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Volumn 24, Issue 19, 2004, Pages 8727-8744

Synapsis of recombination signal sequences located in cis and DNA underwinding in V(D)J recombination

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; DOUBLE STRANDED DNA; HIGH MOBILITY GROUP B1 PROTEIN; HIGH MOBILITY GROUP B2 PROTEIN; RAG1 PROTEIN; RAG2 PROTEIN; RECOMBINANT DNA; SIGNAL PEPTIDE;

EID: 4544302863     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.24.19.8727-8744.2004     Document Type: Article
Times cited : (15)

References (63)
  • 1
    • 0032823310 scopus 로고    scopus 로고
    • The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2
    • Aidinis, V., T. Bonaldi, M. Beltrame, S. Santagata, M. E. Bianchi, and E. Spanopoulou. 1999. The RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2. Mol. Cell. Biol. 19:6532-6542.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6532-6542
    • Aidinis, V.1    Bonaldi, T.2    Beltrame, M.3    Santagata, S.4    Bianchi, M.E.5    Spanopoulou, E.6
  • 2
    • 0031826699 scopus 로고    scopus 로고
    • Distinct roles of RAG1 and RAG2 in binding the V(D)J recombination signal sequences
    • Akamatsu, Y., and M. A. Oettinger. 1998. Distinct roles of RAG1 and RAG2 in binding the V(D)J recombination signal sequences. Mol. Cell. Biol. 18: 4670-4678.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4670-4678
    • Akamatsu, Y.1    Oettinger, M.A.2
  • 3
    • 0141753136 scopus 로고    scopus 로고
    • Regulation of V(D)J recombination by nucleosome positioning at recombination signal sequences
    • Baumann, M., A. Mamais, F. McBlane, H. Xiao, and J. Boyes. 2003. Regulation of V(D)J recombination by nucleosome positioning at recombination signal sequences. EMBO J. 22:5197-5207.
    • (2003) EMBO J. , vol.22 , pp. 5197-5207
    • Baumann, M.1    Mamais, A.2    McBlane, F.3    Xiao, H.4    Boyes, J.5
  • 4
    • 0026609275 scopus 로고
    • The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins
    • Bianchi, M. E., L. Falciola, S. Ferrari, and D. M. Lilley. 1992. The DNA binding site of HMG1 protein is composed of two similar segments (HMG boxes), both of which have counterparts in other eukaryotic regulatory proteins. EMBO J. 11:1055-1063.
    • (1992) EMBO J. , vol.11 , pp. 1055-1063
    • Bianchi, M.E.1    Falciola, L.2    Ferrari, S.3    Lilley, D.M.4
  • 5
    • 0032577448 scopus 로고    scopus 로고
    • IHF modulation of Tn10 transposition: Sensory transduction of supercoiling status via a proposed protein/DNA molecular spring
    • Chalmers, R., A. Guhathakurta, H. Benjamin, and N. Kleckner. 1998. IHF modulation of Tn10 transposition: sensory transduction of supercoiling status via a proposed protein/DNA molecular spring. Cell 93:897-908.
    • (1998) Cell , vol.93 , pp. 897-908
    • Chalmers, R.1    Guhathakurta, A.2    Benjamin, H.3    Kleckner, N.4
  • 6
    • 0028950413 scopus 로고
    • HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG
    • Churchill, M. E., D. N. Jones, T. Glaser, H. Hefner, M. A. Searles, and A. A. Travers. 1995. HMG-D is an architecture-specific protein that preferentially binds to DNA containing the dinucleotide TG. EMBO J. 14:1264-1275.
