0346669751 scopus 로고    scopus 로고
    • Chromatin-associated HMGA and HMGB proteins: Versatile co-regulators of DNA-dependent processes
    • K.D. Grasser Chromatin-associated HMGA and HMGB proteins: versatile co-regulators of DNA-dependent processes Plant Mol. Biol. 53 2003 281 295
    • (2003) Plant Mol. Biol. , vol.53 , pp. 281-295
    • Grasser, K.D.1
  • 16
    • 0027216519 scopus 로고
    • The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures
    • T.T. Paull, M.J. Haykinson, and R.C. Johnson The nonspecific DNA-binding and -bending proteins HMG1 and HMG2 promote the assembly of complex nucleoprotein structures Genes Dev. 7 1993 1521 1534
    • (1993) Genes Dev. , vol.7 , pp. 1521-1534
    • Paull, T.T.1    Haykinson, M.J.2    Johnson, R.C.3
  • 17
    • 0027359690 scopus 로고
    • High-mobility-group 1 protein mediates DNA bending as determined by ring closures
    • P.M. Pil, C.S. Chow, and S.J. Lippard High-mobility-group 1 protein mediates DNA bending as determined by ring closures Proc. Natl Acad. Sci. USA 90 1993 9465 9469
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9465-9469
    • Pil, P.M.1    Chow, C.S.2    Lippard, S.J.3
  • 18
    • 0028359704 scopus 로고
    • DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain
    • M. Štros, J. Štokrová, and J.O. Thomas DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain Nucl. Acids Res. 22 1994 1044 1051
    • (1994) Nucl. Acids Res. , vol.22 , pp. 1044-1051
    • Štros, M.1    Štokrová, J.2    Thomas, J.O.3
  • 19
    • 0028999513 scopus 로고
    • Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY
    • S.H. Teo, K.D. Grasser, and J.O. Thomas Differences in the DNA-binding properties of the HMG-box domains of HMG1 and the sex-determining factor SRY Eur. J. Biochem. 230 1995 943 950
    • (1995) Eur. J. Biochem. , vol.230 , pp. 943-950
    • Teo, S.H.1    Grasser, K.D.2    Thomas, J.O.3
  • 20
    • 0032562599 scopus 로고    scopus 로고
    • DNA bending by the chromosomal protein HMG1 and its high mobility group box domains. Effect of flanking sequences
    • M. Štros DNA bending by the chromosomal protein HMG1 and its high mobility group box domains. Effect of flanking sequences J. Biol. Chem. 273 1998 10355 10361
    • (1998) J. Biol. Chem. , vol.273 , pp. 10355-10361
    • Štros, M.1
  • 21
    • 0024401923 scopus 로고
    • High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA
    • L.G. Sheflin, and S.W. Spaulding High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA Biochemistry 28 1989 5658 5664
    • (1989) Biochemistry , vol.28 , pp. 5658-5664
    • Sheflin, L.G.1    Spaulding, S.W.2
  • 22
    • 0027156630 scopus 로고
    • The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes
    • L.G. Sheflin, N.W. Fucile, and S.W. Spaulding The specific interactions of HMG 1 and 2 with negatively supercoiled DNA are modulated by their acidic C-terminal domains and involve cysteine residues in their HMG 1/2 boxes Biochemistry 32 1993 3238 3248
    • (1993) Biochemistry , vol.32 , pp. 3238-3248
    • Sheflin, L.G.1    Fucile, N.W.2    Spaulding, S.W.3
  • 23
    • 0001779683 scopus 로고    scopus 로고
    • DNA loops and semicatenated DNA junctions
    • C. Gaillard, and F. Strauss DNA loops and semicatenated DNA junctions BMC Biochem. 1 2000 1
    • (2000) BMC Biochem. , vol.1 , pp. 1
    • Gaillard, C.1    Strauss, F.2
  • 24
    • 2542459486 scopus 로고    scopus 로고
    • High affinity binding of proteins HMG1 and HMG2 to semicatenated DNA loops
    • C. Gaillard, and F. Strauss High affinity binding of proteins HMG1 and HMG2 to semicatenated DNA loops BMC Mol. Biol. 1 2000 1
    • (2000) BMC Mol. Biol. , vol.1 , pp. 1
    • Gaillard, C.1    Strauss, F.2
  • 27
    • 2642553083 scopus 로고    scopus 로고
