메뉴 건너뛰기




Volumn 53, Issue , 1999, Pages 245-281

Integrating DNA: Transposases and retroviral integrases

Author keywords

Insertion sequences; Structure; Transposition mechanism; Transposons

Indexed keywords

INTEGRASE; TRANSPOSASE; VIRUS DNA;

EID: 0032723359     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.53.1.245     Document Type: Review
Times cited : (211)

References (185)
  • 1
    • 0025911364 scopus 로고
    • Steady-state kinetic analysis of ATP hydrolysis by the B protein of bacteriophage mu. Involvement of protein oligomerization in the ATPase cycle
    • Adzuma K, Mizuuchi K. 1991. Steady-state kinetic analysis of ATP hydrolysis by the B protein of bacteriophage mu. Involvement of protein oligomerization in the ATPase cycle. J. Biol. Chem. 266:6159-67
    • (1991) J. Biol. Chem. , vol.266 , pp. 6159-6167
    • Adzuma, K.1    Mizuuchi, K.2
  • 2
    • 0032551829 scopus 로고    scopus 로고
    • Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system
    • Agrawal A, Eastman QM, Schatz DG. 1998. Transposition mediated by RAG1 and RAG2 and its implications for the evolution of the immune system. Nature. 394:744-51
    • (1998) Nature , vol.394 , pp. 744-751
    • Agrawal, A.1    Eastman, Q.M.2    Schatz, D.G.3
  • 3
    • 0029871975 scopus 로고    scopus 로고
    • The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis
    • Aldaz H, Schuster E, Baker TA. 1996. The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis. Cell 85:257-69
    • (1996) Cell , vol.85 , pp. 257-269
    • Aldaz, H.1    Schuster, E.2    Baker, T.A.3
  • 4
    • 0028863151 scopus 로고
    • Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase
    • Andrake MD, Skalka AM. 1995. Multimerization determinants reside in both the catalytic core and C terminus of avian sarcoma virus integrase. J. Biol. Chem. 270:29299-306
    • (1995) J. Biol. Chem. , vol.270 , pp. 29299-29306
    • Andrake, M.D.1    Skalka, A.M.2
  • 5
    • 0029814410 scopus 로고    scopus 로고
    • Retroviral integrase, putting the pieces together
    • Andrake MD, Skalka AM. 1996. Retroviral integrase, putting the pieces together. J. Biol. Chem. 271:19633-36
    • (1996) J. Biol. Chem. , vol.271 , pp. 19633-19636
    • Andrake, M.D.1    Skalka, A.M.2
  • 6
    • 0025836710 scopus 로고
    • Purification of TnsB, a transposition protein that binds to the ends of Tn7
    • Arciszewska LK, McKown RL, Craig NL. 1991. Purification of TnsB, a transposition protein that binds to the ends of Tn7. J. Biol. Chem. 266:21736-44
    • (1991) J. Biol. Chem. , vol.266 , pp. 21736-21744
    • Arciszewska, L.K.1    McKown, R.L.2    Craig, N.L.3
  • 7
    • 0030922072 scopus 로고    scopus 로고
    • A metal-induced conformational change and activation of HIV-1 integrase
    • Asante-Appiah E, Skalka AM. 1997. A metal-induced conformational change and activation of HIV-1 integrase, J. Biol. Chem. 272:16196-205
    • (1997) J. Biol. Chem. , vol.272 , pp. 16196-16205
    • Asante-Appiah, E.1    Skalka, A.M.2
  • 8
    • 0027491030 scopus 로고
    • The hobo transposable element of Drosophila can be cross-mobilized in houseflies and excises like the Ac element of maize
    • Atkinson PW, Warren WD, O'Brochta DA. 1993. The hobo transposable element of Drosophila can be cross-mobilized in houseflies and excises like the Ac element of maize. Proc. Natl. Acad. Sci. USA 90:9693-97
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9693-9697
    • Atkinson, P.W.1    Warren, W.D.2    O'Brochta, D.A.3
  • 9
    • 0025872684 scopus 로고
    • Tn7 transposition in vitro proceeds through an excised transposon intermediate generated by staggered breaks in DNA
    • Bainton R, Gamas P, Craig NL. 1991. Tn7 transposition in vitro proceeds through an excised transposon intermediate generated by staggered breaks in DNA. Cell 65:805-16
    • (1991) Cell , vol.65 , pp. 805-816
    • Bainton, R.1    Gamas, P.2    Craig, N.L.3
  • 10
    • 0028317055 scopus 로고
    • Identification of residues in the Mu transposase essential for catalysis
    • Baker TA, Luo L. 1994. Identification of residues in the Mu transposase essential for catalysis. Proc. Natl. Acad. Sci. USA 91:6654-58
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6654-6658
    • Baker, T.A.1    Luo, L.2
  • 11
    • 0026458080 scopus 로고
    • DNA-promoted assembly of the active tetramer of the Mu transposase
    • Baker TA, Mizuuchi K. 1992. DNA-promoted assembly of the active tetramer of the Mu transposase. Genes Dev. 6:2221-32
    • (1992) Genes Dev. , vol.6 , pp. 2221-2232
    • Baker, T.A.1    Mizuuchi, K.2
  • 12
    • 0025794342 scopus 로고
    • MuB protein allosterically activates strand transfer by the transposase of phage Mu
    • Baker TA, Mizuuchi M, Mizuuchi K. 1991. MuB protein allosterically activates strand transfer by the transposase of phage Mu. Cell 65:1003-13
    • (1991) Cell , vol.65 , pp. 1003-1013
    • Baker, T.A.1    Mizuuchi, M.2    Mizuuchi, K.3
  • 13
    • 0030847553 scopus 로고    scopus 로고
    • Drosophila P-element transposase is a novel site-specific endonuclease
    • Beall EL, Rio DC. 1997. Drosophila P-element transposase is a novel site-specific endonuclease. Genes Dev. 11:2137-51
    • (1997) Genes Dev. , vol.11 , pp. 2137-2151
    • Beall, E.L.1    Rio, D.C.2
  • 14
    • 0032055477 scopus 로고    scopus 로고
    • Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro
    • Beall EL, Rio DC. 1998. Transposase makes critical contacts with, and is stimulated by, single-stranded DNA at the P element termini in vitro. EMBO J. 17:2122-36
    • (1998) EMBO J. , vol.17 , pp. 2122-2136
    • Beall, E.L.1    Rio, D.C.2
  • 15
    • 0030892130 scopus 로고    scopus 로고
    • Maize activator transposase has a bipartile DNA binding domain that recognizes subterminal sequences and the terminal inverted repeats
    • Becker HA, Kunze R. 1997. Maize activator transposase has a bipartile DNA binding domain that recognizes subterminal sequences and the terminal inverted repeats. Mol. Gen. Genet. 254:219-30
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 219-230
    • Becker, H.A.1    Kunze, R.2
  • 16
    • 0004224917 scopus 로고
    • Washington, DC: Am. Soc. Microbiol.
    • Berg DE, Howe MM. 1989. Mobile DNA. Washington, DC: Am. Soc. Microbiol.