    • (1995) EMBO J. , vol.14 , pp. 1264-1275
    • Churchill, M.E.1    Jones, D.N.2    Glaser, T.3    Hefner, H.4    Searles, M.A.5    Travers, A.A.6
  • 7
    • 0037458557 scopus 로고    scopus 로고
    • RAG1-DNA binding in V(D)J recombination. Specificity and DNA-induced conformational changes revealed by fluorescence and CD spectroscopy
    • Ciubotaru, M., L. M. Ptaszek, G. A. Baker, S. N. Baker, F. V. Bright, and D. G. Schatz. 2003. RAG1-DNA binding in V(D)J recombination. Specificity and DNA-induced conformational changes revealed by fluorescence and CD spectroscopy. J. Biol. Chem. 278:5584-5596.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5584-5596
    • Ciubotaru, M.1    Ptaszek, L.M.2    Baker, G.A.3    Baker, S.N.4    Bright, F.V.5    Schatz, D.G.6
  • 8
    • 1542345458 scopus 로고    scopus 로고
    • DNA looping and catalysis: The IHF-folded arm of Tn10 promotes conformational changes and hairpin resolution
    • Crellin, P., S. Sewitz, and R. Chalmers. 2004. DNA looping and catalysis: the IHF-folded arm of Tn10 promotes conformational changes and hairpin resolution. Mol. Cell 13:537-547.
    • (2004) Mol. Cell , vol.13 , pp. 537-547
    • Crellin, P.1    Sewitz, S.2    Chalmers, R.3
  • 9
    • 0029814965 scopus 로고    scopus 로고
    • DNA sequence and structure requirements for cleavage of V(D)J recombination signal sequences
    • Cuomo, C. A., C. L. Mundy, and M. A. Oettinger. 1996. DNA sequence and structure requirements for cleavage of V(D)J recombination signal sequences. Mol. Cell. Biol. 16:5683-5690.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5683-5690
    • Cuomo, C.A.1    Mundy, C.L.2    Oettinger, M.A.3
  • 10
    • 0001265782 scopus 로고    scopus 로고
    • RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination
    • Difilippantonio, M. J., C. J. McMahan, Q. M. Eastman, E. Spanopoulou, and D. G. Schatz. 1996. RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination. Cell 87:253-262.
    • (1996) Cell , vol.87 , pp. 253-262
    • Difilippantonio, M.J.1    McMahan, C.J.2    Eastman, Q.M.3    Spanopoulou, E.4    Schatz, D.G.5
  • 11
    • 0029864993 scopus 로고    scopus 로고
    • Initiation of V(D)J recombination in vitro obeying the 12/23 rule
    • Eastman, Q. M., T. M. Leu, and D. G. Schatz. 1996. Initiation of V(D)J recombination in vitro obeying the 12/23 rule. Nature 380:85-88.
    • (1996) Nature , vol.380 , pp. 85-88
    • Eastman, Q.M.1    Leu, T.M.2    Schatz, D.G.3
  • 12
    • 0032939926 scopus 로고    scopus 로고
    • Detection of RAG protein-V(D)J recombination signal interactions near the site of DNA cleavage by UV cross-linking
    • Eastman, Q. M., I. J. Villey, and D. G. Schatz. 1999. Detection of RAG protein-V(D)J recombination signal interactions near the site of DNA cleavage by UV cross-linking. Mol. Cell. Biol. 19:3788-3797.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3788-3797
    • Eastman, Q.M.1    Villey, I.J.2    Schatz, D.G.3
  • 13
    • 0028355759 scopus 로고
    • Mutational analysis of the DNA binding domain A of chromosomal protein HMG1
    • Falciola, L., A. I. Murchie, D. M. Lilley, and M. Bianchi. 1994. Mutational analysis of the DNA binding domain A of chromosomal protein HMG1. Nucleic Acids Res. 22:285-292.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 285-292
    • Falciola, L.1    Murchie, A.I.2    Lilley, D.M.3    Bianchi, M.4
  • 15
    • 0033954892 scopus 로고    scopus 로고
    • Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex
    • Fugmann, S. D., I. J. Villey, L. M. Ptaszek, and D. G. Schatz. 2000. Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex. Mol. Cell 5:97-107.