    • High-affinity binding of tumor-suppressor protein p53 and HMGB1 to hemicatenated DNA loops
    • M. Štros, E. Muselíková-Polanská, Š. Pospíšilová, and F. Strauss High-affinity binding of tumor-suppressor protein p53 and HMGB1 to hemicatenated DNA loops Biochemistry 43 2004 7215 7225
    • (2004) Biochemistry , vol.43 , pp. 7215-7225
    • Štros, M.1    Muselíková-Polanská, E.2    Pospíšilová, Š.3    Strauss, F.4
  • 28
    • 0032524286 scopus 로고    scopus 로고
    • The role of negative superhelicity and length of homology in the formation of paranemic joints promoted by RecA protein
    • B.C. Wong, S.K. Chiu, and S.A. Chow The role of negative superhelicity and length of homology in the formation of paranemic joints promoted by RecA protein J. Biol. Chem. 273 1998 12120 12127
    • (1998) J. Biol. Chem. , vol.273 , pp. 12120-12127
    • Wong, B.C.1    Chiu, S.K.2    Chow, S.A.3
  • 29
    • 0034727674 scopus 로고    scopus 로고
    • Intercalating residues determine the mode of HMG1 domains a and B binding to cisplatin-modified DNA
    • Q. He, U.M. Ohndorf, and S.J. Lippard Intercalating residues determine the mode of HMG1 domains A and B binding to cisplatin-modified DNA Biochemistry 39 2000 14426 14435
    • (2000) Biochemistry , vol.39 , pp. 14426-14435
    • He, Q.1    Ohndorf, U.M.2    Lippard, S.J.3
  • 30
    • 0034680871 scopus 로고    scopus 로고
    • A role of basic residues and the putative intercalating phenylalanine of the HMG-1 box B in DNA supercoiling and binding to four-way DNA junctions
    • M. Štros, and E. Muselíková A role of basic residues and the putative intercalating phenylalanine of the HMG-1 box B in DNA supercoiling and binding to four-way DNA junctions J. Biol. Chem. 275 2000 35699 35707
    • (2000) J. Biol. Chem. , vol.275 , pp. 35699-35707
    • Štros, M.1    Muselíková, E.2
  • 31
    • 0032548929 scopus 로고    scopus 로고
    • Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine
    • Y.M. Yen, B. Wong, and R.C. Johnson Determinants of DNA binding and bending by the Saccharomyces cerevisiae high mobility group protein NHP6A that are important for its biological activities. Role of the unique N terminus and putative intercalating methionine J. Biol. Chem. 273 1998 4424 4435
    • (1998) J. Biol. Chem. , vol.273 , pp. 4424-4435
    • Yen, Y.M.1    Wong, B.2    Johnson, R.C.3
  • 34
    • 1342324028 scopus 로고    scopus 로고
    • IHF and HU: Flexible architects of bent DNA
    • K.K. Swinger, and P.A. Rice IHF and HU: flexible architects of bent DNA Curr. Opin. Struct. Biol. 14 2004 28 35
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 28-35
    • Swinger, K.K.1    Rice, P.A.2
  • 35
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • M.E. Bianchi, M. Beltrame, and G. Paonessa Specific recognition of cruciform DNA by nuclear protein HMG1 Science 243 1989 1056 1059
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 36
    • 0041092343 scopus 로고    scopus 로고
    • HMG box proteins bind to four-way DNA junctions in their open conformation
    • J.R. Pöhler, D.G. Norman, J. Bramham, M.E. Bianchi, and D.M. Lilley HMG box proteins bind to four-way DNA junctions in their open conformation EMBO J. 17 1998 817 826
    • (1998) EMBO J. , vol.17 , pp. 817-826
    • Pöhler, J.R.1    Norman, D.G.2    Bramham, J.3    Bianchi, M.E.4    Lilley, D.M.5
  • 37
    • 0035946944 scopus 로고    scopus 로고
    • Structural requirements for cooperative binding of HMG1 to DNA minicircles
    • M. Webb, D. Payet, K.B. Lee, A.A. Travers, and J.O. Thomas Structural requirements for cooperative binding of HMG1 to DNA minicircles J. Mol. Biol. 309 2001 79 88
    • (2001) J. Mol. Biol. , vol.309 , pp. 79-88
