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Volumn 432, Issue 7020, 2004, Pages 995-1001

Transposition of hAT elements links transposable elements and V(D)J recombination

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ANTIGENS; CATALYSIS; GENES;

EID: 11144245992     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03157     Document Type: Article
Times cited : (177)

References (50)
  • 1
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E. S. et al. Initial sequencing and analysis of the human genome. Nature 409, 860-921 (2001).
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1
  • 2
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J. C. et al. The sequence of the human genome. Science 291, 1304-1351 (2001).
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 3
    • 0032723359 scopus 로고    scopus 로고
    • Integrating DNA: Transposases and retroviral integrases
    • Haren, L., Ton-Hoang, B., & Chandler, M. Integrating DNA: transposases and retroviral integrases. Annu. Rev. Microbiol 53, 245-281 (1999).
    • (1999) Annu. Rev. Microbiol , vol.53 , pp. 245-281
    • Haren, L.1    Ton-Hoang, B.2    Chandler, M.3
  • 5
    • 0035343895 scopus 로고    scopus 로고
    • Comparative architecture of transposase and integrase complexes
    • Rice, P. A. & Baker, T. A. Comparative architecture of transposase and integrase complexes. Nature Struct. Biol. 8, 302-307 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 302-307
    • Rice, P.A.1    Baker, T.A.2
  • 6
    • 0034913514 scopus 로고    scopus 로고
    • Structure and evolution of the hAT transposon superfamily
    • Rubin, E., Lithwick, G. & Levy, A. A. Structure and evolution of the hAT transposon superfamily. Genetics 158, 949-957 (2001).
    • (2001) Genetics , vol.158 , pp. 949-957
    • Rubin, E.1    Lithwick, G.2    Levy, A.A.3
  • 7
    • 0003873979 scopus 로고    scopus 로고
    • (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A.) (ASM, Washington DC)
    • Kunze, R. W. & Weil, C. F. in Mobile DNA II (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A.) 565-610 (ASM, Washington DC, 2002).
    • (2002) Mobile DNA II , pp. 565-610
    • Kunze, R.W.1    Weil, C.F.2
  • 8
    • 0003873979 scopus 로고    scopus 로고
    • (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A.) (ASM, Washington DC)
    • Robertson, H. M. in Mobile DNA II (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A.) 1093-1110 (ASM, Washington DC, 2002).
    • (2002) Mobile DNA II , pp. 1093-1110
    • Robertson, H.M.1
  • 9
    • 0025935671 scopus 로고
    • Evidence for a common evolutionary origin of inverted repeat transposon in Drosophila and plants: Hobo, Activator, and Tam3
    • Calvi, B. R., Hong, T. J., Findley, S. D. & Gelbart, W. M. Evidence for a common evolutionary origin of inverted repeat transposon in Drosophila and plants: hobo, Activator, and Tam3. Cell 66, 465-471 (1991).
    • (1991) Cell , vol.66 , pp. 465-471
    • Calvi, B.R.1    Hong, T.J.2    Findley, S.D.3    Gelbart, W.M.4
  • 10
    • 0028063082 scopus 로고
    • The Hermes transposable element from the house fly, Musca domestica, is a short inverted repeat-type element of the hobo, Ac, and Tam3 (hAT) element family
    • Warren, W, D., Atkinson, P. W. & O'Brochta, D. A. The Hermes transposable element from the house fly, Musca domestica, is a short inverted repeat-type element of the hobo, Ac, and Tam3 (hAT) element family. Genet. Res. 64, 87-97 (1994).
    • (1994) Genet. Res. , vol.64 , pp. 87-97
    • Warren, W.D.1    Atkinson, P.W.2    O'Brochta, D.A.3
  • 11
    • 0029895562 scopus 로고    scopus 로고
    • Hermes, a functional non-Drosophilid insect gene vector from Musca domestica
    • O'Brochta, D. A., Warren, W. D., Saville, K. I. & Atkinson, P. W. Hermes, a functional non-Drosophilid insect gene vector from Musca domestica. Genetics 142, 907-914 (1996).