    • (1989) Mobile DNA
    • Berg, D.E.1    Howe, M.M.2
  • 17
    • 0029166229 scopus 로고
    • The two single-strand cleavages at each end of Tn10 occur in a specific order during transposition
    • Bolland S, Kleckner N. 1995. The two single-strand cleavages at each end of Tn10 occur in a specific order during transposition. Proc. Natl. Acad. Sci. USA 92:7814-18
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7814-7818
    • Bolland, S.1    Kleckner, N.2
  • 18
    • 0030050236 scopus 로고    scopus 로고
    • The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site
    • Bolland S, Kleckner N. 1996. The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site. Cell 84:223-33
    • (1996) Cell , vol.84 , pp. 223-233
    • Bolland, S.1    Kleckner, N.2
  • 19
    • 0008179472 scopus 로고    scopus 로고
    • Functional characterization of the Tn5 transposase by limited proteolysis
    • Braam LA, Reznikoff WS. 1998. Functional characterization of the Tn5 transposase by limited proteolysis. J. Biol. Chem. 273:10908-13
    • (1998) J. Biol. Chem. , vol.273 , pp. 10908-10913
    • Braam, L.A.1    Reznikoff, W.S.2
  • 20
    • 0001363865 scopus 로고    scopus 로고
    • ed. JM Coffin, SH Hughes, HE Varmus, Plainview, NY: Cold Spring Harbor Lab. Press
    • Brown PO. 1997. Integration, Retro-viruses, ed. JM Coffin, SH Hughes, HE Varmus, pp. 161-203. Plainview, NY: Cold Spring Harbor Lab. Press
    • (1997) Integration, Retro-Viruses , pp. 161-203
    • Brown, P.O.1
  • 21
    • 0030566832 scopus 로고    scopus 로고
    • The catalytic domain of human immunodeficiency virus integrase: Ordered active site in the F185H mutant
    • Bujacz G, Alexandratos J, Qing ZL, Clement-Mella C, Wlodawer A. 1996. The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant. FEBS Lett. 398:175-78
    • (1996) FEBS Lett. , vol.398 , pp. 175-178
    • Bujacz, G.1    Alexandratos, J.2    Qing, Z.L.3    Clement-Mella, C.4    Wlodawer, A.5
  • 22
    • 0030746054 scopus 로고    scopus 로고
    • Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity
    • Bujacz G, Alexandratos J, Wlodawer A, Merkel G, Andrake M, et al. 1997. Binding of different divalent cations to the active site of avian sarcoma virus integrase and their effects on enzymatic activity. J. Biol. Chem. 272:18161-68
    • (1997) J. Biol. Chem. , vol.272 , pp. 18161-18168
    • Bujacz, G.1    Alexandratos, J.2    Wlodawer, A.3    Merkel, G.4    Andrake, M.5
  • 23
    • 0028865574 scopus 로고
    • High-resolution structure of the catalytic domain of avian sarcoma virus integrase
    • Bujacz G, Jaskolski M, Alexandratos J, Wlodawer A, Merkel G, et al. 1995. High-resolution structure of the catalytic domain of avian sarcoma virus integrase. J. Mol. Biol. 253:333-46
    • (1995) J. Mol. Biol. , vol.253 , pp. 333-346
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5
  • 24
    • 0029643858 scopus 로고    scopus 로고
    • The catalytic domain of avian sarcoma virus integrase: Conformation of the active-site residues in the presence of divalent cations
    • Bujacz G, Jaskolski M, Alexandratos J, Wlodawer A, Merkel G, et al. 1996. The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure 4:89-96
    • (1996) Structure , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5
  • 25
    • 0027456715 scopus 로고
    • Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding
    • Bushman FD, Engelman A, Palmer I, Wingfield P, Craigie R. 1993. Domains of the integrase protein of human immunodeficiency virus type 1 responsible for polynucleotidyl transfer and zinc binding. Proc. Natl. Acad. Sci. USA 90:3428-32
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3428-3432
    • Bushman, F.D.1    Engelman, A.2    Palmer, I.3    Wingfield, P.4    Craigie, R.5
  • 27
    • 0030199188 scopus 로고    scopus 로고
    • DNA transposition: Jumping gene machine, some assembly required
    • Chaconas G, Lavoie BD, Watson MA. 1996. DNA transposition: jumping gene machine, some assembly required. Curr. Biol. 6:817-20
    • (1996) Curr. Biol. , vol.6 , pp. 817-820
    • Chaconas, G.1    Lavoie, B.D.2    Watson, M.A.3
  • 28
    • 0032577448 scopus 로고    scopus 로고
    • IHF modulation of Tn10 transposition: Sensory transduction of supercoiling status via a proposed protein/DNA molecular spring
    • Chalmers R, Guhathakurta A, Benjamin H, Kleckner N. 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
  • 29
    • 0028239766 scopus 로고
    • Tn10/IS10 transposase purification, activation, and in vitro reaction
    • Chalmers RM, Kleckner N. 1994. Tn10/IS10 transposase purification, activation, and in vitro reaction. J. Biol. Chem. 269:8029-35
    • (1994) J. Biol. Chem. , vol.269 , pp. 8029-8035
    • Chalmers, R.M.1    Kleckner, N.2
  • 30
    • 0026549933 scopus 로고
    • Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus
    • Chow SA, Vincent KA, Ellison V, Brown PO. 1992. Reversal of integration and DNA splicing mediated by integrase of human immunodeficiency virus. Science 255:723-26
    • (1992) Science , vol.255 , pp. 723-726
    • Chow, S.A.1    Vincent, K.A.2    Ellison, V.3    Brown, P.O.4
  • 31
    • 0031576325 scopus 로고    scopus 로고
    • Solution structure of the 1γ subdomain of the Mu end DNA-binding domain of phage Mu transposase
    • Clubb RT, Schumacher S, Mizuuchi K, Gronenborn AM, Cloro GM. 1997. Solution structure of the 1γ subdomain of the Mu end DNA-binding domain of phage Mu transposase. J. Mol. Biol. 273:19-25
    • (1997) J. Mol. Biol. , vol.273 , pp. 19-25
    • Clubb, R.T.1    Schumacher, S.2    Mizuuchi, K.3    Gronenborn, A.M.4    Cloro, G.M.5
  • 32
    • 0003100670 scopus 로고
    • Consequences and mechanisms of transposition in Antirrhinum majus
    • ed. D Berg, M Howe, Washington, DC: Am. Soc. Microbiol.
    • Coen ES, Robbins TP, Almcida J, Hudson A, Carpenter R, 1989. Consequences and mechanisms of transposition in Antirrhinum majus. In Mobile DNA, ed. D Berg, M Howe, pp. 413-36. Washington, DC: Am. Soc. Microbiol.