    • Webb, M.1    Payet, D.2    Lee, K.B.3    Travers, A.A.4    Thomas, J.O.5
  • 38
    • 0036170213 scopus 로고    scopus 로고
    • Distorted DNA structures induced by HMGB2 possess a high affinity for HMGB2
    • Y. Nakamura, M. Shimizu, and M. Yoshida Distorted DNA structures induced by HMGB2 possess a high affinity for HMGB2 J. Biochem. (Tokyo) 131 2002 153 160
    • (2002) J. Biochem. (Tokyo) , vol.131 , pp. 153-160
    • Nakamura, Y.1    Shimizu, M.2    Yoshida, M.3
  • 39
    • 0020584610 scopus 로고
    • Facile transition of poly[d(TG)xd(CA)] into a left-handed helix in physiological conditions
    • D.B. Haniford, and D.E. Pulleyblank Facile transition of poly[d(TG)xd(CA)] into a left-handed helix in physiological conditions Nature 302 1983 632 634
    • (1983) Nature , vol.302 , pp. 632-634
    • Haniford, D.B.1    Pulleyblank, D.E.2
  • 40
    • 0345552286 scopus 로고
    • The sequence (dC-dA)n X (dG-dT)n forms left-handed Z-DNA in negatively supercoiled plasmids
    • A. Nordheim, and A. Rich The sequence (dC-dA)n X (dG-dT)n forms left-handed Z-DNA in negatively supercoiled plasmids Proc. Natl Acad. Sci. USA 80 1983 1821 1825
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 1821-1825
    • Nordheim, A.1    Rich, A.2
  • 42
    • 0025331602 scopus 로고
    • High mobility group proteins 1 and 2 bind preferentially to brominated poly(dG-dC).poly(dG-dC) in the Z-DNA conformation but not to other types of Z-DNA
    • T. Christen, M. Bischoff, R. Hobi, and C.C. Kuenzle High mobility group proteins 1 and 2 bind preferentially to brominated poly(dG-dC).poly(dG-dC) in the Z-DNA conformation but not to other types of Z-DNA FEBS Letters 267 1990 139 141
    • (1990) FEBS Letters , vol.267 , pp. 139-141
    • Christen, T.1    Bischoff, M.2    Hobi, R.3    Kuenzle, C.C.4
  • 43
    • 0022423921 scopus 로고
    • Hierarchy of binding sites for chromosomal proteins HMG 1 and 2 in supercoiled deoxyribonucleic acid
    • H. Hamada, and M. Bustin Hierarchy of binding sites for chromosomal proteins HMG 1 and 2 in supercoiled deoxyribonucleic acid Biochemistry 24 1985 1428 1433
    • (1985) Biochemistry , vol.24 , pp. 1428-1433
    • Hamada, H.1    Bustin, M.2
  • 44
    • 0025001734 scopus 로고
    • Z-DNA-binding proteins. Identification critically depends on the proper choice of ligands
    • K.J. Rohner, R. Hobi, and C.C. Kuenzle Z-DNA-binding proteins. Identification critically depends on the proper choice of ligands J. Biol. Chem. 265 1990 19112 19115
    • (1990) J. Biol. Chem. , vol.265 , pp. 19112-19115
    • Rohner, K.J.1    Hobi, R.2    Kuenzle, C.C.3
  • 45
    • 0029954441 scopus 로고    scopus 로고
    • Preferential binding of the archaebacterial histone-like MC1 protein to negatively supercoiled DNA minicircles
    • C. Teyssier, F. Toulme, J.P. Touzel, A. Gervais, J.C. Maurizot, and F. Culard Preferential binding of the archaebacterial histone-like MC1 protein to negatively supercoiled DNA minicircles Biochemistry 35 1996 7954 7958
    • (1996) Biochemistry , vol.35 , pp. 7954-7958
    • Teyssier, C.1    Toulme, F.2    Touzel, J.P.3    Gervais, A.4    Maurizot, J.C.5    Culard, F.6
  • 46
    • 0033982040 scopus 로고    scopus 로고
    • Recognition of distorted DNA structures by HMG domains
    • A. Travers Recognition of distorted DNA structures by HMG domains Curr. Opin. Struct. Biol. 10 2000 102 109
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 102-109
    • Travers, A.1
  • 47
    • 0033485515 scopus 로고    scopus 로고
    • The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition
    • F.V.t. Murphy, R.M. Sweet, and M.E. Churchill The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition EMBO J. 18 1999 6610 6618
    • (1999) EMBO J. , vol.18 , Issue.23 , pp. 6610-6618