    • (1996) Genetics , vol.142 , pp. 907-914
    • O'Brochta, D.A.1    Warren, W.D.2    Saville, K.I.3    Atkinson, P.W.4
  • 12
    • 0035997348 scopus 로고    scopus 로고
    • V(D)J recombination: RAG proteins, repair factors, and regulation
    • Gellert, M. V(D)J recombination: RAG proteins, repair factors, and regulation. Annu. Rev. Biochem. 71, 101-132 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 101-132
    • Gellert, M.1
  • 13
    • 0026792892 scopus 로고
    • V(D)J recombination: Broken DNA molecules with covalently sealed (hairpin) coding ends in SCID mouse thymoctes
    • Roth, D. B., Menetski, J. P., Nakajima, P. B., Bosma, M. J. & Gellert, M, V(D)J recombination: broken DNA molecules with covalently sealed (hairpin) coding ends in SCID mouse thymoctes. Cell 70, 983-991 (1992).
    • (1992) Cell , vol.70 , pp. 983-991
    • Roth, D.B.1    Menetski, J.P.2    Nakajima, P.B.3    Bosma, M.J.4    Gellert, M.5
  • 14
    • 0031848525 scopus 로고    scopus 로고
    • Tfol: An Ac-like transposon from the plant pathogenic fungus Fusarium oxysporum
    • Okuda, M., Ikeda, K., Namiki, E., Nishi, K. & Tsuge, T. Tfol: an Ac-like transposon from the plant pathogenic fungus Fusarium oxysporum. Mol Gen. Genet. 258, 599-607 (1998).
    • (1998) Mol Gen. Genet. , vol.258 , pp. 599-607
    • Okuda, M.1    Ikeda, K.2    Namiki, E.3    Nishi, K.4    Tsuge, T.5
  • 15
    • 0030871750 scopus 로고    scopus 로고
    • The Hermes element from Musca domestica can transpose in four families of cyclorrhaphan flies
    • Sarkar, A. et al. The Hermes element from Musca domestica can transpose in four families of cyclorrhaphan flies. Genetics 99, 15-29 (1997).
    • (1997) Genetics , vol.99 , pp. 15-29
    • Sarkar, A.1
  • 16
    • 0032475879 scopus 로고    scopus 로고
    • Tn10 transposition via a DNA hairpin intermediate
    • Kennedy, A., Guhathakurta, A., Kleckner, N. & Haniford, D. B. Tn10 transposition via a DNA hairpin intermediate. Cell 95, 125-134 (1998).
    • (1998) Cell , vol.95 , pp. 125-134
    • Kennedy, A.1    Guhathakurta, A.2    Kleckner, N.3    Haniford, D.B.4
  • 17
  • 18
    • 0032555758 scopus 로고    scopus 로고
    • DNA transposition by the RAG1 and RAG2 proteins: A possible source of oncogenic translocations
    • Hiom, K., Melek, M. & Gellert, M. DNA transposition by the RAG1 and RAG2 proteins: a possible source of oncogenic translocations. Cell 94, 463-470 (1998).
    • (1998) Cell , vol.94 , pp. 463-470
    • Hiom, K.1    Melek, M.2    Gellert, M.3
  • 19
    • 0032551829 scopus 로고    scopus 로고
    • Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system
    • Agrawal, A., Eastman, O. M. & Schatz, D. G. Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system. Nature 394, 744-751 (1998).
    • (1998) Nature , vol.394 , pp. 744-751
    • Agrawal, A.1    Eastman, O.M.2    Schatz, D.G.3
  • 20
    • 0029967722 scopus 로고    scopus 로고
    • Similarities between initiation of V(D)J recombination and retroviral integration
    • van Gent, D. C., Mizuuchi, K. & Gellert, M. Similarities between initiation of V(D)J recombination and retroviral integration. Science 271, 1592-1594 (1996).
    • (1996) Science , vol.271 , pp. 1592-1594
    • Van Gent, D.C.1    Mizuuchi, K.2    Gellert, M.3
  • 21
    • 0034724557 scopus 로고    scopus 로고
    • Single active site catalysis of the successive phosphoryl transfer steps by DNA transposases: Insights from phosphorothioate stereoselectivity
    • Kennedy, A. K., Haniford, D. B. & Mizuuchi, K. Single active site catalysis of the successive phosphoryl transfer steps by DNA transposases: insights from phosphorothioate stereoselectivity. Cell 101, 295-305 (2000).