    • (1989) Mobile DNA , pp. 413-436
    • Coen, E.S.1    Robbins, T.P.2    Almcida, J.3    Hudson, A.4    Carpenter, R.5
  • 33
    • 0031860891 scopus 로고    scopus 로고
    • Extensive, nonrandom diversity of excision footprints generated by Ds-like transposon Ascot-1 suggests new parallels with V(D)J recombination
    • Colot V, Hacdens V, Rossignol JL. 1998. Extensive, nonrandom diversity of excision footprints generated by Ds-like transposon Ascot-1 suggests new parallels with V(D)J recombination. Mol. Cell Biol. 18:4337-46
    • (1998) Mol. Cell Biol. , vol.18 , pp. 4337-4346
    • Colot, V.1    Hacdens, V.2    Rossignol, J.L.3
  • 35
    • 0023646797 scopus 로고
    • Transposition of Mu DNA: Joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu
    • Craigie R, Mizuuchi K. 1987. Transposition of Mu DNA: joining of Mu to target DNA can be uncoupled from cleavage at the ends of Mu. Cell 51:493-501
    • (1987) Cell , vol.51 , pp. 493-501
    • Craigie, R.1    Mizuuchi, K.2
  • 36
    • 0021676867 scopus 로고
    • Site-specific recognition of the bacterio-phage Mu ends by the Mu A protein
    • Craigie R, Mizuuchi M, Mizuuchi K. 1984. Site-specific recognition of the bacterio-phage Mu ends by the Mu A protein. Cell 39:387-94
    • (1984) Cell , vol.39 , pp. 387-394
    • Craigie, R.1    Mizuuchi, M.2    Mizuuchi, K.3
  • 37
    • 0025998488 scopus 로고
    • Role of divalent metal ions in the hammer-head RNA cleavage reaction
    • Dahm SC, Uhlenbeck OC. 1991. Role of divalent metal ions in the hammer-head RNA cleavage reaction. Biochemistry 30:9464-69
    • (1991) Biochemistry , vol.30 , pp. 9464-9469
    • Dahm, S.C.1    Uhlenbeck, O.C.2
  • 38
    • 0033597135 scopus 로고    scopus 로고
    • Three dimensional structure of a Tu5-related protein determined to 2.9 Å resolution
    • Davies DR, Braam LM, Reznikoff WS, Rayment I. 1999. Three dimensional structure of a Tu5-related protein determined to 2.9 Å resolution. J. Biol. Chem. 274:11904-13
    • (1999) J. Biol. Chem. , vol.274 , pp. 11904-11913
    • Davies, D.R.1    Braam, L.M.2    Reznikoff, W.S.3    Rayment, I.4
  • 39
    • 0028053230 scopus 로고
    • A proposed superfamily of transposase genes: Transposon-like elements in ciliated protozoa and a common "D35E" motif
    • Doak TG, Docrder FP, Jahn CL, Herrick G. 1994. A proposed superfamily of transposase genes: transposon-like elements in ciliated protozoa and a common "D35E" motif. Proc. Natl. Acad. Sci. USA 91:942-46
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 942-946
    • Doak, T.G.1    Docrder, F.P.2    Jahn, C.L.3    Herrick, G.4
  • 40
    • 0027272791 scopus 로고
    • Conserved residues Pro-109 and Asp-116 are required for interaction of the human immunodeficiency virus type 1 integrase protein with its viral DNA substrate
    • Drelich M, Haenggi M, Mous J. 1993. Conserved residues Pro-109 and Asp-116 are required for interaction of the human immunodeficiency virus type 1 integrase protein with its viral DNA substrate. J. Virol. 67:5041-44
    • (1993) J. Virol. , vol.67 , pp. 5041-5044
    • Drelich, M.1    Haenggi, M.2    Mous, J.3
  • 41
    • 0026740842 scopus 로고
    • Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro
    • Drelich M, Wilhelm R, Mous J. 1992. Identification of amino acid residues critical for endonuclease and integration activities of HIV-1 IN protein in vitro, Virology 188:459-68
    • (1992) Virology , vol.188 , pp. 459-468
    • Drelich, M.1    Wilhelm, R.2    Mous, J.3
  • 42
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda F, Hickman AB, Jenkins TM, Engelman A, Craigie R, Davies DR. 1994. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 266:1981-86
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 44
    • 0031260521 scopus 로고    scopus 로고
    • The solution structure of the amino-terminal HHCC domain of HIV-2 integrase: A three-helix bundle stabilized by zinc
    • Eijkelenboom AP, van den Ent FM, Vos A, Doreleijers JF, Hard K, et al. 1997. The solution structure of the amino-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc. Curr. Biol. 7:739-46
    • (1997) Curr. Biol. , vol.7 , pp. 739-746
    • Eijkelenboom, A.P.1    Van den Ent, F.M.2    Vos, A.3    Doreleijers, J.F.4    Hard, K.5
  • 45
    • 0028239062 scopus 로고
    • A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro
    • Ellison V, Brown PO. 1994. A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro. Proc. Natl. Acad. Sci. USA 91:7316-20
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7316-7320
    • Ellison, V.1    Brown, P.O.2
  • 46
    • 0028888455 scopus 로고
    • An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer
    • Ellison V, Gerton J, Vincent KA, Brown PO. 1995, An essential interaction between distinct domains of HIV-1 integrase mediates assembly of the active multimer. J. Biol. Chem. 270:3320-26
    • (1995) J. Biol. Chem. , vol.270 , pp. 3320-3326
    • Ellison, V.1    Gerton, J.2    Vincent, K.A.3    Brown, P.O.4
  • 47
    • 0027179694 scopus 로고
    • Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex
    • Engelman A, Bushman FD, Craigie R. 1993. Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex. EMBO J. 12:3269-75
    • (1993) EMBO J. , vol.12 , pp. 3269-3275
    • Engelman, A.1    Bushman, F.D.2    Craigie, R.3
  • 48
    • 0026649557 scopus 로고
    • Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro
    • Engelman A, Craigie R. 1992, Identification of conserved amino acid residues critical for human immunodeficiency virus type 1 integrase function in vitro. J. Virol. 66:6361-69
    • (1992) J. Virol. , vol.66 , pp. 6361-6369
    • Engelman, A.1    Craigie, R.2
  • 49
    • 0028067324 scopus 로고
    • The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding
    • Engelman A, Hickman AB, Craigie R. 1994. The core and carboxyl-terminal domains of the integrase protein of human immunodeficiency virus type 1 each contribute to nonspecific DNA binding. J. Virol. 68:5911-17
    • (1994) J. Virol. , vol.68 , pp. 5911-5917
    • Engelman, A.1    Hickman, A.B.2    Craigie, R.3
  • 50
    • 0026330796 scopus 로고
    • HIV-1 DNA integration: Mechanism of viral DNA cleavage and DNA strand transfer
    • Engelman A, Mizuuchi K, Craigic R. 1991. HIV-1 DNA integration: mechanism of viral DNA cleavage and DNA strand transfer. Cell 67:1211-21
    • (1991) Cell , vol.67 , pp. 1211-1221
    • Engelman, A.1    Mizuuchi, K.2    Craigic, R.3
  • 52
    • 0025103072 scopus 로고
    • High-frequeney P element loss in Drosophila is homolog dependent
    • Engels WR, Johnson-Schlitz DM, Eggleston WB, Sved J. 1990. High-frequeney P element loss in Drosophila is homolog dependent. Cell 62:515-25
    • (1990) Cell , vol.62 , pp. 515-525
    • Engels, W.R.1    Johnson-Schlitz, D.M.2    Eggleston, W.B.3    Sved, J.4
  • 53
    • 0032189652 scopus 로고    scopus 로고
    • Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction
    • Esposito D, Craigie R. 1998. Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction. EMBO J. 17:5832-43
    • (1998) EMBO J. , vol.17 , pp. 5832-5843
    • Esposito, D.1    Craigie, R.2
  • 54
    • 0031004162 scopus 로고    scopus 로고
    • HIV-1 cDNA integration: Requirement of HMG I(Y) protein for function of preintegration complexes in vitro
    • Farnet CM, Bushman FD. 1997. HIV-1 cDNA integration: requirement of HMG I(Y) protein for function of preintegration complexes in vitro. Cell 88:483-92
    • (1997) Cell , vol.88 , pp. 483-492
    • Farnet, C.M.1    Bushman, F.D.2
  • 55
    • 0025053617 scopus 로고
    • Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences?