    • Murphy, F.V.1    Sweet, R.M.2    Churchill, M.E.3
  • 48
    • 0037088757 scopus 로고    scopus 로고
    • Construction and electrophoretic migration of single-stranded DNA knots and catenanes
    • A. Bucka, and A. Stasiak Construction and electrophoretic migration of single-stranded DNA knots and catenanes Nucl. Acids Res. 30 2002 e24
    • (2002) Nucl. Acids Res. , vol.30 , pp. 24
    • Bucka, A.1    Stasiak, A.2
  • 49
    • 0028918977 scopus 로고
    • A single HMG domain in high-mobility group 1 protein binds to DNAs as small as 20 base pairs containing the major cisplatin adduct
    • C.S. Chow, C.M. Barnes, and S.J. Lippard A single HMG domain in high-mobility group 1 protein binds to DNAs as small as 20 base pairs containing the major cisplatin adduct Biochemistry 34 1995 2956 2964
    • (1995) Biochemistry , vol.34 , pp. 2956-2964
    • Chow, C.S.1    Barnes, C.M.2    Lippard, S.J.3
  • 50
    • 0033607614 scopus 로고    scopus 로고
    • Structure-specific binding of the two tandem HMG boxes of HMG1 to four-way junction DNA is mediated by the a domain
    • M. Webb, and J.O. Thomas Structure-specific binding of the two tandem HMG boxes of HMG1 to four-way junction DNA is mediated by the A domain J. Mol. Biol. 294 1999 373 387
    • (1999) J. Mol. Biol. , vol.294 , pp. 373-387
    • Webb, M.1    Thomas, J.O.2
  • 51
    • 0032518462 scopus 로고    scopus 로고
    • Formation of large nucleoprotein complexes upon binding of the high-mobility group (HMG) box B-domain of HMG1 protein to supercoiled DNA
    • M. Štros, and J. Reich Formation of large nucleoprotein complexes upon binding of the high-mobility group (HMG) box B-domain of HMG1 protein to supercoiled DNA Eur. J. Biochem. 251 1998 427 434
    • (1998) Eur. J. Biochem. , vol.251 , pp. 427-434
    • Štros, M.1    Reich, J.2
  • 52
    • 0029117147 scopus 로고
    • Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA
    • S.H. Teo, K.D. Grasser, C.H. Hardman, R.W. Broadhurst, E.D. Laue, and J.O. Thomas Two mutations in the HMG-box with very different structural consequences provide insights into the nature of binding to four-way junction DNA EMBO J. 14 1995 3844 3853
    • (1995) EMBO J. , vol.14 , pp. 3844-3853
    • Teo, S.H.1    Grasser, K.D.2    Hardman, C.H.3    Broadhurst, R.W.4    Laue, E.D.5    Thomas, J.O.6
  • 54
    • 0035901480 scopus 로고    scopus 로고
    • Two mutations of basic residues within the N-terminus of HMG-1 B domain with different effects on DNA supercoiling and binding to bent DNA
    • M. Štros Two mutations of basic residues within the N-terminus of HMG-1 B domain with different effects on DNA supercoiling and binding to bent DNA Biochemistry 40 2001 4769 4779
    • (2001) Biochemistry , vol.40 , pp. 4769-4779
    • Štros, M.1
  • 55
    • 0019435940 scopus 로고
    • Homologous pairing and topological linkage of DNA molecules by combined action of E. coli RecA protein and topoisomerase I
    • R.P. Cunningham, A.M. Wu, T. Shibata, C. DasGupta, and C.M. Radding Homologous pairing and topological linkage of DNA molecules by combined action of E. coli RecA protein and topoisomerase I Cell 24 1981 213 223
    • (1981) Cell , vol.24 , pp. 213-223
    • Cunningham, R.P.1    Wu, A.M.2    Shibata, T.3    Dasgupta, C.4    Radding, C.M.5
  • 56
    • 0020841303 scopus 로고
    • Synapsis and the formation of paranemic joints by E. coli RecA protein
    • M. Bianchi, C. DasGupta, and C.M. Radding Synapsis and the formation of paranemic joints by E. coli RecA protein Cell 34 1983 931 939
    • (1983) Cell , vol.34 , pp. 931-939
    • Bianchi, M.1    Dasgupta, C.2    Radding, C.M.3
  • 57
    • 0023058297 scopus 로고
    • Homologous pairing of DNA molecules by Ustilago rec1 protein is promoted by sequences of Z-DNA