    • (2000) Cell , vol.101 , pp. 295-305
    • Kennedy, A.K.1    Haniford, D.B.2    Mizuuchi, K.3
  • 22
    • 0025899314 scopus 로고
    • Inversion of the phosphate chirality at the target site of the Mu DNA strand transfer: Evidence for a one-step transesterification mechanism
    • Mizuuchi, K. & Adzuma, K. Inversion of the phosphate chirality at the target site of the Mu DNA strand transfer: evidence for a one-step transesterification mechanism. Cell 66, 129-140 (1991).
    • (1991) Cell , vol.66 , pp. 129-140
    • Mizuuchi, K.1    Adzuma, K.2
  • 23
    • 0141958834 scopus 로고    scopus 로고
    • The C-terminus of the Hermes transposase contains a protein multimerization domain
    • Michel, K., O'Brochta. D. A. & Atkinson, P. W. The C-terminus of the Hermes transposase contains a protein multimerization domain. Insect Biochem. Mol. Biol. 33, 959-970 (2003).
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 959-970
    • Michel, K.1    O'Brochta, D.A.2    Atkinson, P.W.3
  • 24
    • 0032125708 scopus 로고    scopus 로고
    • The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition
    • Namgoong, S. & Harshey, R. The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition. EMBO J. 17, 3775-3785 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3775-3785
    • Namgoong, S.1    Harshey, R.2
  • 25
    • 0033569428 scopus 로고    scopus 로고
    • Orginization and dynamics of the Mu transpososome: Recombination by communication between two active sites
    • Williams, T. L., Jackson, E. L., Carritte, A. & Baker, T. A. Orginization and dynamics of the Mu transpososome: recombination by communication between two active sites. Genes Dev. 13, 2725-2737 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2725-2737
    • Williams, T.L.1    Jackson, E.L.2    Carritte, A.3    Baker, T.A.4
  • 26
    • 0023056233 scopus 로고
    • Transposable elements generate novel spatial patterns of gene expression in Antirrhinum majus
    • Coen, E. S., Carpenter, R. & Martin, C. Transposable elements generate novel spatial patterns of gene expression in Antirrhinum majus. Cell 47, 285-296 (1986).
    • (1986) Cell , vol.47 , pp. 285-296
    • Coen, E.S.1    Carpenter, R.2    Martin, C.3
  • 27
    • 0033780451 scopus 로고    scopus 로고
    • Transposition of maize Ac/Ds transposable elements in the yeast Saccharomyces cerevisiae
    • Weil, C. F. & Kunze, R. Transposition of maize Ac/Ds transposable elements in the yeast Saccharomyces cerevisiae. Nature Genet. 26, 187-190 (2000).
    • (2000) Nature Genet. , vol.26 , pp. 187-190
    • Weil, C.F.1    Kunze, R.2
  • 28
    • 0037155703 scopus 로고    scopus 로고
    • Hairpin opening and overhang processing by an Artemis/DNA-dependent protein, kinase complex in nonhomologous end joining and V(D)J recombination
    • Ma, Y., Pannicke, U., Schwarz, K. & Lieber, M. R. Hairpin opening and overhang processing by an Artemis/DNA-dependent protein, kinase complex in nonhomologous end joining and V(D)J recombination. Cell 108, 781-794 (2002).
    • (2002) Cell , vol.108 , pp. 781-794
    • Ma, Y.1    Pannicke, U.2    Schwarz, K.3    Lieber, M.R.4
  • 29
    • 1642458360 scopus 로고    scopus 로고
    • Microhomology-dependent end joining and repair of transposon-induced DNA hairpins by host factors in Saccharomyces cerevisiae
    • Yu, J., Marshall, K., Yamaguchi, M., Haber, J. E. & Weil, C. F. Microhomology-dependent end joining and repair of transposon-induced DNA hairpins by host factors in Saccharomyces cerevisiae. Mol. Cell. Biol 24, 1351-1364 (2004).
