메뉴 건너뛰기




Volumn 22, Issue 1, 2010, Pages 10-16

The origins of the Rag genes-From transposition to V(D)J recombination

Author keywords

Adaptive immunity; Evolution; RAG1; RAG2; Transposase

Indexed keywords

RAG1 PROTEIN; RAG2 PROTEIN; RECOMBINASE; TRANSPOSASE;

EID: 77949269476     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.smim.2009.11.004     Document Type: Review
Times cited : (87)

References (52)
  • 1
    • 0020534965 scopus 로고
    • Somatic generation of antibody diversity
    • Tonegawa S. Somatic generation of antibody diversity. Nature 302 (1983) 575-581
    • (1983) Nature , vol.302 , pp. 575-581
    • Tonegawa, S.1
  • 2
    • 0018627375 scopus 로고
    • Sequences at the somatic recombination sites of immunoglobulin light-chain genes
    • Sakano H., Huppi K., Heinrich G., and Tonegawa S. Sequences at the somatic recombination sites of immunoglobulin light-chain genes. Nature 280 (1979) 288-294
    • (1979) Nature , vol.280 , pp. 288-294
    • Sakano, H.1    Huppi, K.2    Heinrich, G.3    Tonegawa, S.4
  • 3
    • 0025301095 scopus 로고
    • RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination
    • Oettinger M.A., Schatz D.G., Gorka C., and Baltimore D. RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science 248 (1990) 1517-1523
    • (1990) Science , vol.248 , pp. 1517-1523
    • Oettinger, M.A.1    Schatz, D.G.2    Gorka, C.3    Baltimore, D.4
  • 4
    • 0024846088 scopus 로고
    • The V(D)J recombination activating gene, RAG-1
    • Schatz D.G., Oettinger M.A., and Baltimore D. The V(D)J recombination activating gene, RAG-1. Cell 59 (1989) 1035-1048
    • (1989) Cell , vol.59 , pp. 1035-1048
    • Schatz, D.G.1    Oettinger, M.A.2    Baltimore, D.3
  • 6
    • 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., van Gent D.C., Ramsden D.A., Romeo C., Cuomo C.A., Gellert M., et al. Cleavage at a V(D)J recombination signal requires only RAG1 and RAG2 proteins and occurs in two steps. Cell 83 (1995) 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
  • 7
    • 0032555758 scopus 로고    scopus 로고
    • DNA transposition by the RAG1 and RAG2 proteins: a possible source of oncogenic translocations
    • Hiom K., Melek M., and Gellert M. DNA transposition by the RAG1 and RAG2 proteins: a possible source of oncogenic translocations. Cell 94 (1998) 463-470
    • (1998) Cell , vol.94 , pp. 463-470
    • Hiom, K.1    Melek, M.2    Gellert, M.3
  • 8
    • 0032551829 scopus 로고    scopus 로고
    • Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system
    • Agrawal A., Eastman Q.M., and Schatz D.G. Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system. Nature 394 (1998) 744-751
    • (1998) Nature , vol.394 , pp. 744-751
    • Agrawal, A.1    Eastman, Q.M.2    Schatz, D.G.3
  • 9
    • 0345146909 scopus 로고    scopus 로고
    • In vivo transposition mediated by V(D)J recombinase in human T lymphocytes
    • Messier T.L., O'Neill J.P., Hou S.M., Nicklas J.A., and Finette B.A. In vivo transposition mediated by V(D)J recombinase in human T lymphocytes. EMBO J 22 (2003) 1381-1388
    • (2003) EMBO J , vol.22 , pp. 1381-1388
    • Messier, T.L.1    O'Neill, J.P.2    Hou, S.M.3    Nicklas, J.A.4    Finette, B.A.5
  • 10
    • 32044434448 scopus 로고    scopus 로고
    • Mobilization of RAG-generated signal ends by transposition and insertion in vivo
    • Chatterji M., Tsai C.L., and Schatz D.G. Mobilization of RAG-generated signal ends by transposition and insertion in vivo. Mol Cell Biol 26 (2006) 1558-1568
    • (2006) Mol Cell Biol , vol.26 , pp. 1558-1568