    • E.B. Kmiec, and W.K. Holloman Homologous pairing of DNA molecules by Ustilago rec1 protein is promoted by sequences of Z-DNA Cell 44 1986 545 554
    • (1986) Cell , vol.44 , pp. 545-554
    • Kmiec, E.B.1    Holloman, W.K.2
  • 58
    • 0024990434 scopus 로고
    • Triple-helical DNA pairing intermediates formed by recA protein
    • S.W. Umlauf, M.M. Cox, and R.B. Inman Triple-helical DNA pairing intermediates formed by recA protein J. Biol. Chem. 265 1990 16898 16912
    • (1990) J. Biol. Chem. , vol.265 , pp. 16898-16912
    • Umlauf, S.W.1    Cox, M.M.2    Inman, R.B.3
  • 59
    • 0026761011 scopus 로고
    • Evidence that intergenic spacer repeats of Drosophila melanogaster rRNA genes function as X-Y pairing sites in male meiosis, and a general model for achiasmatic pairing
    • B.D. McKee, L. Habera, and J.A. Vrana Evidence that intergenic spacer repeats of Drosophila melanogaster rRNA genes function as X-Y pairing sites in male meiosis, and a general model for achiasmatic pairing Genetics 132 1992 529 544
    • (1992) Genetics , vol.132 , pp. 529-544
    • McKee, B.D.1    Habera, L.2    Vrana, J.A.3
  • 60
    • 17344376854 scopus 로고    scopus 로고
    • Patterns of variation in the intergenic spacers of ribosomal DNA in Drosophila melanogaster support a model for genetic exchanges during X-Y pairing
    • C. Polanco, A.I. Gonzalez, and G.A. Dover Patterns of variation in the intergenic spacers of ribosomal DNA in Drosophila melanogaster support a model for genetic exchanges during X-Y pairing Genetics 155 2000 1221 1229
    • (2000) Genetics , vol.155 , pp. 1221-1229
    • Polanco, C.1    Gonzalez, A.I.2    Dover, G.A.3
  • 61
    • 0022457421 scopus 로고
    • Structure of replicating simian virus 40 minichromosomes. the replication fork, core histone segregation and terminal structures
    • J.M. Sogo, H. Stahl, T. Koller, and R. Knippers Structure of replicating simian virus 40 minichromosomes. The replication fork, core histone segregation and terminal structures J. Mol. Biol. 189 1986 189 204
    • (1986) J. Mol. Biol. , vol.189 , pp. 189-204
    • Sogo, J.M.1    Stahl, H.2    Koller, T.3    Knippers, R.4
  • 62
    • 0031835961 scopus 로고    scopus 로고
    • Geometry and physics of catenanes applied to the study of DNA replication
    • B. Laurie, V. Katritch, J. Sogo, T. Koller, J. Dubochet, and A. Stasiak Geometry and physics of catenanes applied to the study of DNA replication Biophys. J. 74 1998 2815 2822
    • (1998) Biophys. J. , vol.74 , pp. 2815-2822
    • Laurie, B.1    Katritch, V.2    Sogo, J.3    Koller, T.4    Dubochet, J.5    Stasiak, A.6
  • 63
    • 0034656994 scopus 로고    scopus 로고
    • Hemicatenanes form upon inhibition of DNA replication
    • I. Lucas, and O. Hyrien Hemicatenanes form upon inhibition of DNA replication Nucl. Acids Res. 28 2000 2187 2193
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2187-2193
    • Lucas, I.1    Hyrien, O.2
  • 64
    • 0042692792 scopus 로고    scopus 로고
    • Rad52-independent accumulation of joint circular minichromosomes during S phase in Saccharomyces cerevisiae
    • R.E. Wellinger, P. Schar, and J.M. Sogo Rad52-independent accumulation of joint circular minichromosomes during S phase in Saccharomyces cerevisiae Mol. Cell. Biol. 23 2003 6363 6372
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6363-6372
    • Wellinger, R.E.1    Schar, P.2    Sogo, J.M.3
  • 65
    • 0347416973 scopus 로고    scopus 로고
    • Branch migrating sister chromatid junctions form at replication origins through Rad51/Rad52-independent mechanisms
    • M. Lopes, C. Cotta-Ramusino, G. Liberi, and M. Foiani Branch migrating sister chromatid junctions form at replication origins through Rad51/Rad52-independent mechanisms Mol. Cell 12 2003 1499 1510