    • (2000) Mol. Cell , vol.5 , pp. 97-107
    • Fugmann, S.D.1    Villey, I.J.2    Ptaszek, L.M.3    Schatz, D.G.4
  • 16
    • 0035997348 scopus 로고    scopus 로고
    • V(D)J recombination: RAG proteins, repair factors, and regulation
    • Gellert, M. 2002. V(D)J recombination: RAG proteins, repair factors, and regulation. Annu. Rev. Biochem. 71:101-132.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 101-132
    • Gellert, M.1
  • 18
    • 0033168204 scopus 로고    scopus 로고
    • Nucleosome structure completely inhibits in vitro cleavage by the V(D)J recombinase
    • Golding, A., S. Chandler, E. Ballestar, A. P. Wolffe, and M. S. Schlissel. 1999. Nucleosome structure completely inhibits in vitro cleavage by the V(D)J recombinase. EMBO J. 18:3712-3723.
    • (1999) EMBO J. , vol.18 , pp. 3712-3723
    • Golding, A.1    Chandler, S.2    Ballestar, E.3    Wolffe, A.P.4    Schlissel, M.S.5
  • 19
    • 0030795764 scopus 로고    scopus 로고
    • A complex of RAG-1 and RAG-2 proteins persists on DNA after single-strand cleavage at V(D)J recombination signal sequences
    • Grawunder, U., and M. R. Lieber. 1997. A complex of RAG-1 and RAG-2 proteins persists on DNA after single-strand cleavage at V(D)J recombination signal sequences. Nucleic Acids Res. 25:1375-1382.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1375-1382
    • Grawunder, U.1    Lieber, M.R.2
  • 20
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., K. Giese, and J. Pagel. 1994. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10:94-100.
    • (1994) Trends Genet. , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 21
    • 0034727674 scopus 로고    scopus 로고
    • Intercalating residues determine the mode of HMG1 domains A and B binding to cisplatin-modified DNA
    • He, Q., U. M. Ohndorf, and S. J. Lippard. 2000. Intercalating residues determine the mode of HMG1 domains A and B binding to cisplatin-modified DNA. Biochemistry 39:14426-14435.
    • (2000) Biochemistry , vol.39 , pp. 14426-14435
    • He, Q.1    Ohndorf, U.M.2    Lippard, S.J.3
  • 22
    • 0032084698 scopus 로고    scopus 로고
    • Assembly of a 12/23 paired signal complex: A critical control point in V(D)J recombination
    • Hiom, K., and M. Gellert. 1998. Assembly of a 12/23 paired signal complex: a critical control point in V(D)J recombination. Mol. Cell 1:1011-1019.
    • (1998) Mol. Cell , vol.1 , pp. 1011-1019
    • Hiom, K.1    Gellert, M.2
  • 23
    • 0017903484 scopus 로고
    • Nonhistone proteins HMG1 and HMG2 change the DNA helical structure
    • Javaherian, K., J. F. Liu, and J. C. Wang. 1978. Nonhistone proteins HMG1 and HMG2 change the DNA helical structure. Science 199:1345-1346.
    • (1978) Science , vol.199 , pp. 1345-1346
    • Javaherian, K.1    Liu, J.F.2    Wang, J.C.3
  • 24
    • 0018787029 scopus 로고
    • Nonhistone proteins HMG1 and HMG2 unwind DNA double helix
    • Javaherian, K., M. Sadeghi, and L. F. Liu. 1979. Nonhistone proteins HMG1 and HMG2 unwind DNA double helix. Nucleic Acids Res. 6:3569-3580.
    • (1979) Nucleic Acids Res. , vol.6 , pp. 3569-3580
    • Javaherian, K.1    Sadeghi, M.2    Liu, L.F.3
  • 25
    • 0036682598 scopus 로고    scopus 로고
    • Ordered assembly of the V(D)J synaptic complex ensures accurate recombination
    • Jones, J. M., and M. Gellert. 2002. Ordered assembly of the V(D)J synaptic complex ensures accurate recombination. EMBO J. 21:4162-4171.
    • (2002) EMBO J. , vol.21 , pp. 4162-4171
    • Jones, J.M.1    Gellert, M.2
  • 26
    • 0000675571 scopus 로고    scopus 로고
    • Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase
    • Kim, D. R., Y. Dai, C. L. Mundy, W. Yang, and M. A. Oettinger. 1999. Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase. Genes Dev. 13:3070-3080.