    • Chatterji, M.1    Tsai, C.L.2    Schatz, D.G.3
  • 11
    • 0028867419 scopus 로고
    • New insights into V(D)J recombination and its role in the evolution of the immune system
    • Thompson C.B. New insights into V(D)J recombination and its role in the evolution of the immune system. Immunity 3 (1995) 531-539
    • (1995) Immunity , vol.3 , pp. 531-539
    • Thompson, C.B.1
  • 12
    • 7444236477 scopus 로고    scopus 로고
    • Antigen receptor genes and the evolution of a recombinase
    • Schatz D.G. Antigen receptor genes and the evolution of a recombinase. Semin Immunol 16 (2004) 245-256
    • (2004) Semin Immunol , vol.16 , pp. 245-256
    • Schatz, D.G.1
  • 13
    • 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. Expression and V(D)J recombination activity of mutated RAG-1 proteins. Nucleic Acids Res 21 (1993) 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
  • 14
    • 0027197151 scopus 로고
    • Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination
    • Silver D.P., Spanopoulou E., Mulligan R.C., and Baltimore D. Dispensable sequence motifs in the RAG-1 and RAG-2 genes for plasmid V(D)J recombination. Proc Natl Acad Sci USA 90 (1993) 6100-6104
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6100-6104
    • Silver, D.P.1    Spanopoulou, E.2    Mulligan, R.C.3    Baltimore, D.4
  • 15
    • 3242879258 scopus 로고    scopus 로고
    • The taming of a transposon: V(D)J recombination and the immune system
    • Jones J.M., and Gellert M. The taming of a transposon: V(D)J recombination and the immune system. Immunol Rev 200 (2004) 233-248
    • (2004) Immunol Rev , vol.200 , pp. 233-248
    • Jones, J.M.1    Gellert, M.2
  • 18
    • 64649092651 scopus 로고    scopus 로고
    • The roles of the RAG1 and RAG2 "non-core" regions in V(D)J recombination and lymphocyte development
    • Jones J.M., and Simkus C. The roles of the RAG1 and RAG2 "non-core" regions in V(D)J recombination and lymphocyte development. Arch Immunol Ther Exp (Warsz) 57 (2009) 105-116
    • (2009) Arch Immunol Ther Exp (Warsz) , vol.57 , pp. 105-116
    • Jones, J.M.1    Simkus, C.2
  • 19
    • 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. The homeodomain region of Rag-1 reveals the parallel mechanisms of bacterial and V(D)J recombination. Cell 87 (1996) 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
  • 20
    • 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. RAG1 mediates signal sequence recognition and recruitment of RAG2 in V(D)J recombination. Cell 87 (1996) 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
  • 21
    • 66149096706 scopus 로고    scopus 로고
    • Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis
    • Yin F.F., Bailey S., Innis C.A., Ciubotaru M., Kamtekar S., Steitz T.A., et al. Structure of the RAG1 nonamer binding domain with DNA reveals a dimer that mediates DNA synapsis. Nat Struct Mol Biol 16 (2009) 499-508
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 499-508
    • Yin, F.F.1    Bailey, S.2    Innis, C.A.3    Ciubotaru, M.4    Kamtekar, S.5    Steitz, T.A.6
  • 22
  • 23
    • 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. Identification of two topologically independent domains in RAG1 and their role in macromolecular interactions relevant to V(D)J recombination. J Biol Chem 276 (2001) 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
  • 24
    • 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. The central domain of core RAG1 preferentially recognizes single-stranded recombination signal sequence heptamer. J Biol Chem 278 (2003) 18235-18240