    • (2003) Mol. Cell , vol.12 , pp. 1499-1510
    • Lopes, M.1    Cotta-Ramusino, C.2    Liberi, G.3    Foiani, M.4
  • 66
    • 0028972024 scopus 로고
    • Identification of double Holliday junctions as intermediates in meiotic recombination
    • A. Schwacha, and N. Kleckner Identification of double Holliday junctions as intermediates in meiotic recombination Cell 83 1995 783 791
    • (1995) Cell , vol.83 , pp. 783-791
    • Schwacha, A.1    Kleckner, N.2
  • 67
    • 0035195043 scopus 로고    scopus 로고
    • Prominent mitochondrial DNA recombination intermediates in human heart muscle
    • O.A. Kajander, P.J. Karhunen, I.J. Holt, and H.T. Jacobs Prominent mitochondrial DNA recombination intermediates in human heart muscle EMBO Rep. 2 2001 1007 1012
    • (2001) EMBO Rep. , vol.2 , pp. 1007-1012
    • Kajander, O.A.1    Karhunen, P.J.2    Holt, I.J.3    Jacobs, H.T.4
  • 68
    • 0035947237 scopus 로고    scopus 로고
    • DNA replication-dependent formation of joint DNA molecules in Physarum polycephalum
    • M. Benard, C. Maric, and G. Pierron DNA replication-dependent formation of joint DNA molecules in Physarum polycephalum Mol. Cell 7 2001 971 980
    • (2001) Mol. Cell , vol.7 , pp. 971-980
    • Benard, M.1    Maric, C.2    Pierron, G.3
  • 69
    • 0036809071 scopus 로고    scopus 로고
    • Increased recombination intermediates and homologous integration hot spots at DNA replication origins
    • M. Segurado, M. Gomez, and F. Antequera Increased recombination intermediates and homologous integration hot spots at DNA replication origins Mol. Cell 10 2002 907 916
    • (2002) Mol. Cell , vol.10 , pp. 907-916
    • Segurado, M.1    Gomez, M.2    Antequera, F.3
  • 71
    • 0017195605 scopus 로고
    • The number of superhelical turns in native virion SV40 DNA and minicol DNA determined by the band counting method
    • M. Shure, and J. Vinograd The number of superhelical turns in native virion SV40 DNA and minicol DNA determined by the band counting method Cell 8 1976 215 226
    • (1976) Cell , vol.8 , pp. 215-226
    • Shure, M.1    Vinograd, J.2
  • 72
    • 0017385956 scopus 로고
    • The problems of eukaryotic and prokaryotic DNA packaging and in vivo conformation posed by superhelix density heterogeneity
    • M. Shure, D.E. Pulleyblank, and J. Vinograd The problems of eukaryotic and prokaryotic DNA packaging and in vivo conformation posed by superhelix density heterogeneity Nucl. Acids Res. 4 1977 1183 1205
    • (1977) Nucl. Acids Res. , vol.4 , pp. 1183-1205
    • Shure, M.1    Pulleyblank, D.E.2    Vinograd, J.3
  • 73
    • 0025176779 scopus 로고
    • Ethanol precipitation of DNA with linear polyacrylamide as carrier
    • C. Gaillard, and F. Strauss Ethanol precipitation of DNA with linear polyacrylamide as carrier Nucl. Acids Res. 18 1990 378
    • (1990) Nucl. Acids Res. , vol.18 , pp. 378
    • Gaillard, C.1    Strauss, F.2
  • 74
    • 0034434469 scopus 로고    scopus 로고
    • Eliminating DNA losses and denaturation upon storage in plastic microtubes
    • C. Gaillard, and F. Strauss Eliminating DNA losses and denaturation upon storage in plastic microtubes Int. Biotechnol. Lab. 18 2000 24
    • (2000) Int. Biotechnol. Lab. , vol.18 , pp. 24
    • Gaillard, C.1    Strauss, F.2
  • 76
    • 0028278444 scopus 로고
    • Association of poly(CA).poly(TG) DNA fragments into four-stranded complexes bound by HMG1 and 2
    • C. Gaillard, and F. Strauss Association of poly(CA).poly(TG) DNA fragments into four-stranded complexes bound by HMG1 and 2 Science 264 1994 433 436
    • (1994) Science , vol.264 , pp. 433-436
    • Gaillard, C.1    Strauss, F.2


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