    • (1999) Genes Dev. , vol.13 , pp. 3070-3080
    • Kim, D.R.1    Dai, Y.2    Mundy, C.L.3    Yang, W.4    Oettinger, M.A.5
  • 27
    • 0037592865 scopus 로고    scopus 로고
    • The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity
    • Klass, J., F. V. T. Murphy, S. Fouts, M. Serenil, A. Changela, J. Siple, and M. E. Churchill. 2003. The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity. Nucleic Acids Res. 31:2852-2864.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2852-2864
    • Klass, J.1    Murphy, F.V.T.2    Fouts, S.3    Serenil, M.4    Changela, A.5    Siple, J.6    Churchill, M.E.7
  • 28
    • 0032239155 scopus 로고    scopus 로고
    • Accessibility of nucleosomal DNA to V(D)J cleavage is modulated by RSS positioning and HMG1
    • Kwon, J., A. N. Imbalzano, A. Matthews, and M. A. Oettinger. 1998. Accessibility of nucleosomal DNA to V(D)J cleavage is modulated by RSS positioning and HMG1. Mol. Cell 2:829-839.
    • (1998) Mol. Cell , vol.2 , pp. 829-839
    • Kwon, J.1    Imbalzano, A.N.2    Matthews, A.3    Oettinger, M.A.4
  • 29
    • 0033380368 scopus 로고    scopus 로고
    • Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination
    • Landree, M. A., J. A. Wibbenmeyer, and D. B. Roth. 1999. Mutational analysis of RAG1 and RAG2 identifies three catalytic amino acids in RAG1 critical for both cleavage steps of V(D)J recombination. Genes Dev. 13: 3059-3069.
    • (1999) Genes Dev. , vol.13 , pp. 3059-3069
    • Landree, M.A.1    Wibbenmeyer, J.A.2    Roth, D.B.3
  • 30
    • 0027646025 scopus 로고
    • A signature for the HMG-1 box DNA-binding proteins
    • Landsman, D., and M. Bustin. 1993. A signature for the HMG-1 box DNA-binding proteins. Bioessays 15:539-546.
    • (1993) Bioessays , vol.15 , pp. 539-546
    • Landsman, D.1    Bustin, M.2
  • 31
    • 0023801238 scopus 로고
    • The defect in murine severe combined immune deficiency: Joining of signal sequences but not coding segments in V(D)J recombination
    • Lieber, M. R., J. E. Hesse, S. Lewis, G. C. Bosma, N. Rosenberg, K. Mizuuchi, M. J. Bosma, and M. Gellert. 1988. The defect in murine severe combined immune deficiency: joining of signal sequences but not coding segments in V(D)J recombination. Cell 55:7-16.
    • (1988) Cell , vol.55 , pp. 7-16
    • Lieber, M.R.1    Hesse, J.E.2    Lewis, S.3    Bosma, G.C.4    Rosenberg, N.5    Mizuuchi, K.6    Bosma, M.J.7    Gellert, M.8
  • 32
    • 0034175813 scopus 로고    scopus 로고
    • Stimulation of V(D)J recombination by histone acetylation
    • McBlane, F., and J. Boyes. 2000. Stimulation of V(D)J recombination by histone acetylation. Curr. Biol. 10:483-486.
