메뉴 건너뛰기




Volumn 47, Issue 43, 2008, Pages 11204-11211

Quantitative analyses of RAG-RSS interactions and conformations revealed by atomic force microscopy

Author keywords

[No Author keywords available]

Indexed keywords

ATOMIC PHYSICS; ATOMS; BENDING (DEFORMATION); BINDING SITES; CONFORMATIONS; DNA; ELECTRIC SPARK GAPS; FLOW INTERACTIONS; GENES; MICROSCOPIC EXAMINATION; NUCLEIC ACIDS; ORGANIC ACIDS; PROTEINS; SCANNING PROBE MICROSCOPY; VANADIUM COMPOUNDS;

EID: 54849423896     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801426x     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0030678531 scopus 로고    scopus 로고
    • Nicking is asynchronous and stimulated by synapsis in 12/23 rule-regulated V(D)J cleavage
    • Eastman, Q. M., and Schatz, D. G. (1997) Nicking is asynchronous and stimulated by synapsis in 12/23 rule-regulated V(D)J cleavage. Nucleic Acids Res. 25, 4370-4378.
    • (1997) Nucleic Acids Res , vol.25 , pp. 4370-4378
    • Eastman, Q.M.1    Schatz, D.G.2
  • 2
    • 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 Lieber, M. R. (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
  • 3
    • 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 Lieber, M. R. (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
  • 4
    • 0028237683 scopus 로고
    • Definition of a core region of RAG-2 that is functional in V(D)J recombination
    • Sadofsky, M. J., Hesse, J. E., and Geliert, M. 1994) Definition of a core region of RAG-2 that is functional in V(D)J recombination. Nucleic Acids Res. 22, 1805-1809.
    • (1994) Nucleic Acids Res , vol.22 , pp. 1805-1809
    • Sadofsky, M.J.1    Hesse, J.E.2    Geliert, M.3
  • 5
    • 0027770854 scopus 로고
    • Expression and V(D)J recombination activity of mutated RAG-1 proteins
    • Sadofsky, M. J., Hesse, J. E., McBlane, J. F., and Gellert, M. (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
  • 6
    • 0001265782 scopus 로고    scopus 로고
    • RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination
    • Difilippantonio, M. J., McMahan, C. J., Eastman, Q. M., Spanopoulou, E., and Schatz, D. G. (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
  • 7
    • 0030592523 scopus 로고    scopus 로고
    • The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination
    • Spanopoulou, E., Zaitseva, F., Wang, F. H., Santagata, S., Baltimore, D., and Panayotou, G. (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
  • 8
    • 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 Desiderio, S. (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
  • 9
    • 0033548653 scopus 로고    scopus 로고
    • RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro
    • Mo, X., Bailin, T., and Sadofsky, M. J. (1999) RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro. J. Biol. Chem. 274, 7025-7031.
    • (1999) J. Biol. Chem , vol.274 , pp. 7025-7031
    • Mo, X.1    Bailin, T.2    Sadofsky, M.J.3
  • 10
    • 0035813101 scopus 로고    scopus 로고
    • Identification of two topologically independent domains in RAG1 and their role in macromolecular interactions relevant to V(D)J recombination
    • Arbuckle, J. L., Fauss, L. A., Simpson, R., Ptaszek, L. M., and Rodgers, K. K. (2001) Identification of two topologically independent domains in RAG1 and their role in macromolecular interactions relevant to V(D)J recombination. J. Biol. Chem. 276, 37093-37101.
    • (2001) J. Biol. Chem , vol.276 , pp. 37093-37101
    • Arbuckle, J.L.1    Fauss, L.A.2    Simpson, R.3    Ptaszek, L.M.4    Rodgers, K.K.5
  • 11
    • 0038719678 scopus 로고    scopus 로고
    • The central domain of core RAG1 preferentially recognizes single-stranded recombination signal sequence heptamer
    • Peak, M. M., Arbuckle, J. L., and Rodgers, K. K. (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
  • 12
    • 41949095597 scopus 로고    scopus 로고
    • RAG-heptamer interaction in the synaptic complex is a crucial biochemical checkpoint for the 12/23 recombination rule
    • Nishihara, T., Nagawa, F., Imai, T., and Sakano, H. (2008) RAG-heptamer interaction in the synaptic complex is a crucial biochemical checkpoint for the 12/23 recombination rule. J. Biol. Chem. 283, 4877-4885.
    • (2008) J. Biol. Chem , vol.283 , pp. 4877-4885
    • Nishihara, T.1    Nagawa, F.2    Imai, T.3    Sakano, H.4
  • 13