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1351-1364
    • Yu, J.1    Marshall, K.2    Yamaguchi, M.3    Haber, J.E.4    Weil, C.F.5
  • 30
    • 0035108439 scopus 로고    scopus 로고
    • Separation-of-function mutants reveal critical roles for RAG2 in both the cleavage and joining steps of V(D)J recombination
    • Qiu, I. X., Kale, S. B., Yarnell, S. H. & Roth, D. B. Separation-of-function mutants reveal critical roles for RAG2 in both the cleavage and joining steps of V(D)J recombination. Mol. Cell 7, 77-87 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 77-87
    • Qiu, I.X.1    Kale, S.B.2    Yarnell, S.H.3    Roth, D.B.4
  • 31
    • 1942421722 scopus 로고    scopus 로고
    • RAG proteins shepherd double-strand breaks to a specific pathway, suppressing error-prone repair, but RAG nicking initiates homologous recombination
    • Lee, G., Neiditch, M., Salus, S. & Roth, D. RAG proteins shepherd double-strand breaks to a specific pathway, suppressing error-prone repair, but RAG nicking initiates homologous recombination. Cell 117, 171-184 (2004).
    • (2004) Cell , vol.117 , pp. 171-184
    • Lee, G.1    Neiditch, M.2    Salus, S.3    Roth, D.4
  • 32
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choke
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choke. Nucleic Acids Res. 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 33
    • 0029858349 scopus 로고    scopus 로고
    • The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products
    • Sarnovsky, R., May, E. W. & Craig, N. L. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 15, 6348-6361 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6348-6361
    • Sarnovsky, R.1    May, E.W.2    Craig, N.L.3
  • 34
    • 0027398505 scopus 로고
    • Metal ion catalysis in the Tetrahymena ribozyme reaction
    • Piccirilli, J. A., Vyie, J. S., Caruthers, M. H. & Cech, T. R. Metal ion catalysis in the Tetrahymena ribozyme reaction. Nature 361, 85-88 (1993).
    • (1993) Nature , vol.361 , pp. 85-88
    • Piccirilli, J.A.1    Vyie, J.S.2    Caruthers, M.H.3    Cech, T.R.4
  • 35
    • 0033603053 scopus 로고    scopus 로고
    • All three residues of the Tn10 transposase DDE catalytic triad function in divalent metal ion binding
    • Allingham, J., Pribil, P. & Haniford, D. All three residues of the Tn10 transposase DDE catalytic triad function in divalent metal ion binding. J. Mol. Biol. 289, 1195-1206 (1999).
    • (1999) J. Mol. Biol. , vol.289 , pp. 1195-1206
    • Allingham, J.1    Pribil, P.2    Haniford, D.3
  • 36
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam, C. & Steitz, T. Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr. Opin. Struct. Biol. 8, 54-63 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 54-63
    • Brautigam, C.1    Steitz, T.2
  • 37
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HEV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda, E et al. Crystal structure of the catalytic domain of HEV-1 integrase: similarity to other polynucleotidyl transferases. Science 266, 1981-1986 (1994).
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, E.1
  • 38
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. I., Bryson, K. & Jones, D. T. The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405 (2000).
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.I.1    Bryson, K.2    Jones, D.T.3
  • 39
    • 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. & Octtinger, M. A. Mutations of acidic residues in RAG1 define the active site of the V(D)J recombinase. Genes Dev, 13, 3070-3080 (1999).
    • (1999) Genes Dev , vol.13 , pp. 3070-3080
    • Kim, D.R.1    Dai, Y.2    Mundy, C.L.3    Yang, W.4    Octtinger, M.A.5
  • 40
    • 0033954892 scopus 로고    scopus 로고
    • Identification of two catalytic residues in RAG1 that define 2 single active site within the RAG1/RAG2 protein complex
    • Fugmann, S. D., Villey, I. J., Ptaszek, L. M. & Schatz, D. G. Identification of two catalytic residues in RAG1 that define 2 single active site within the RAG1/RAG2 protein complex. Mol Cell 5, 97-107 (2000).