    • (2000) Curr. Biol. , vol.10 , pp. 483-486
    • McBlane, F.1    Boyes, J.2
  • 33
    • 0026573580 scopus 로고
    • A general and fast method to generate multiple site directed mutations
    • Mikaelian, I., and A. Sergeant. 1992. A general and fast method to generate multiple site directed mutations. Nucleic Acids Res. 20:376.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 376
    • Mikaelian, I.1    Sergeant, A.2
  • 34
    • 0034159929 scopus 로고    scopus 로고
    • A highly ordered structure in V(D)J recombination cleavage complexes is facilitated by HMG1
    • Mo, X., T. Bailin, S. Noggle, and M. J. Sadofsky. 2000. A highly ordered structure in V(D)J recombination cleavage complexes is facilitated by HMG1. Nucleic Acids Res. 28:1228-1236.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1228-1236
    • Mo, X.1    Bailin, T.2    Noggle, S.3    Sadofsky, M.J.4
  • 36
    • 0036788786 scopus 로고    scopus 로고
    • Footprint analysis of recombination signal sequences in the 12/23 synaptic complex of V(D)J recombination
    • Nagawa, F., M. Kodama, T. Nishihara, K. Ishiguro, and H. Sakano. 2002. Footprint analysis of recombination signal sequences in the 12/23 synaptic complex of V(D)J recombination. Mol. Cell. Biol. 22:7217-7225.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7217-7225
    • Nagawa, F.1    Kodama, M.2    Nishihara, T.3    Ishiguro, K.4    Sakano, H.5
  • 37
    • 0038719678 scopus 로고    scopus 로고
    • The central domain of core RAG1 preferentially recognizes single-stranded recombination signal sequence heptamer
    • Peak, M. M., J. L. Arbuckle, and K. K. Rodgers. 2003. The central domain of core RAG1 preferentially recognizes single-stranded recombination signal sequence heptamer. J. Biol. Chem. 278:18235-18240.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18235-18240
    • Peak, M.M.1    Arbuckle, J.L.2    Rodgers, K.K.3
  • 38
    • 0027359690 scopus 로고
    • High-mobility-group 1 protein mediates DNA bending as determined by ring closures
    • Pil, P. M., C. S. Chow, and S. J. Lippard. 1993. High-mobility-group 1 protein mediates DNA bending as determined by ring closures. Proc. Natl. Acad. Sci. USA 90:9465-9469.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9465-9469
    • Pil, P.M.1    Chow, C.S.2    Lippard, S.J.3
  • 39
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin
    • Pil, P. M., and S. J. Lippard. 1992. Specific binding of chromosomal protein HMG1 to DNA damaged by the anticancer drug cisplatin. Science 256:234-237.
    • (1992) Science , vol.256 , pp. 234-237
    • Pil, P.M.1    Lippard, S.J.2
  • 40
    • 0041092343 scopus 로고    scopus 로고
    • HMG box proteins bind to four-way DNA junctions in their open conformation
    • Pohler, J. R. G., D. G. Norman, J. Bramham, M. E. Bianchi, and D. M. Lilley. 1998. HMG box proteins bind to four-way DNA junctions in their open conformation. EMBO J. 17:817-826.
    • (1998) EMBO J. , vol.17 , pp. 817-826
    • Pohler, J.R.G.1    Norman, D.G.2    Bramham, J.3    Bianchi, M.E.4    Lilley, D.M.5
  • 41
    • 0028291092 scopus 로고
    • Conservation of sequence in recombination signal sequence spacers
    • Ramsden, D. A., K. Baetz, and G. E. Wu. 1994. Conservation of sequence in recombination signal sequence spacers. Nucleic Acids Res. 22:1785-1796.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1785-1796
    • Ramsden, D.A.1    Baetz, K.2    Wu, G.E.3
  • 42
    • 0029891597 scopus 로고    scopus 로고
    • Distinct DNA sequence and structure requirements for the two steps of V(D)J recombination signal cleavage
    • Ramsden, D. A., J. F. McBlane, D. C. van Gent, and M. Gellert. 1996. Distinct DNA sequence and structure requirements for the two steps of V(D)J recombination signal cleavage. EMBO J. 15:3197-3206.