    • 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 Desiderio, S. (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
  • 14
    • 0031826699 scopus 로고    scopus 로고
    • Distinct roles of RAG1 and RAG2 in binding the V(D)J recombination signal sequences
    • Akamatsu, Y., and Oettinger, M. A. (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
  • 15
    • 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
  • 16
    • 0029814965 scopus 로고    scopus 로고
    • DNA sequence and structure requirements for cleavage of V(D)J recombination signal sequences
    • Cuomo, C. A., Mundy, C. L., and Oettinger, M. A. (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
  • 17
    • 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., McBlane, J. F., van Gent, D. C., and Gellert, M. (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
  • 18
    • 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., Bonaldi, T., Beltrame, M., Santagata, S., Bianchi, M. E., and Spanopoulou, E. (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
  • 19
    • 0037841390 scopus 로고    scopus 로고
    • Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials
    • Shlyakhtenko, L. S., Gall, A. A., Filonov, A., Cerovac, Z., Lushnikov, A., and Lyubchenko, Y. L. (2003) Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials. Ultramicroscopy 97, 279-287.
    • (2003) Ultramicroscopy , vol.97 , pp. 279-287
    • Shlyakhtenko, L.S.1    Gall, A.A.2    Filonov, A.3    Cerovac, Z.4    Lushnikov, A.5    Lyubchenko, Y.L.6
  • 21
    • 0034814802 scopus 로고    scopus 로고
    • A novel single-molecule study to determine protein-protein association constants
    • Ratcliff, G. C., and Erie, D. A. (2001) A novel single-molecule study to determine protein-protein association constants. J. Am. Chem. Soc. 123, 5632-5635.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 5632-5635
    • Ratcliff, G.C.1    Erie, D.A.2
  • 22
    • 0037388110 scopus 로고    scopus 로고
    • Self-association and conformational properties of RAG1: Implications for formation of the V(D)J recombinase
    • Godderz, L. J., Rahman, N. S., Risinger, G. M., Arbuckle, J. L., and Rodgers, K. K. (2003) Self-association and conformational properties of RAG1: implications for formation of the V(D)J recombinase. Nucleic Acids Res. 31, 2014-2023.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2014-2023
    • Godderz, L.J.1    Rahman, N.S.2    Risinger, G.M.3    Arbuckle, J.L.4    Rodgers, K.K.5
  • 23
    • 0028859015 scopus 로고
    • Specific binding of the NikA protein to one arm of 17-base-pair inverted repeat sequences within the oriT region of plasmid
    • Furuya, N., and Komano, T. (1995) Specific binding of the NikA protein to one arm of 17-base-pair inverted repeat sequences within the oriT region of plasmid. J. Bacteriol. 177, 46-51.
    • (1995) J. Bacteriol , vol.177 , pp. 46-51
    • Furuya, N.1    Komano, T.2
  • 24
    • 0028364238 scopus 로고
    • Multiple DNA conformational changes induced by an initiator protein precede the nicking reaction in a rolling circle replication origin
    • Higashitani, A., Greenstein, D., Hirokawa, H., Asano, S., and Horiuchi, K. (1994) Multiple DNA conformational changes induced by an initiator protein precede the nicking reaction in a rolling circle replication origin. J. Mol. Biol. 237, 388-400.
    • (1994) J. Mol. Biol , vol.237 , pp. 388-400
    • Higashitani, A.1    Greenstein, D.2    Hirokawa, H.3    Asano, S.4    Horiuchi, K.5
  • 25
    • 34047146480 scopus 로고    scopus 로고
    • Interactions between the RepB initiator protein of plasmid pMV158 and two distant DNA regions within the origin of replication
    • Ruiz-Maso, J. A., Lurz, R., Espinosa, M., and Del Solar, G. 2007) Interactions between the RepB initiator protein of plasmid pMV158 and two distant DNA regions within the origin of replication. Nucleic Acids Res.
    • (2007) Nucleic Acids Res
    • Ruiz-Maso, J.A.1    Lurz, R.2    Espinosa, M.3    Del Solar, G.4
  • 27
    • 0030994385 scopus 로고    scopus 로고
    • Stimulation of V(D)J cleavage by high mobility group proteins
    • van Gent, D. C., Hiom, K., Pauli, T. T., and Gellert, M. (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    Pauli, T.T.3    Gellert, M.4
  • 28
    • 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., Weis-Garcia, F., Malik, S., Besmer, E., Bustin, M., Nussenzweig, M. C., and Cortes, P. 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