    • (2000) Mol Cell , vol.5 , pp. 97-107
    • Fugmann, S.D.1    Villey, I.J.2    Ptaszek, L.M.3    Schatz, D.G.4
  • 41
    • 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
    • Landrec, M. A., Wibbenmeyer, J. A. & 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, 3059-3069 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 3059-3069
    • Landrec, M.A.1    Wibbenmeyer, J.A.2    Roth, D.B.3
  • 42
    • 0003873979 scopus 로고    scopus 로고
    • (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A.) (ASM, Washington DC)
    • Walbot, V in Mobile DNA II (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A.) 533-563 (ASM, Washington DC, 2002).
    • (2002) Mobile DNA II , pp. 533-563
    • Walbot, V.1
  • 43
    • 0344442909 scopus 로고    scopus 로고
    • Molecular evolutionary analysis of the widespread piggyBac transposon family and related "domesticated" sequences
    • Sarkar, A. et al. Molecular evolutionary analysis of the widespread piggyBac transposon family and related "domesticated" sequences. Mol Genet. Genom. 270, 173-180 (2003).
    • (2003) Mol Genet. Genom. , vol.270 , pp. 173-180
    • Sarkar, A.1
  • 45
    • 0033597135 scopus 로고    scopus 로고
    • The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9 Å resolution
    • Davies, D. R., Braam, L. M., Reznikoff, W. S. & Rayment, I. The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9 Å resolution. J. Biol Chem. 274, 11904-11913 (1999).
    • (1999) J. Biol Chem. , vol.274 , pp. 11904-11913
    • Davies, D.R.1    Braam, L.M.2    Reznikoff, W.S.3    Rayment, I.4
  • 46
    • 0037192801 scopus 로고    scopus 로고
    • Mutational analysis of the base flipping event found in Tn5 transposition
    • Ason, B. & Reznikoff, W. S. Mutational analysis of the base flipping event found in Tn5 transposition. J. Biol Chem. 277, 11284-11291 (2002).
    • (2002) J. Biol Chem. , vol.277 , pp. 11284-11291
    • Ason, B.1    Reznikoff, W.S.2
  • 47
    • 0036240040 scopus 로고    scopus 로고
    • Mutational analysis of all conserved basic amino acids in RAG-1 reveals catalytic, step arrest, and joining-deficient mutants in the V(D)J recombinase
    • Huye, L. E., Purugganan, M. M., Jiang, M. M. & Roth, D. B. Mutational analysis of all conserved basic amino acids in RAG-1 reveals catalytic, step arrest, and joining-deficient mutants in the V(D)J recombinase. Mol Cell. Biol. 22, 3460-3473 (2002).
    • (2002) Mol Cell. Biol. , vol.22 , pp. 3460-3473
    • Huye, L.E.1    Purugganan, M.M.2    Jiang, M.M.3    Roth, D.B.4
  • 48
    • 4644325594 scopus 로고    scopus 로고
    • Mixing active-site components: A recipe for the unique enzymatic activity of a telomere resolvase
    • Bankhead, T. & Chaconas, G. Mixing active-site components: a recipe for the unique enzymatic activity of a telomere resolvase. Proc. Natl Acad. Sci. USA 101, 13768-13773 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13768-13773
    • Bankhead, T.1    Chaconas, G.2
  • 49
    • 3242877122 scopus 로고    scopus 로고
    • Putting the pieces together: Identification and characterization of structural domains in the V(D)J recombination protein RAG1
    • De, P. & Rodgers, K. Putting the pieces together: identification and characterization of structural domains in the V(D)J recombination protein RAG1. Immunol Rev. 200, 70-82 (2004).
    • (2004) Immunol Rev. , vol.200 , pp. 70-82
    • De, P.1    Rodgers, K.2
  • 50
    • 0344936724 scopus 로고    scopus 로고
    • The origins of V(D)J recombination
    • Lewis, S. M. & Wu, G. E. The origins of V(D)J recombination. Cell 88, 159-162 (1997).
    • (1997) Cell , vol.88 , pp. 159-162
    • Lewis, S.M.1    Wu, G.E.2


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