    • (2003) J Biol Chem , vol.278 , pp. 18235-18240
    • Peak, M.M.1    Arbuckle, J.L.2    Rodgers, K.K.3
  • 26
    • 0034616993 scopus 로고    scopus 로고
    • Three-dimensional structure of the Tn5 synaptic complex transposition intermediate
    • Davies D.R., Goryshin I.Y., Reznikoff W.S., and Rayment I. Three-dimensional structure of the Tn5 synaptic complex transposition intermediate. Science 289 (2000) 77-85
    • (2000) Science , vol.289 , pp. 77-85
    • Davies, D.R.1    Goryshin, I.Y.2    Reznikoff, W.S.3    Rayment, I.4
  • 27
    • 11144223344 scopus 로고    scopus 로고
    • Molecular biology: hairpins at split ends in DNA
    • Oettinger M.A. Molecular biology: hairpins at split ends in DNA. Nature 432 (2004) 960-961
    • (2004) Nature , vol.432 , pp. 960-961
    • Oettinger, M.A.1
  • 28
    • 11144245992 scopus 로고    scopus 로고
    • Transposition of hAT elements links transposable elements and V(D)J recombination
    • Zhou L., Mitra R., Atkinson P.W., Hickman A.B., Dyda F., and Craig N.L. Transposition of hAT elements links transposable elements and V(D)J recombination. Nature 432 (2004) 995-1001
    • (2004) Nature , vol.432 , pp. 995-1001
    • Zhou, L.1    Mitra, R.2    Atkinson, P.W.3    Hickman, A.B.4    Dyda, F.5    Craig, N.L.6
  • 29
    • 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., Villey I.J., Ptaszek L.M., and Schatz D.G. Identification of two catalytic residues in RAG1 that define a single active site within the RAG1/RAG2 protein complex. Mol Cell 5 (2000) 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
  • 30
    • 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., Wibbenmeyer J.A., and Roth D.B. 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 (1999) 3059-3069
    • (1999) Genes Dev , vol.13 , pp. 3059-3069
    • Landree, M.A.1    Wibbenmeyer, J.A.2    Roth, D.B.3
  • 31
    • 0000675571 scopus 로고    scopus 로고
    • Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase
    • Kim D.R., Dai Y., Mundy C.L., Yang W., and Oettinger M.A. Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase. Genes Dev 13 (1999) 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
  • 32
    • 0027184481 scopus 로고
    • A general two-metal-ion mechanism for catalytic RNA
    • Steitz T.A., and Steitz J.A. A general two-metal-ion mechanism for catalytic RNA. Proc Natl Acad Sci USA 90 (1993) 6498-6502
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6498-6502
    • Steitz, T.A.1    Steitz, J.A.2
  • 33
    • 65349136539 scopus 로고    scopus 로고
    • New superfamilies of eukaryotic DNA transposons and their internal divisions
    • Bao W., Jurka M.G., Kapitonov V.V., and Jurka J. New superfamilies of eukaryotic DNA transposons and their internal divisions. Mol Biol Evol 26 (2009) 983-993
    • (2009) Mol Biol Evol , vol.26 , pp. 983-993
    • Bao, W.1    Jurka, M.G.2    Kapitonov, V.V.3    Jurka, J.4
  • 34
    • 42349111552 scopus 로고    scopus 로고
    • A universal classification of eukaryotic transposable elements implemented in Repbase
    • [author reply 4]
    • Kapitonov V.V., and Jurka J. A universal classification of eukaryotic transposable elements implemented in Repbase. Nat Rev Genet 9 (2008) 411-412 [author reply 4]
    • (2008) Nat Rev Genet , vol.9 , pp. 411-412
    • Kapitonov, V.V.1    Jurka, J.2
  • 35
    • 22744445703 scopus 로고    scopus 로고
    • RAG1 core and V(D)J recombination signal sequences were derived from Transib transposons