    • (1996) EMBO J. , vol.15 , pp. 3197-3206
    • Ramsden, D.A.1    McBlane, J.F.2    Van Gent, D.C.3    Gellert, M.4
  • 43
    • 0033565820 scopus 로고    scopus 로고
    • A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2
    • Rodgers, K. K., I. J. Villey, L. Ptaszek, E. Corbett, D. G. Schatz, and J. E. Coleman. 1999. A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2. Nucleic Acids Res. 27:2938-2946.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2938-2946
    • Rodgers, K.K.1    Villey, I.J.2    Ptaszek, L.3    Corbett, E.4    Schatz, D.G.5    Coleman, J.E.6
  • 46
    • 0030980386 scopus 로고    scopus 로고
    • V(D)J recombination: Modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins
    • Sawchuk, D. J., F. Weis-Garcia, S. Malik, E. Besmer, M. Bustin, M. C. Nussenzweig, and P. Cortes. 1997. V(D)J recombination: modulation of RAG1 and RAG2 cleavage activity on 12/23 substrates by whole cell extract and DNA-bending proteins. J. Exp. Med. 185:2025-2032.
    • (1997) J. Exp. Med. , vol.185 , pp. 2025-2032
    • Sawchuk, D.J.1    Weis-Garcia, F.2    Malik, S.3    Besmer, E.4    Bustin, M.5    Nussenzweig, M.C.6    Cortes, P.7
  • 47
    • 0027410476 scopus 로고
    • V(D)J recombination: Signal and coding joint resolution are uncoupled and depend on parallel synapsis of the sites
    • Sheehan, K. M., and M. R. Lieber. 1993. V(D)J recombination: signal and coding joint resolution are uncoupled and depend on parallel synapsis of the sites. Mol. Cell. Biol. 13:1363-1370.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1363-1370
    • Sheehan, K.M.1    Lieber, M.R.2
  • 48
    • 0024401923 scopus 로고
    • High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA
    • Sheflin, L. G., and S. W. Spaulding. 1989. High mobility group protein 1 preferentially conserves torsion in negatively supercoiled DNA. Biochemistry 28:5658-5664.
    • (1989) Biochemistry , vol.28 , pp. 5658-5664
    • Sheflin, L.G.1    Spaulding, S.W.2
  • 49
    • 0030592523 scopus 로고    scopus 로고
    • The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination
    • Spanopoulou, E., F. Zaitseva, F. H. Wang, S. Santagata, D. Baltimore, and G. Panayotou. 1996. The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination. Cell 87:263-276.
    • (1996) Cell , vol.87 , pp. 263-276
    • Spanopoulou, E.1    Zaitseva, F.2    Wang, F.H.3    Santagata, S.4    Baltimore, D.5    Panayotou, G.6
  • 50
    • 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
    • Stros, M., and E. Muselikova. 2000. 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. 275:35699-35707.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35699-35707
    • Stros, M.1    Muselikova, E.2
  • 51
    • 0036171148 scopus 로고    scopus 로고
    • Fine structure and activity of discrete RAG-HMG complexes on V(D)J recombination signals
    • Swanson, P. C. 2002. Fine structure and activity of discrete RAG-HMG complexes on V(D)J recombination signals. Mol. Cell. Biol. 22:1340-1351.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1340-1351
    • Swanson, P.C.1
  • 52
    • 0036839614 scopus 로고    scopus 로고
    • A RAG-I/RAG-2 tetramer supports 12/23-regulated synapsis, cleavage, and transposition of V(D)J recombination signals
    • Swanson, P. C. 2002. A RAG-I/RAG-2 tetramer supports 12/23-regulated synapsis, cleavage, and transposition of V(D)J recombination signals. Mol. Cell. Biol. 22:7790-7801.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7790-7801
    • Swanson, P.C.1
  • 53
    • 0032908830 scopus 로고    scopus 로고
    • RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex
    • Swanson, P. C., and S. Desiderio. 1999. RAG-2 promotes heptamer occupancy by RAG-1 in the assembly of a V(D)J initiation complex. Mol. Cell. Biol. 19:3674-3683.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3674-3683
    • Swanson, P.C.1    Desiderio, S.2
  • 54
    • 0032126295 scopus 로고    scopus 로고
    • V(D)J recombination signal recognition: Distinct, overlapping DNA-protein contacts in complexes containing RAG1 with and without RAG2
    • Swanson, P. C., and S. Desiderio. 1998. V(D)J recombination signal recognition: distinct, overlapping DNA-protein contacts in complexes containing RAG1 with and without RAG2. Immunity 9:115-125.
