메뉴 건너뛰기




Volumn 21, Issue 6, 2001, Pages 2038-2047

A C-terminal region of RAG1 contacts the coding DNA during V(D)J recombination

Author keywords

[No Author keywords available]

Indexed keywords

RAG1 PROTEIN; RAG2 PROTEIN; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN;

EID: 0035018257     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.6.2038-2047.2001     Document Type: Article
Times cited : (36)

References (49)
  • 1
    • 0033934684 scopus 로고    scopus 로고
    • Postcleavage sequence specificity in V(D)J recombination
    • Agard, E. A., and S. M. Lewis. 2000. Postcleavage sequence specificity in V(D)J recombination. Mol. Cell. Biol. 20:5032-5040.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5032-5040
    • Agard, E.A.1    Lewis, S.M.2
  • 2
    • 0030887862 scopus 로고    scopus 로고
    • RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination
    • Agrawal, A., and D. G. Schatz. 1997. RAG1 and RAG2 form a stable postcleavage synaptic complex with DNA containing signal ends in V(D)J recombination. Cell 89:43-53.
    • (1997) Cell , vol.89 , pp. 43-53
    • Agrawal, A.1    Schatz, D.G.2
  • 3
    • 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
  • 4
    • 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
  • 5
    • 0345379607 scopus 로고    scopus 로고
    • A RAG1 and RAG2 tetramer complex is active in cleavage in V(D)J recombination
    • Bailin, T., X. Mo, and M. J. Sadofsky. 1999. A RAG1 and RAG2 tetramer complex is active in cleavage in V(D)J recombination. Mol. Cell. Biol. 19:4664-4671.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4664-4671
    • Bailin, T.1    Mo, X.2    Sadofsky, M.J.3
  • 7
    • 0025129447 scopus 로고
    • Mapping the active site of ribonuclease P RNA using a substrate containing a photoaffinily agent
    • Burgin, A. B., and N. R. Pace. 1990. Mapping the active site of ribonuclease P RNA using a substrate containing a photoaffinily agent. EMBO J. 9:4111-4118.
    • (1990) EMBO J. , vol.9 , pp. 4111-4118
    • Burgin, A.B.1    Pace, N.R.2
  • 8
    • 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
  • 9
    • 0034616993 scopus 로고    scopus 로고
    • Three-dimensional structure of the Tn5 synaptic complex transposition intermediate
    • Davies, D. R., I. Y. Goryshin, W. S. Reznikoff, and I. Rayment. 2000. Three-dimensional structure of the Tn5 synaptic complex transposition intermediate. Science 289:77-85.
    • (2000) Science , vol.289 , pp. 77-85
    • Davies, D.R.1    Goryshin, I.Y.2    Reznikoff, W.S.3    Rayment, I.4
  • 10
    • 0029864993 scopus 로고    scopus 로고
    • Initiation of V(D)J recombination in-vitro obeying the 12/23-rule
    • Eastman, Q. M., T. M. J. 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.J.2    Schatz, D.G.3
  • 11
    • 0032939926 scopus 로고    scopus 로고
    • Defection 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. Defection 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
  • 12
    • 0030984706 scopus 로고    scopus 로고
    • The composition of coding joints formed in V(D)J recombination is strongly affected by the nucleotide sequence of the coding ends and their relationship to the recombination signal sequences
    • Ezekiel, U. R., T. Sun, G. Bozek, and U. Storb. 1997. The composition of coding joints formed in V(D)J recombination is strongly affected by the nucleotide sequence of the coding ends and their relationship to the recombination signal sequences. Mol. Cell. Biol. 17:4191-4197.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4191-4197
    • Ezekiel, U.R.1    Sun, T.2    Bozek, G.3    Storb, U.4
  • 14
    • 0029655319 scopus 로고    scopus 로고
    • Mechanistic constraints on diversity in human V(D)J recombination
    • Gauss, G. H., and M. R. Lieber. 1996. Mechanistic constraints on diversity in human V(D)J recombination. Mol. Cell. Biol. 16:258-269.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 258-269
    • Gauss, G.H.1    Lieber, M.R.2
  • 15
    • 0030966099 scopus 로고    scopus 로고
    • Recent advances in understanding V(D)J recombination
    • Gellert, M. 1997. Recent advances in understanding V(D)J recombination. Adv. Immunol. 64:39-64.
    • (1997) Adv. Immunol. , vol.64 , pp. 39-64
    • Gellert, M.1
  • 16
    • 0027237601 scopus 로고