    • Fayet O, Ramond P, Polard P, Prere MF, Chandler M. 1990. Functional similarities between retroviruses and the IS3 family of bacterial insertion sequences? Mol. Microbiol. 4:1771-77
    • (1990) Mol. Microbiol. , vol.4 , pp. 1771-1777
    • Fayet, O.1    Ramond, P.2    Polard, P.3    Prere, M.F.4    Chandler, M.5
  • 57
    • 0031949592 scopus 로고    scopus 로고
    • Effects of mutations in residues near the active site of human immunodeficiency virus type 1 integrase on specific enzyme-substrate interactions
    • Gerton JL, Ohgi S, Olsen M, DeRisi J, Brown PO. 1998. Effects of mutations in residues near the active site of human immunodeficiency virus type 1 integrase on specific enzyme-substrate interactions. J. Virol. 72:5046-55
    • (1998) J. Virol. , vol.72 , pp. 5046-5055
    • Gerton, J.L.1    Ohgi, S.2    Olsen, M.3    DeRisi, J.4    Brown, P.O.5
  • 58
    • 0029655365 scopus 로고    scopus 로고
    • The En/Spm transposable element of maize
    • Gierl A. 1996. The En/Spm transposable element of maize. Curr. Top. Microbiol. Immunol. 204:145-59
    • (1996) Curr. Top. Microbiol. Immunol. , vol.204 , pp. 145-159
    • Gierl, A.1
  • 60
    • 0032528271 scopus 로고    scopus 로고
    • Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination
    • Gopaul DN, Guo F, Van DG. 1998. Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination. EMBO J. 17:4175-87
    • (1998) EMBO J. , vol.17 , pp. 4175-4187
    • Gopaul, D.N.1    Guo, F.2    Van, D.G.3
  • 62
    • 0029609126 scopus 로고
    • DNA transposition: From a black box to a color monitor
    • Grindley ND, Leschziner AE. 1995. DNA transposition: from a black box to a color monitor. Cell 83:1063-66
    • (1995) Cell , vol.83 , pp. 1063-1066
    • Grindley, N.D.1    Leschziner, A.E.2
  • 63
    • 0027452696 scopus 로고
    • Tn7 transposition creates a hotspot for homologous recombination at the transposon donor site
    • Hagemann AT, Craig NL. 1993. Tn7 transposition creates a hotspot for homologous recombination at the transposon donor site. Genetics 133:9-16
    • (1993) Genetics , vol.133 , pp. 9-16
    • Hagemann, A.T.1    Craig, N.L.2
  • 64
    • 0025964138 scopus 로고
    • Kinetic and structural analysis of a cleaved donor intermediate and a strand transfer intermediate in Tn10 transposition
    • Haniford DB, Benjamin HW, Kleckner N. 1991. Kinetic and structural analysis of a cleaved donor intermediate and a strand transfer intermediate in Tn10 transposition. Cell 64:171-79
    • (1991) Cell , vol.64 , pp. 171-179
    • Haniford, D.B.1    Benjamin, H.W.2    Kleckner, N.3
  • 65
    • 0028276599 scopus 로고
    • Tn10 transposition in vivo: Temporal separation of cleavages at the two transposon ends and roles of terminal basepairs subsequent to interaction of ends
    • Haniford D, Kleckner N. 1994. Tn10 transposition in vivo: temporal separation of cleavages at the two transposon ends and roles of terminal basepairs subsequent to interaction of ends. EMBO J. 13:3401-11
    • (1994) EMBO J. , vol.13 , pp. 3401-3411
    • Haniford, D.1    Kleckner, N.2
  • 67
    • 0032538273 scopus 로고    scopus 로고
    • Multiple oligomerisation domains in the IS911 transposase: A leucine zipper motif is essential for activity
    • Haren L, Polard P, Ton-Hoang B, Chandler M. 1998. Multiple oligomerisation domains in the IS911 transposase: a leucine zipper motif is essential for activity. J. Mol. Biol. 283:29-41
    • (1998) J. Mol. Biol. , vol.283 , pp. 29-41
    • Haren, L.1    Polard, P.2    Ton-Hoang, B.3    Chandler, M.4
  • 68
    • 0030875813 scopus 로고    scopus 로고
    • Mapping features of HIV-1 integrase near selected sites on viral and target DNA molecules in an active enzyme-DNA complex by photo-cross-linking
    • Heuer TS, Brown PO. 1997. Mapping features of HIV-1 integrase near selected sites on viral and target DNA molecules in an active enzyme-DNA complex by photo-cross-linking. Biochemistry 36:10655-65
    • (1997) Biochemistry , vol.36 , pp. 10655-10665
    • Heuer, T.S.1    Brown, P.O.2
  • 69
    • 0032510707 scopus 로고    scopus 로고
    • Photo-crosslinking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex
    • Heuer TS, Brown PO. 1998. Photo-crosslinking studies suggest a model for the architecture of an active human immunodeficiency virus type 1 integrase-DNA complex. Biochemistry 37:6667-78
    • (1998) Biochemistry , vol.37 , pp. 6667-6678
    • Heuer, T.S.1    Brown, P.O.2
  • 70
    • 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. 1998. DNA transposition by the RAG1 and RAG2 proteins: a possible source of oncogenic translocations. Cell 94:463-70
    • (1998) Cell , vol.94 , pp. 463-470
    • Hiom, K.1    Melek, M.2    Gellert, M.3
  • 71
    • 0029980485 scopus 로고    scopus 로고
    • A soluble active mutant of HIV-1 integrase: Involvement of both the core and carboxyl-terminal domains in multimerization
    • Jenkins TM, Engelman A, Ghirlando R, Craigie R. 1996. A soluble active mutant of HIV-1 integrase: involvement of both the core and carboxyl-terminal domains in multimerization. J. Biol. Chem. 271:7712-18
    • (1996) J. Biol. Chem. , vol.271 , pp. 7712-7718
    • Jenkins, T.M.1    Engelman, A.2    Ghirlando, R.3    Craigie, R.4
  • 72
    • 0030828521 scopus 로고    scopus 로고
    • Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking
    • Jenkins TM, Esposito D, Engelman A, Craigie R. 1997. Critical contacts between HIV-1 integrase and viral DNA identified by structure-based analysis and photo-crosslinking. EMBO J. 16:6849-59
    • (1997) EMBO J. , vol.16 , pp. 6849-6859
    • Jenkins, T.M.1    Esposito, D.2    Engelman, A.3    Craigie, R.4
  • 73
    • 0031576367 scopus 로고    scopus 로고
    • The phiX174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transposition
    • Jones JM, Nakai H. 1997. The phiX174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transposition. EMBO J. 16:6886-95
    • (1997) EMBO J. , vol.16 , pp. 6886-6895
    • Jones, J.M.1    Nakai, H.2
  • 74
    • 0029920756 scopus 로고    scopus 로고
    • Multiple roles for divalent metal tons in DNA transposition: Distinct stages of Tn10 transposition have different Mg2+ requirements
    • Junop MS, Haniford DB. 1996. Multiple roles for divalent metal tons in DNA transposition: distinct stages of Tn10 transposition have different Mg2+ requirements. EMBO J. 15:2547-55
    • (1996) EMBO J. , vol.15 , pp. 2547-2555
    • Junop, M.S.1    Haniford, D.B.2
  • 75
    • 0030959067 scopus 로고    scopus 로고
    • Factors responsible for target site selection in Tn10 transposition: A role for the DDE motif in target DNA capture
    • Junop MS, Haniford DB. 1997. Factors responsible for target site selection in Tn10 transposition: a role for the DDE motif in target DNA capture. EMBO J. 16:2646-55
    • (1997) EMBO J. , vol.16 , pp. 2646-2655
    • Junop, M.S.1    Haniford, D.B.2
  • 76
    • 0027525261 scopus 로고
    • Genetic analysis of homomeric interactions of human immunodeficiency virus type 1 integrase using the yeast two-hybrid system
    • Kalpana GV, Goff SP. 1993. Genetic analysis of homomeric interactions of human immunodeficiency virus type 1 integrase using the yeast two-hybrid system. Proc. Natl. Acad. Sci. USA 90:10593-97
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10593-10597