  • 29
    • 0036839614 scopus 로고    scopus 로고
    • A RAG-1/RAG-2 tetramer supports 12/23-regulated synapsis, cleavage, and transposition of V(D)J recombination signals
    • Swanson, P. C. (2002) A RAG-1/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
  • 30
    • 54849420186 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., Kriatchko, A. N., Swanson, P. C., Bright, F. V., and Schatz, D. G. (2007) RAG1-DNA binding in V(D)J recombination. Specificity and DNA-induced conformational changes revealed by fluorescence and CD spectroscopy. Mol. Cell. Biol.
    • (2007) Mol. Cell. Biol
    • Ciubotaru, M.1    Kriatchko, A.N.2    Swanson, P.C.3    Bright, F.V.4    Schatz, D.G.5
  • 32
    • 0033040499 scopus 로고    scopus 로고
    • DNA restriction dependent on two recognition sites: Activities of the SfiI restriction-modification system in Escherichia coli
    • Bilcock, D. T., and Halford, S. E. (1999) DNA restriction dependent on two recognition sites: activities of the SfiI restriction-modification system in Escherichia coli. Mol. Microbiol. 31, 1243-1254.
    • (1999) Mol. Microbiol , vol.31 , pp. 1243-1254
    • Bilcock, D.T.1    Halford, S.E.2
  • 33
    • 33846014618 scopus 로고    scopus 로고
    • Probing interactions within the synaptic DNA-SfiI complex by AFM force spectroscopy
    • Krasnoslobodtsev, A. V., Shlyakhtenko, L. S., and Lyubchenko, Y. L. (2007) Probing interactions within the synaptic DNA-SfiI complex by AFM force spectroscopy. J. Mol. Biol. 365, 1407-1416.
    • (2007) J. Mol. Biol , vol.365 , pp. 1407-1416
    • Krasnoslobodtsev, A.V.1    Shlyakhtenko, L.S.2    Lyubchenko, Y.L.3
  • 34
    • 28644435380 scopus 로고    scopus 로고
    • A view of consecutive binding events from structures of tetrameric endonuclease SfiI bound to DNA
    • Vanamee, E. S., Viadiu, H., Kucera, R., Dorner, L., Picone, S., Schildkraut, I., and Aggarwal, A. K. (2005) A view of consecutive binding events from structures of tetrameric endonuclease SfiI bound to DNA. EMBO J. 24, 4198-4208.
    • (2005) EMBO J , vol.24 , pp. 4198-4208
    • Vanamee, E.S.1    Viadiu, H.2    Kucera, R.3    Dorner, L.4    Picone, S.5    Schildkraut, I.6    Aggarwal, A.K.7
  • 37
    • 33845500268 scopus 로고    scopus 로고
    • Stepwise binding and bending of DNA by Escherichia coli integration host factor
    • Sugimura, S., and Crothers, D. M. (2006) Stepwise binding and bending of DNA by Escherichia coli integration host factor. Proc. Natl. Acad. Sci. U.S.A. 103, 18510-18514.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 18510-18514
    • Sugimura, S.1    Crothers, D.M.2
  • 39
    • 1542287213 scopus 로고    scopus 로고
    • A non-B-DNA structure at the Bcl-2 major breakpoint region is cleaved by the RAG complex
    • Raghavan, S. C., Swanson, P. C., Wu, X., Hsieh, C. L., and Lieber, M. R. (2004) A non-B-DNA structure at the Bcl-2 major breakpoint region is cleaved by the RAG complex. Nature 428, 88-93.
    • (2004) Nature , vol.428 , pp. 88-93
    • Raghavan, S.C.1    Swanson, P.C.2    Wu, X.3    Hsieh, C.L.4    Lieber, M.R.5
  • 40
    • 21744455557 scopus 로고    scopus 로고
    • Double-strand break formation by the RAG complex at the bcl-2 major breakpoint region and at other non-B DNA structures in vitro
    • Raghavan, S. C., Swanson, P. C., Ma, Y., and Lieber, M. R. (2005) Double-strand break formation by the RAG complex at the bcl-2 major breakpoint region and at other non-B DNA structures in vitro. Mol. Cell. Biol. 25, 5904-5919.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 5904-5919
    • Raghavan, S.C.1    Swanson, P.C.2    Ma, Y.3    Lieber, M.R.4
  • 41
    • 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 Lieber, M. R. (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
  • 42
    • 34247604497 scopus 로고    scopus 로고
    • The structure-specific nicking of small heteroduplexes by the RAG complex: Implications for lymphoid chromosomal translocations
    • Raghavan, S. C., Gu, J., Swanson, P. C., and Lieber, M. R. (2007) The structure-specific nicking of small heteroduplexes by the RAG complex: Implications for lymphoid chromosomal translocations. DNA Repair (Amsterdam) 6, 751-759.
    • (2007) DNA Repair (Amsterdam) , vol.6 , pp. 751-759
    • Raghavan, S.C.1    Gu, J.2    Swanson, P.C.3    Lieber, M.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.