    • Kapitonov V.V., and Jurka J. RAG1 core and V(D)J recombination signal sequences were derived from Transib transposons. PLoS Biol 3 (2005) e181
    • (2005) PLoS Biol , vol.3
    • Kapitonov, V.V.1    Jurka, J.2
  • 36
    • 0037975554 scopus 로고    scopus 로고
    • Molecular paleontology of transposable elements in the Drosophila melanogaster genome
    • Kapitonov V.V., and Jurka J. Molecular paleontology of transposable elements in the Drosophila melanogaster genome. Proc Natl Acad Sci USA 100 (2003) 6569-6574
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6569-6574
    • Kapitonov, V.V.1    Jurka, J.2
  • 37
    • 41149163571 scopus 로고    scopus 로고
    • Molluscan mobile elements similar to the vertebrate recombination-activating genes
    • Panchin Y., and Moroz L.L. Molluscan mobile elements similar to the vertebrate recombination-activating genes. Biochem Biophys Res Commun 369 (2008) 818-823
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 818-823
    • Panchin, Y.1    Moroz, L.L.2
  • 38
    • 0031712128 scopus 로고    scopus 로고
    • The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis
    • Callebaut I., and Mornon J.P. The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis. Cell Mol Life Sci 54 (1998) 880-891
    • (1998) Cell Mol Life Sci , vol.54 , pp. 880-891
    • Callebaut, I.1    Mornon, J.P.2
  • 39
    • 37249041657 scopus 로고    scopus 로고
    • RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination
    • Matthews A.G., Kuo A.J., Ramon-Maiques S., Han S., Champagne K.S., Ivanov D., et al. RAG2 PHD finger couples histone H3 lysine 4 trimethylation with V(D)J recombination. Nature 450 (2007) 1106-1110
    • (2007) Nature , vol.450 , pp. 1106-1110
    • Matthews, A.G.1    Kuo, A.J.2    Ramon-Maiques, S.3    Han, S.4    Champagne, K.S.5    Ivanov, D.6
  • 40
    • 0033961690 scopus 로고    scopus 로고
    • The kelch repeat superfamily of proteins: propellers of cell function
    • Adams J., Kelso R., and Cooley L. The kelch repeat superfamily of proteins: propellers of cell function. Trends Cell Biol 10 (2000) 17-24
    • (2000) Trends Cell Biol , vol.10 , pp. 17-24
    • Adams, J.1    Kelso, R.2    Cooley, L.3
  • 41
    • 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 Gellert M. Definition of a core region of RAG-2 that is functional in V(D)J recombination. Nucleic Acids Res 22 (1994) 1805-1809
    • (1994) Nucleic Acids Res , vol.22 , pp. 1805-1809
    • Sadofsky, M.J.1    Hesse, J.E.2    Gellert, M.3
  • 42
    • 0034765256 scopus 로고    scopus 로고
    • Identification of basic residues in RAG2 critical for DNA binding by the RAG1-RAG2 complex
    • Fugmann S.D., and Schatz D.G. Identification of basic residues in RAG2 critical for DNA binding by the RAG1-RAG2 complex. Mol Cell 8 (2001) 899-910
    • (2001) Mol Cell , vol.8 , pp. 899-910
    • Fugmann, S.D.1    Schatz, D.G.2
  • 43
    • 4644283372 scopus 로고    scopus 로고
    • Joining mutants of RAG1 and RAG2 that demonstrate impaired interactions with the coding-end DNA
    • Nagawa F., Hirose S., Nishizumi H., Nishihara T., and Sakano H. Joining mutants of RAG1 and RAG2 that demonstrate impaired interactions with the coding-end DNA. J Biol Chem 279 (2004) 38360-38368
    • (2004) J Biol Chem , vol.279 , pp. 38360-38368
    • Nagawa, F.1    Hirose, S.2    Nishizumi, H.3    Nishihara, T.4    Sakano, H.5
  • 44
    • 33745713437 scopus 로고    scopus 로고
    • It takes a PHD to read the histone code
    • Mellor J. It takes a PHD to read the histone code. Cell 126 (2006) 22-24
    • (2006) Cell , vol.126 , pp. 22-24
    • Mellor, J.1
  • 45