    • Kalpana, G.V.1    Goff, S.P.2
  • 77
    • 0025011051 scopus 로고
    • The avian retroviral IN protein is both necessary and sufficient for integrative recombination in vitro
    • Katz RA, Merkel G, Kulkosky J, Leis J, Skalka AM. 1990. The avian retroviral IN protein is both necessary and sufficient for integrative recombination in vitro. Cell 63:87-95
    • (1990) Cell , vol.63 , pp. 87-95
    • Katz, R.A.1    Merkel, G.2    Kulkosky, J.3    Leis, J.4    Skalka, A.M.5
  • 78
    • 0026638840 scopus 로고
    • P element transposition in vitro proceeds by a cut-and-paste mechanism and uses GTP as a cofactor
    • Kaufman PD, Rio DC. 1992. P element transposition in vitro proceeds by a cut-and-paste mechanism and uses GTP as a cofactor. Cell 69:27-39
    • (1992) Cell , vol.69 , pp. 27-39
    • Kaufman, P.D.1    Rio, D.C.2
  • 80
    • 0029960810 scopus 로고    scopus 로고
    • Isolation and characterization of IS10 transposase separation of function mutants: Identification of amino acid residues in transposase that are important for active site function and the stability of transposition intermediates
    • Kennedy AK, Haniford DB. 1996. Isolation and characterization of IS10 transposase separation of function mutants: identification of amino acid residues in transposase that are important for active site function and the stability of transposition intermediates. J. Mol. Biol. 256:533-47
    • (1996) J. Mol. Biol. , vol.256 , pp. 533-547
    • Kennedy, A.K.1    Haniford, D.B.2
  • 81
    • 0026035178 scopus 로고
    • Retroviral integrase domains: DNA binding and the recognition of LTR sequences
    • Erratum. 1991. Nucleic Acids Res. 19:1358
    • Khan E, Mack JP, Katz RA, Kulkosky J, Skalka AM. 1991. Retroviral integrase domains: DNA binding and the recognition of LTR sequences. Nucleic Acids Res. 19:851-60 (Erratum. 1991. Nucleic Acids Res. 19:1358)
    • (1991) Nucleic Acids Res. , vol.19 , pp. 851-860
    • Khan, E.1    Mack, J.P.2    Katz, R.A.3    Kulkosky, J.4    Skalka, A.M.5
  • 82
    • 0028883476 scopus 로고
    • Mutational analysis of the att DNA-binding domain of phage Mu transposase
    • Kim K, Harshey RM. 1995. Mutational analysis of the att DNA-binding domain of phage Mu transposase, Nucleic Acids Res. 23:3937-43
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3937-3943
    • Kim, K.1    Harshey, R.M.2
  • 83
    • 0028883169 scopus 로고
    • Step-arrest mutants of phage Mu transposase, Implications in DNA-protein assembly, Mu end cleavage, and strand transfer
    • Kim K, Namgoong SY, Jayaram M, Harshey RM. 1995. Step-arrest mutants of phage Mu transposase, Implications in DNA-protein assembly, Mu end cleavage, and strand transfer. J. Biol. Chem. 270:1472-79
    • (1995) J. Biol. Chem. , vol.270 , pp. 1472-1479
    • Kim, K.1    Namgoong, S.Y.2    Jayaram, M.3    Harshey, R.M.4
  • 84
    • 0029655788 scopus 로고    scopus 로고
    • Tn10 and IS10 transposition and chromosome rearrangements: Mechanisms and regulation in vivo and in vitro
    • Kleckner N, Chalmers RM, Kwon D, Sakai J, Bolland S. 1996. Tn10 and IS10 transposition and chromosome rearrangements: mechanisms and regulation in vivo and in vitro. Curr Top. Microbiol. Immunol. 204:49-82
    • (1996) Curr Top. Microbiol. Immunol. , vol.204 , pp. 49-82
    • Kleckner, N.1    Chalmers, R.M.2    Kwon, D.3    Sakai, J.4    Bolland, S.5
  • 85
    • 0032553544 scopus 로고    scopus 로고
    • Mutational analysis of the Mu transposase. Contributions of two distinct regions of domain II to recombination
    • Krementsova E, Giffin MJ, Pincus D, Baker TA. 1998. Mutational analysis of the Mu transposase. Contributions of two distinct regions of domain II to recombination. J. Biol. Chem. 273:31358-65
    • (1998) J. Biol. Chem. , vol.273 , pp. 31358-31365
    • Krementsova, E.1    Giffin, M.J.2    Pincus, D.3    Baker, T.A.4
  • 86
    • 0030020897 scopus 로고    scopus 로고
    • ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
    • Kruklitis R, Welty DJ, Nakai H. 1996. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15:935-44
    • (1996) EMBO J. , vol.15 , pp. 935-944
    • Kruklitis, R.1    Welty, D.J.2    Nakai, H.3
  • 87
    • 0028790504 scopus 로고
    • Enhanced and coordinated processing of synapsed viral DNA ends by retroviral integrases in vitro
    • Kukolj G, Skalka AM. 1995. Enhanced and coordinated processing of synapsed viral DNA ends by retroviral integrases in vitro. Genes Dev. 9:2556-67
    • (1995) Genes Dev. , vol.9 , pp. 2556-2567
    • Kukolj, G.1    Skalka, A.M.2
  • 88
    • 0026719238 scopus 로고
    • Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases
    • Kulkosky J, Jones KS, Katz RA, Mack JP, Skalka AM. 1992. Residues critical for retroviral integrative recombination in a region that is highly conserved among retroviral/retrotransposon integrases and bacterial insertion sequence transposases. Mol. Cell Biol. 12:2331-38
    • (1992) Mol. Cell Biol. , vol.12 , pp. 2331-2338
    • Kulkosky, J.1    Jones, K.S.2    Katz, R.A.3    Mack, J.P.4    Skalka, A.M.5
  • 89
    • 0028850802 scopus 로고
    • Activities and substrate specificity of the evolutionarily conserved central domain of retroviral integrase
    • Kulkosky J, Katz RA, Merkel G, Skalka AM. 1995. Activities and substrate specificity of the evolutionarily conserved central domain of retroviral integrase. Virology 206:448-56
    • (1995) Virology , vol.206 , pp. 448-456
    • Kulkosky, J.1    Katz, R.A.2    Merkel, G.3    Skalka, A.M.4
  • 90
    • 0029655326 scopus 로고    scopus 로고
    • The maize transposable element activator (Ac)
    • Kunze R. 1996. The maize transposable element activator (Ac). Curr. Top. Microbiol. Immunol. 204:161-94
    • (1996) Curr. Top. Microbiol. Immunol. , vol.204 , pp. 161-194
    • Kunze, R.1
  • 92
    • 0029144546 scopus 로고
    • Structural domains of IS10 transposase and reconstitution of transposition activity from proteolytic fragments lacking an interdomain linker
    • Kwon D, Chalmers RM, Kleckner N. 1995. Structural domains of IS10 transposase and reconstitution of transposition activity from proteolytic fragments lacking an interdomain linker. Proc. Natl. Acad. Sci. USA 92:8234-38
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8234-8238
    • Kwon, D.1    Chalmers, R.M.2    Kleckner, N.3
  • 93
    • 0026072804 scopus 로고
    • Substrate specificity of recombinant human immunodeficiency virus integrase protein
    • LaFemina RL, Callahan PL, Cordingley MG. 1991. Substrate specificity of recombinant human immunodeficiency virus integrase protein. J. Virol. 65:5624-30
    • (1991) J. Virol. , vol.65 , pp. 5624-5630
    • LaFemina, R.L.1    Callahan, P.L.2    Cordingley, M.G.3
  • 94
    • 0030926820 scopus 로고    scopus 로고
    • A purified mariner transposase is sufficient to mediate transposition in vitro
    • Lampe DJ, Churchill ME, Robertson HM. 1997. A purified mariner transposase is sufficient to mediate transposition in vitro (erratum). EMBO J. 16:4153
    • (1997) EMBO J. , vol.16 , pp. 4153
    • Lampe, D.J.1    Churchill, M.E.2    Robertson, H.M.3
  • 96
    • 0025850374 scopus 로고
    • Structural aspects of a higher order nucleoprotein complex: Induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome
    • Lavoie BD, Chan BS, Allison RG, Chaconas G. 1991. Structural aspects of a higher order nucleoprotein complex: induction of an altered DNA structure at the Mu-host junction of the Mu type 1 transpososome. EMBO J. 10:3051-59
    • (1991) EMBO J. , vol.10 , pp. 3051-3059
    • Lavoie, B.D.1    Chan, B.S.2    Allison, R.G.3    Chaconas, G.4
  • 97
    • 0032528302 scopus 로고    scopus 로고
    • DNA binding by the KP repressor protein inhibits P-element transposase activity in vitro
    • Lee CC, Beall EL, Rio DC. 1998. DNA binding by the KP repressor protein inhibits P-element transposase activity in vitro. EMBO J. 17:4166-74
    • (1998) EMBO J. , vol.17 , pp. 4166-4174
    • Lee, C.C.1    Beall, E.L.2    Rio, D.C.3
  • 98
    • 0030614408 scopus 로고    scopus 로고
    • Zn2+ promotes the self-association of human immunodeficiency virus type-I integrase in vitro
    • Lee SP, Xiao J, Knutson JR, Lewis MS, Han MK. 1997. Zn2+ promotes the self-association of human immunodeficiency virus type-I integrase in vitro. Biochemistry 36:173-80
    • (1997) Biochemistry , vol.36 , pp. 173-180
    • Lee, S.P.1    Xiao, J.2    Knutson, J.R.3    Lewis, M.S.4    Han, M.K.5
  • 100
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the CIpX chaperone
    • Levchenko I, Luo L, Baker TA. 1995. Disassembly of the Mu transposase tetramer by the CIpX chaperone. Genes Dev. 9:2399-408
    • (1995) Genes Dev. , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 102
    • 0029861753 scopus 로고    scopus 로고
    • Subunit interactions in the mariner transposase
    • Lohe AR, Sullivan DT, Hartl DL. 1996. Subunit interactions in the mariner transposase. Genetics 144:1087-95
    • (1996) Genetics , vol.144 , pp. 1087-1095
    • Lohe, A.R.1    Sullivan, D.T.2    Hartl, D.L.3
  • 103
    • 0001166515 scopus 로고    scopus 로고
    • Structure-based mutational analysis of the C-terminal DNA-binding domain of human immunodeficiency virus type 1 integrase: Critical residues for protein oligomerization and DNA binding
    • Lutzke RP, Plasterk RA. 1998. Structure-based mutational analysis of the C-terminal DNA-binding domain of human immunodeficiency virus type 1 integrase: critical residues for protein oligomerization and DNA binding. J. Virol. 72:484 1-48
    • (1998) J. Virol. , vol.72 , pp. 4841-4848
    • Lutzke, R.P.1    Plasterk, R.A.2
  • 104
    • 0028034050 scopus 로고
    • Characterization of the minimal DNA-binding domain of the HIV integrase protein
    • Lutzke RA, Vink C, Plasterk RH. 1994. Characterization of the minimal DNA-binding domain of the HIV integrase protein. Nucleic Acids Res. 22:4125-31
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4125-4131
    • Lutzke, R.A.1    Vink, C.2    Plasterk, R.H.3
  • 105
    • 0024974958 scopus 로고
    • Regulation of IS1 transposition by the insA gene product
    • Machida C, Machida Y. 1989. Regulation of IS1 transposition by the insA gene product. J. Mol. Biol. 208:567-74
    • (1989) J. Mol. Biol. , vol.208 , pp. 567-574
    • Machida, C.1    Machida, Y.2
  • 108
    • 0023122585 scopus 로고
    • B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer
    • Maxwell A, Craigie R, Mizuuchi K. 1987. B protein of bacteriophage mu is an ATPase that preferentially stimulates intermolecular DNA strand transfer. Proc. Natl. Acad. Sci. USA 84:699-703
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 699-703
    • Maxwell, A.1    Craigie, R.2    Mizuuchi, K.3
  • 109
    • 0029984672 scopus 로고    scopus 로고
    • Switching from cut-and-paste to replicative Tn7 transposition
    • May EW, Craig NL. 1996. Switching from cut-and-paste to replicative Tn7 transposition. Science 272:401-4
    • (1996) Science , vol.272 , pp. 401-404
    • May, E.W.1    Craig, N.L.2
  • 110
    • 0026799383 scopus 로고
    • Polynucieotidyl transfer reactions in transpositional DNA recombination
    • Mizuuchi K. 1992. Polynucieotidyl transfer reactions in transpositional DNA recombination. J. Biol. Chem. 267:21273-76
    • (1992) J. Biol. Chem. , vol.267 , pp. 21273-21276
    • Mizuuchi, K.1
  • 111
    • 0026637325 scopus 로고
    • Transpositional recombination: Mechanistic insights from studies of Mu and other elements
    • Mizuuchi K. 1992. Transpositional recombination: mechanistic insights from studies of Mu and other elements. Annu. Rev Biochem. 61:1011-51
    • (1992) Annu. Rev Biochem. , vol.61 , pp. 1011-1051
    • Mizuuchi, K.1
  • 112
    • 0030628279 scopus 로고    scopus 로고
    • Polynucleotidyl transfer reactions in site-specific DNA recombination
    • Mizuuchi K. 1997. Polynucleotidyl transfer reactions in site-specific DNA recombination. Genes Cells 2:1-12
    • (1997) Genes Cells , vol.2 , pp. 1-12
    • Mizuuchi, K.1
  • 113
    • 0025899314 scopus 로고
    • Inversion of the phosphate chirality ar the target site of Mu DNA strand transfer: Evidence for a one-step transesterification mechanism
    • Mizuuchi K, Adzuma K. 1991. Inversion of the phosphate chirality ar the target site of Mu DNA strand transfer: evidence for a one-step transesterification mechanism. Cell 66:129-140
    • (1991) Cell , vol.66 , pp. 129-140
    • Mizuuchi, K.1    Adzuma, K.2
  • 114
    • 0026093974 scopus 로고
    • DNase protection analysis of the stable synaptic complexes involved in Mu transposition
    • Mizuuchi M, Baker TA, Mizuuchi K. 1991. DNase protection analysis of the stable synaptic complexes involved in Mu transposition. Proc. Natl. Acad. Sci. USA 88:9031-35
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9031-9035
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 115
    • 0026708067 scopus 로고
    • Assembly of the active form of the transposase-Mu DNA complex: A critical control point in Mu transposition
    • Mizuuchi M, Baker TA. Mizuuchi K. 1992. Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition. Cell 70:303-11
    • (1992) Cell , vol.70 , pp. 303-311
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 116
    • 0026652466 scopus 로고
    • A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the vital integrase in vivo
    • Murphy JE, Goff SP. 1992. A mutation at one end of Moloney murine leukemia virus DNA blocks cleavage of both ends by the vital integrase in vivo. J. Virol. 66:5092-95
    • (1992) J. Virol. , vol.66 , pp. 5092-5095
    • Murphy, J.E.1    Goff, S.P.2
  • 117
    • 0030828364 scopus 로고    scopus 로고
    • A new set of Mu DNA transposition intermediates: Alternate pathways of target capture preceding strand transfer
    • Naigamwalla DZ, Chaconas G. 1997. A new set of Mu DNA transposition intermediates: alternate pathways of target capture preceding strand transfer. EMBO J. 16:5227-34
    • (1997) EMBO J. , vol.16 , pp. 5227-5234
    • Naigamwalla, D.Z.1    Chaconas, G.2
  • 118
    • 0342934743 scopus 로고
    • Structural domains in phage Mu transposase: Identification of the site-specific DNA-binding domain
    • Nakayama C, Teplow DB, Harshey RM. 1987. Structural domains in phage Mu transposase: identification of the site-specific DNA-binding domain. Proc. Natl. Acad. Sci. USA 84:1809-13
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1809-1813
    • Nakayama, C.1    Teplow, D.B.2    Harshey, R.M.3
  • 119
    • 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 SY, Harshey RM. 1998. The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition. EMBO J. 17:3775-85