    • Coding end sequence can markedly affect the initiation of V(D)J recombination
    • Gerstein, R. M., and M. R. Lieber. 1993. Coding end sequence can markedly affect the initiation of V(D)J recombination. Genes Dev. 7:1459-1469.
    • (1993) Genes Dev. , vol.7 , pp. 1459-1469
    • Gerstein, R.M.1    Lieber, M.R.2
  • 18
    • 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
  • 19
    • 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
  • 20
    • 0001316589 scopus 로고    scopus 로고
    • Functional analysis of coordinated cleavage in V(D)J recombination
    • Kim, D. R., and M. A. Oettinger. 1998. Functional analysis of coordinated cleavage in V(D)J recombination. Mol. Cell. Biol. 18:4679-4688.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4679-4688
    • Kim, D.R.1    Oettinger, M.A.2
  • 21
    • 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
  • 22
    • 0028048275 scopus 로고
    • The mechanism of V(D)J joining: Lessons from molecular, immunulugical, and comparative analyses
    • Lewis, S. M. 1994. The mechanism of V(D)J joining: lessons from molecular, immunulugical, and comparative analyses. Adv. Immunol. 56:27-150.
    • (1994) Adv. Immunol. , vol.56 , pp. 27-150
    • Lewis, S.M.1
  • 23
    • 0026052160 scopus 로고
    • Cutting and closing without recombination in V(D)J joining
    • Lewis, S. M., and J. E. Hesse. 1991. Cutting and closing without recombination in V(D)J joining. EMBO J. 10:3631-3639.
    • (1991) EMBO J. , vol.10 , pp. 3631-3639
    • Lewis, S.M.1    Hesse, J.E.2
  • 24
    • 0024255703 scopus 로고
    • Novel strand exchanges in V(D)J recombination
    • Lewis, S. M., J. E. Hesse, K. Mizuuchi, and M. Gellert. 1988. Novel strand exchanges in V(D)J recombination. Cell 55:1099-1107.
    • (1988) Cell , vol.55 , pp. 1099-1107
    • Lewis, S.M.1    Hesse, J.E.2    Mizuuchi, K.3    Gellert, M.4
  • 25
    • 0028805853 scopus 로고
    • Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps
    • McBlane, J. F., D. C. van Gent, D. A. Ramsden, C. Romeo, C. A. Cuomo, M. Gellert, and M. A. Oettinger. 1995. Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps. Cell 83:387-395.
    • (1995) Cell , vol.83 , pp. 387-395
    • McBlane, J.F.1    Van Gent, D.C.2    Ramsden, D.A.3    Romeo, C.4    Cuomo, C.A.5    Gellert, M.6    Oettinger, M.A.7
  • 26
    • 0033592331 scopus 로고    scopus 로고
    • Mapping protease susceptibility sites on the Escherichia coli transcription factor sigma70
    • McMahan, S. A., and R. R. Burgess. 1999. Mapping protease susceptibility sites on the Escherichia coli transcription factor sigma70. Biochemistry 38: 12424-12431.
    • (1999) Biochemistry , vol.38 , pp. 12424-12431
    • McMahan, S.A.1    Burgess, R.R.2
  • 27
    • 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. 28:1228-12.36.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1228-1236
    • Mo, X.1    Bailin, T.2    Noggle, S.3    Sadofsky, M.J.4
  • 28
    • 0033548653 scopus 로고    scopus 로고
    • RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro
    • Mo, X., T. Bailin, and M. J. Sadofsky. 1999. RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro. J. Biol. Chem. 274:7025-7032.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7025-7032
    • Mo, X.1    Bailin, T.2    Sadofsky, M.J.3
  • 29
    • 0030929878 scopus 로고    scopus 로고
    • Nucleotide deletion and P addition in V(D)J recombination: A determinant role of the coding-end sequence
    • Nadel, B., and A. J. Feeney. 1997. Nucleotide deletion and P addition in V(D)J recombination: a determinant role of the coding-end sequence. Mol. Cell. Biol. 17:3768-3778.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3768-3778
    • Nadel, B.1    Feeney, A.J.2
  • 30
    • 0032541021 scopus 로고    scopus 로고
    • Spatial organization of transcription elongation complex in Escherichia coli
    • Nudler, E., I. Gusarov, E. Avetissova, M. Kozlov, and A. Goldfarb. 1998. Spatial organization of transcription elongation complex in Escherichia coli. Science 281:424-428.
    • (1998) Science , vol.281 , pp. 424-428
    • Nudler, E.1    Gusarov, I.2    Avetissova, E.3    Kozlov, M.4    Goldfarb, A.5
  • 31
    • 0025301095 scopus 로고
    • RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination
    • Oettinger, M. A., D. G. Schatz, C. Gorka, and D. Baltimore. 1990. RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science 248:1517-1523.
    • (1990) Science , vol.248 , pp. 1517-1523
    • Oettinger, M.A.1    Schatz, D.G.2    Gorka, C.3    Baltimore, D.4
  • 32
    • 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
  • 33
    • 0030753633 scopus 로고    scopus 로고
    • Cell-free V(D)J recombination
    • Ramsden, D. A., T. T. Paull, and M. Gellert. 1997. Cell-free V(D)J recombination. Nature 388:488-491.
    • (1997) Nature , vol.388 , pp. 488-491
    • Ramsden, D.A.1    Paull, T.T.2    Gellert, M.3
  • 34
    • 0027770854 scopus 로고
    • Expression and V(D)J recombination activity of mutated RAG-1 proteins
    • Sadofsky, M. J., J. E. Hesse, J. F. McBlane, and M. Gellert. 1993. Expression and V(D)J recombination activity of mutated RAG-1 proteins. Nucleic Acids Res. 21:5644-5650.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5644-5650
    • Sadofsky, M.J.1    Hesse, J.E.2    McBlane, J.F.3    Gellert, M.4
  • 35
    • 0029092358 scopus 로고
    • RAG-1 mutations that affect the target specificity of V(D)J recombination: A possible direct role of RAG-1 in site recognition
    • Sadofsky, M. J., J. E. Hesse, D. C. van Gent, and M. Gellert. 1995. RAG-1 mutations that affect the target specificity of V(D)J recombination: a possible direct role of RAG-1 in site recognition. Genes Dev. 9:2193-2199.
    • (1995) Genes Dev. , vol.9 , pp. 2193-2199
    • Sadofsky, M.J.1    Hesse, J.E.2    Van Gent, D.C.3    Gellert, M.4
  • 36
    • 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 F. 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, F.7
  • 37
    • 0024846088 scopus 로고
    • The V(D)J recombination activating gene. RAG-1
    • Schatz, D. G., M. A. Oettinger, and D. Baltimore. 1989. The V(D)J recombination activating gene. RAG-1. Cell 59:1035-1048.
    • (1989) Cell , vol.59 , pp. 1035-1048
    • Schatz, D.G.1    Oettinger, M.A.2    Baltimore, D.3
  • 38
    • 0032973315 scopus 로고    scopus 로고
    • DNA hairpin opening mediated by the RAG1 and RAG2 proteins
    • Shockett, P. E., and D. G. Schatz. 1999. DNA hairpin opening mediated by the RAG1 and RAG2 proteins. Mol. Cell. Biol. 19:4159-4166.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4159-4166
    • Shockett, P.E.1    Schatz, D.G.2
  • 39
    • 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. 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.3    Santagata, S.4    Baltimore, D.5    Panayotou, G.6
  • 40
    • 0032789128 scopus 로고    scopus 로고
    • Signal joint formation is inhibited in murine seid preB cells and fibroblasts in substrates with bomopolymeric coding ends
    • Sun, T., U. R. Ezekiel, L. Erskine, R. Agulo, G. Bozek, D. Roth, and U. Storb. 1999. Signal joint formation is inhibited in murine seid preB cells and fibroblasts in substrates with bomopolymeric coding ends. Mol. Immunol. 36:551-558.
    • (1999) Mol. Immunol. , vol.36 , pp. 551-558
    • Sun, T.1    Ezekiel, U.R.2    Erskine, L.3    Agulo, R.4    Bozek, G.5    Roth, D.6    Storb, U.7
  • 41
    • 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
  • 42
    • 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
  • 43
    • 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
  • 44
    • 0030994385 scopus 로고    scopus 로고
    • Stimulation of V(D)J cleavage by high mobility group proteins
    • van Gent, D. C., K. Hiom, T. T. Paull, and M. Gelert. 1997. Stimulation of V(D)J cleavage by high mobility group proteins. EMBO J. 16:2665-2670.
    • (1997) EMBO J. , vol.16 , pp. 2665-2670
    • Van Gent, D.C.1    Hiom, K.2    Paull, T.T.3    Gelert, M.4
  • 46
    • 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
  • 47
    • 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
  • 48
    • 0027717964 scopus 로고
    • Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins
    • Willis, M. C., B. J. Hicke, O. C. Uhlenbeck, T. R. Cech, and T. H. Koch. 1993. Photocrosslinking of 5-iodouracil-substituted RNA and DNA to proteins. Science 262:1255-1257.
    • (1993) Science , vol.262 , pp. 1255-1257
    • Willis, M.C.1    Hicke, B.J.2    Uhlenbeck, O.C.3    Cech, T.R.4    Koch, T.H.5
  • 49
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.