    • (1998) Immunity , vol.9 , pp. 115-125
    • Swanson, P.C.1    Desiderio, S.2
  • 55
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • Tonegawa, S. 1983. Somatic generation of antibody diversity. Nature 302: 575-581.
    • (1983) Nature , vol.302 , pp. 575-581
    • Tonegawa, S.1
  • 56
    • 0030009253 scopus 로고    scopus 로고
    • The RAG1 and RAG2 proteins establish the 12/23 rule in V(D)J recombination
    • van Gent, D. C., D. A. Ramsden, and M. Gellert. 1996. The RAG1 and RAG2 proteins establish the 12/23 rule in V(D)J recombination. Cell 85: 107-113.
    • (1996) Cell , vol.85 , pp. 107-113
    • Van Gent, D.C.1    Ramsden, D.A.2    Gellert, M.3
  • 58
    • 0031770944 scopus 로고    scopus 로고
    • The RAG-HMG1 complex enforces the 12/23 rule of V(D)J recombination specifically at the double-hairpin formation step
    • West, R. B., and M. R. Lieber. 1998. The RAG-HMG1 complex enforces the 12/23 rule of V(D)J recombination specifically at the double-hairpin formation step. Mol. Cell. Biol. 18:6408-6415.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6408-6415
    • West, R.B.1    Lieber, M.R.2
  • 59
    • 0033512850 scopus 로고    scopus 로고
    • Mechanistic basis for coding end sequence effects in the initiation of V(D)J recombination
    • Yu, K., and M. R. Lieber. 1999. Mechanistic basis for coding end sequence effects in the initiation of V(D)J recombination. Mol. Cell. Biol. 19:8094-8102.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8094-8102
    • Yu, K.1    Lieber, M.R.2
  • 60
    • 0033782185 scopus 로고    scopus 로고
    • The nicking step in V(D)J recombination is independent of synapsis: Implications for the immune repertoire
    • Yu, K., and M. R. Lieber. 2000. The nicking step in V(D)J recombination is independent of synapsis: implications for the immune repertoire. Mol. Cell. Biol. 20:7914-7921.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7914-7921
    • Yu, K.1    Lieber, M.R.2
  • 61
    • 0348140583 scopus 로고    scopus 로고
    • Kinetic analysis of the nicking and hairpin formation steps in V(D)J recombination
    • Yu, K., A. Taghva, Y. Ma, and M. R. Lieber. 2004. Kinetic analysis of the nicking and hairpin formation steps in V(D)J recombination. DNA Repair 3:67-75.
    • (2004) DNA Repair , vol.3 , pp. 67-75
    • Yu, K.1    Taghva, A.2    Ma, Y.3    Lieber, M.R.4
  • 62
    • 0034892672 scopus 로고    scopus 로고
    • Simultaneous measurement of binding constants and unwinding angles by gel electrophoresis
    • Zeman, S. M., and D. M. Crothers. 2001. Simultaneous measurement of binding constants and unwinding angles by gel electrophoresis. Methods Enzymol. 340:51-68.
    • (2001) Methods Enzymol. , vol.340 , pp. 51-68
    • Zeman, S.M.1    Crothers, D.M.2
  • 63
    • 0032516019 scopus 로고    scopus 로고
    • Simultaneous determination of helical unwinding angles and intrinsic association constants in ligand-DNA complexes: The interaction between DNA and calichearubicin B
    • Zeman, S. M., K. M. Depew, S. J. Danishefsky, and D. M. Crothers. 1998. Simultaneous determination of helical unwinding angles and intrinsic association constants in ligand-DNA complexes: the interaction between DNA and calichearubicin B. Proc. Natl. Acad. Sci. USA 95:4327-4332.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4327-4332
    • Zeman, S.M.1    Depew, K.M.2    Danishefsky, S.J.3    Crothers, D.M.4


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