    • (1998) EMBO J. , vol.17 , pp. 3775-3785
    • Namgoong, S.Y.1    Harshey, R.M.2
  • 120
    • 0032536109 scopus 로고    scopus 로고
    • Mutational analysis of domain IIβ of bacteriophage Mu transposase: Domains IIα and IIβ belongs to different catalytic complementation groups
    • Namgoong SY, Kim K, Saxena P, Yang JY, Jayaram M, et al. 1998. Mutational analysis of domain IIβ of bacteriophage Mu transposase: domains IIα and IIβ belongs to different catalytic complementation groups. J. Mol. Biol. 275:221-32
    • (1998) J. Mol. Biol. , vol.275 , pp. 221-232
    • Namgoong, S.Y.1    Kim, K.2    Saxena, P.3    Yang, J.Y.4    Jayaram, M.5
  • 121
    • 0027245588 scopus 로고
    • Formation of the tandem repeat (IS30)2 and its role in IS30-mediated transpositional DNA rearrangements
    • Olasz F, Stalder R, Arber W. 1993. Formation of the tandem repeat (IS30)2 and its role in IS30-mediated transpositional DNA rearrangements. Mol. Gen. Genet. 239:177-87
    • (1993) Mol. Gen. Genet. , vol.239 , pp. 177-187
    • Olasz, F.1    Stalder, R.2    Arber, W.3
  • 122
  • 123
    • 0031010740 scopus 로고    scopus 로고
    • A helix-turn-helix DNA-binding motif predicted for transposases of DNA transposons
    • Pictrokovski S, Henikoff S. 1997. A helix-turn-helix DNA-binding motif predicted for transposases of DNA transposons. Mol. Gen. Genet. 254:689-95
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 689-695
    • Pictrokovski, S.1    Henikoff, S.2
  • 125
    • 0028840748 scopus 로고
    • An in vivo transposase-catalyzed single-stranded DNA circularization reaction
    • Polard P, Chandler M. 1995. An in vivo transposase-catalyzed single-stranded DNA circularization reaction. Genes Dev. 9:2846-58
    • (1995) Genes Dev. , vol.9 , pp. 2846-2858
    • Polard, P.1    Chandler, M.2
  • 126
    • 0028928168 scopus 로고
    • Bacterial transposases and retroviral integrases
    • Polard P, Chandler M. 1995. Bacterial transposases and retroviral integrases. Mol. Microbiol. 15:13-23
    • (1995) Mol. Microbiol. , vol.15 , pp. 13-23
    • Polard, P.1    Chandler, M.2
  • 128
    • 0023112502 scopus 로고
    • Mode of replicon fusion mediated by the duplicated insertion sequence IS21 in Escherichia coli
    • Reimmann C, Haas D. 1987. Mode of replicon fusion mediated by the duplicated insertion sequence IS21 in Escherichia coli. Genetics 115:619-25
    • (1987) Genetics , vol.115 , pp. 619-625
    • Reimmann, C.1    Haas, D.2
  • 130
    • 0027517782 scopus 로고
    • The IS4 family of insertion sequences: Evidence for a conserved transposase motif
    • Rezsohazy R, Hallet B, Delcour J, Mahillon J. 1993. The IS4 family of insertion sequences: evidence for a conserved transposase motif. Mol. Microbiol. 9:1283-95
    • (1993) Mol. Microbiol. , vol.9 , pp. 1283-1295
    • Rezsohazy, R.1    Hallet, B.2    Delcour, J.3    Mahillon, J.4
  • 132
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: A common structural motif for DNA transposition and retroviral integration
    • Rice P, Mizuuchi K. 1995. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell 82:209-20
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.1    Mizuuchi, K.2
  • 133
    • 0025309894 scopus 로고
    • Tn552, a novel transposable element from Staphylococcus aureus
    • Rowland SJ, Dyke KG. 1990. Tn552, a novel transposable element from Staphylococcus aureus. Mol. Microbiol. 4:961-75
    • (1990) Mol. Microbiol. , vol.4 , pp. 961-975
    • Rowland, S.J.1    Dyke, K.G.2
  • 136
    • 0029143391 scopus 로고
    • Identification and characterization of a pre-cleavage synaptic complex that is an early intermediate in Tn10 transposition
    • Sakai J, Chalmers RM, Kleckner N. 1995. Identification and characterization of a pre-cleavage synaptic complex that is an early intermediate in Tn10 transposition. EMBO J. 14:4374-83
    • (1995) EMBO J. , vol.14 , pp. 4374-4383
    • Sakai, J.1    Chalmers, R.M.2    Kleckner, N.3
  • 137
    • 0030967281 scopus 로고    scopus 로고
    • The Tn10 synaptic complex can capture a target DNA only after transposon excision
    • Sakai J, Kleckner N. 1997. The Tn10 synaptic complex can capture a target DNA only after transposon excision. Cell 89:205-14
    • (1997) Cell , vol.89 , pp. 205-214
    • Sakai, J.1    Kleckner, N.2
  • 138
    • 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 RJ, May EW, Craig NL. 1996. The Tn7 transposase is a heteromeric complex in which DNA breakage and joining activities are distributed between different gene products. EMBO J. 15:6348-61
    • (1996) EMBO J. , vol.15 , pp. 6348-6361
    • Sarnovsky, R.J.1    May, E.W.2    Craig, N.L.3
  • 139
    • 0029986753 scopus 로고    scopus 로고
    • Mu transpositional recombination: Donor DNA cleavage and strand transfer in trans by the Mu transposase
    • Savilahti H, Mizuuchi K. 1996. Mu transpositional recombination: donor DNA cleavage and strand transfer in trans by the Mu transposase. Cell 85:271-80
    • (1996) Cell , vol.85 , pp. 271-280
    • Savilahti, H.1    Mizuuchi, K.2
  • 140
    • 0029096898 scopus 로고
    • The phage Mu transpososome core: DNA requirements for assembly and function
    • Savilahti H, Rice PA, Mizuuchi K. 1995. The phage Mu transpososome core: DNA requirements for assembly and function. EMBO J. 14:4893-903
    • (1995) EMBO J. , vol.14 , pp. 4893-4903
    • Savilahti, H.1    Rice, P.A.2    Mizuuchi, K.3
  • 141
    • 0031464544 scopus 로고    scopus 로고
    • Solution structure of the Mu end DNA-binding Iβ subdomain of phage Mu transposase: Modular DNA recognition by two tethered domains
    • Schumacher S, Clubb RT, Cai M, Mizuuchi K, Clore GM, Gronenborn AM. 1997, Solution structure of the Mu end DNA-binding Iβ subdomain of phage Mu transposase: modular DNA recognition by two tethered domains. EMBO J. 16:7532-41
    • (1997) EMBO J. , vol.16 , pp. 7532-7541
    • Schumacher, S.1    Clubb, R.T.2    Cai, M.3    Mizuuchi, K.4    Clore, G.M.5    Gronenborn, A.M.6
  • 142
    • 0031050297 scopus 로고    scopus 로고
    • Disruption of the terminal base pairs of retroviral DNA during integration
    • Scottoline BP, Chow S, Ellison V, Brown PO. 1997. Disruption of the terminal base pairs of retroviral DNA during integration. Genes Dev. 11:371-82
    • (1997) Genes Dev. , vol.11 , pp. 371-382
    • Scottoline, B.P.1    Chow, S.2    Ellison, V.3    Brown, P.O.4
  • 143
    • 0032189817 scopus 로고    scopus 로고
    • Host proteins can stimulate Tn7 transposition: A novel role for the ribosomal protein L29 and the acyl carrier protein
    • Sharpe PL, Craig NL. 1998. Host proteins can stimulate Tn7 transposition: a novel role for the ribosomal protein L29 and the acyl carrier protein. EMBO J. 17:5822-31
    • (1998) EMBO J. , vol.17 , pp. 5822-5831
    • Sharpe, P.L.1    Craig, N.L.2
  • 144
    • 0025366844 scopus 로고
    • Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity
    • Sherman PA, Fyfe JA. 1990. Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity. Proc. Natl. Acad. Sci. USA 87:5119-23
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5119-5123
    • Sherman, P.A.1    Fyfe, J.A.2
  • 145
    • 0001070790 scopus 로고
    • Tn3 and related transposable elements: Site-specific recombination and transposition
    • cd. D. Berg, M. Howe, Washington, DC: Am. Soc. Microbiol.