    • 35349024178 scopus 로고    scopus 로고
    • A plant homeodomain in Rag-2 that binds hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement
    • Liu Y., Subrahmanyam R., Chakraborty T., Sen R., and Desiderio S. A plant homeodomain in Rag-2 that binds hypermethylated lysine 4 of histone H3 is necessary for efficient antigen-receptor-gene rearrangement. Immunity (2007)
    • (2007) Immunity
    • Liu, Y.1    Subrahmanyam, R.2    Chakraborty, T.3    Sen, R.4    Desiderio, S.5
  • 46
    • 37649026007 scopus 로고    scopus 로고
    • The plant homeodomain finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2
    • Ramon-Maiques S., Kuo A.J., Carney D., Matthews A.G., Oettinger M.A., Gozani O., et al. The plant homeodomain finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2. Proc Natl Acad Sci USA 104 (2007) 18993-18998
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18993-18998
    • Ramon-Maiques, S.1    Kuo, A.J.2    Carney, D.3    Matthews, A.G.4    Oettinger, M.A.5    Gozani, O.6
  • 47
    • 0033427205 scopus 로고    scopus 로고
    • Cyclin A/CDK2 regulates V(D)J recombination by coordinating RAG-2 accumulation and DNA repair
    • Lee J., and Desiderio S. Cyclin A/CDK2 regulates V(D)J recombination by coordinating RAG-2 accumulation and DNA repair. Immunity 11 (1999) 771-781
    • (1999) Immunity , vol.11 , pp. 771-781
    • Lee, J.1    Desiderio, S.2
  • 49
    • 24944585768 scopus 로고    scopus 로고
    • Macroarray analysis of coelomocyte gene expression in response to LPS in the sea urchin. Identification of unexpected immune diversity in an invertebrate
    • Nair S.V., Del Valle H., Gross P.S., Terwilliger D.P., and Smith L.C. Macroarray analysis of coelomocyte gene expression in response to LPS in the sea urchin. Identification of unexpected immune diversity in an invertebrate. Physiol Genomics 22 (2005) 33-47
    • (2005) Physiol Genomics , vol.22 , pp. 33-47
    • Nair, S.V.1    Del Valle, H.2    Gross, P.S.3    Terwilliger, D.P.4    Smith, L.C.5
  • 50
    • 45049086632 scopus 로고    scopus 로고
    • The PHD domain of the sea urchin RAG2 homolog, SpRAG2L, recognizes dimethylated lysine 4 in histone H3 tails
    • Wilson D.R., Norton D.D., and Fugmann S.D. The PHD domain of the sea urchin RAG2 homolog, SpRAG2L, recognizes dimethylated lysine 4 in histone H3 tails. Dev Comp Immunol 32 (2008) 1221-1230
    • (2008) Dev Comp Immunol , vol.32 , pp. 1221-1230
    • Wilson, D.R.1    Norton, D.D.2    Fugmann, S.D.3
  • 51
    • 0029796084 scopus 로고    scopus 로고
    • Primordial emergence of the recombination activating gene 1 (RAG1): sequence of the complete shark gene indicates homology to microbial integrases
    • Bernstein R.M., Schluter S.F., Bernstein H., and Marchalonis J.J. Primordial emergence of the recombination activating gene 1 (RAG1): sequence of the complete shark gene indicates homology to microbial integrases. Proc Natl Acad Sci USA 93 (1996) 9454-9459
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9454-9459
    • Bernstein, R.M.1    Schluter, S.F.2    Bernstein, H.3    Marchalonis, J.J.4
  • 52
    • 3242877717 scopus 로고    scopus 로고
    • Computational tools for understanding sequence variability in recombination signals
    • Cowell L.G., Davila M., Ramsden D., and Kelsoe G. Computational tools for understanding sequence variability in recombination signals. Immunol Rev 200 (2004) 57-69
    • (2004) Immunol Rev , vol.200 , pp. 57-69
    • Cowell, L.G.1    Davila, M.2    Ramsden, D.3    Kelsoe, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.