    • Sherratt D. 1989. Tn3 and related transposable elements: site-specific recombination and transposition. In Mobile DNA, cd. D. Berg, M. Howe, pp. 163-84. Washington, DC: Am. Soc. Microbiol.
    • (1989) Mobile DNA , pp. 163-184
    • Sherratt, D.1
  • 146
    • 0030932575 scopus 로고    scopus 로고
    • Central core domain of retroviral integrase is responsible for target site selection
    • Shibagaki Y, Chow SA. 1997. Central core domain of retroviral integrase is responsible for target site selection. J. Biol. Chem. 272:8361-69
    • (1997) J. Biol. Chem. , vol.272 , pp. 8361-8369
    • Shibagaki, Y.1    Chow, S.A.2
  • 147
    • 0025247877 scopus 로고
    • The N-terminal domain of the insertion sequence 30 transposase interacts specifically with the terminal inverted repeats of the element
    • Stalder R, Caspers P, Olasz F, Arber W. 1990. The N-terminal domain of the insertion sequence 30 transposase interacts specifically with the terminal inverted repeats of the element. J. Biol. Chem. 265:3757-62
    • (1990) J. Biol. Chem. , vol.265 , pp. 3757-3762
    • Stalder, R.1    Caspers, P.2    Olasz, F.3    Arber, W.4
  • 148
    • 0030859543 scopus 로고    scopus 로고
    • Avoiding self: Two Tn7-encoded proteins mediate target immunity in Tn7 transposition
    • Stellwagen AE, Craig NL. 1997. Avoiding self: two Tn7-encoded proteins mediate target immunity in Tn7 transposition. EMBO J. 16:6823-34
    • (1997) EMBO J. , vol.16 , pp. 6823-6834
    • Stellwagen, A.E.1    Craig, N.L.2
  • 149
    • 0023663468 scopus 로고
    • Transpososomes: Stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA
    • Surette MG, Buch SJ, Chaconas G. 1987. Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA. Cell 49:253-62
    • (1987) Cell , vol.49 , pp. 253-262
    • Surette, M.G.1    Buch, S.J.2    Chaconas, G.3
  • 150
    • 0025804518 scopus 로고
    • Stimulation of the Mu A protein-mediated strand cleavage reaction by the Mu B protein, and the requirement of DNA nicking for stable type 1 transpososome formation. In vitro transposition characteristics of mini-Mu plasmids carrying terminal base pair mutations
    • Surette MG, Harkness T, Chaconas G. 1991. Stimulation of the Mu A protein-mediated strand cleavage reaction by the Mu B protein, and the requirement of DNA nicking for stable type 1 transpososome formation. In vitro transposition characteristics of mini-Mu plasmids carrying terminal base pair mutations. J. Biol. Chem. 266:3118-24
    • (1991) J. Biol. Chem. , vol.266 , pp. 3118-3124
    • Surette, M.G.1    Harkness, T.2    Chaconas, G.3
  • 151
    • 0029890247 scopus 로고    scopus 로고
    • Isolation, characterization and transposition of an (IS2)2 intermediate
    • Szeverenyi I, Bodoky T, Olasz F. 1996. Isolation, characterization and transposition of an (IS2)2 intermediate. Mol. Gen. Genet. 251:281-89
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 281-289
    • Szeverenyi, I.1    Bodoky, T.2    Olasz, F.3
  • 152
    • 0031565988 scopus 로고    scopus 로고
    • Defining functional regions of the IS903 transposase
    • Tavakoli NP, DeVost J, Derbyshire KM. 1997. Defining functional regions of the IS903 transposase. J. Mol. Biol. 274:491-504
    • (1997) J. Mol. Biol. , vol.274 , pp. 491-504
    • Tavakoli, N.P.1    DeVost, J.2    Derbyshire, K.M.3
  • 154
    • 18244413221 scopus 로고    scopus 로고
    • Assembly of a strong promoter following IS911 circularization anal the role of circles in transposition
    • Ton-Hoang B, Betermier M, Polard P, Chandler M. 1997. Assembly of a strong promoter following IS911 circularization anal the role of circles in transposition. EMBO J. 16:3357-71
    • (1997) EMBO J. , vol.16 , pp. 3357-3371
    • Ton-Hoang, B.1    Betermier, M.2    Polard, P.3    Chandler, M.4
  • 155
    • 0032481375 scopus 로고    scopus 로고
    • Efficient transposition of IS911 circles in vitro
    • Ton-Hoang B, Polard P, Chandler M. 1998. Efficient transposition of IS911 circles in vitro, EMBO J. 17:1169-81
    • (1998) EMBO J. , vol.17 , pp. 1169-1181
    • Ton-Hoang, B.1    Polard, P.2    Chandler, M.3
  • 156
    • 0028670149 scopus 로고
    • Role of the Mg2+ ion in the Escherichia coli ribonuclease HI reaction
    • Uchiyama Y, Iwai S, Ueno Y, Ikehara M, Ohtsuka E. 1994. Role of the Mg2+ ion in the Escherichia coli ribonuclease HI reaction. J. Biochem. (Tokyo). 116:1322-29
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 1322-1329
    • Uchiyama, Y.1    Iwai, S.2    Ueno, Y.3    Ikehara, M.4    Ohtsuka, E.5
  • 157
    • 0031965842 scopus 로고    scopus 로고
    • Mutational scan of the human immunodeficiency virus type 2 integrase protein
    • van den Ent FM, Vos A, Plasterk RH. 1998. Mutational scan of the human immunodeficiency virus type 2 integrase protein. J. Virol. 72:3916-24
    • (1998) J. Virol. , vol.72 , pp. 3916-3924
    • Van den Ent, F.M.1    Vos, A.2    Plasterk, R.H.3
  • 158
    • 0025775488 scopus 로고
    • DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2
    • van Gent DC, Elgersma Y, Bolk MW, Vink C, Plasterk RH. 1991. DNA binding properties of the integrase proteins of human immunodeficiency viruses types 1 and 2. Nucleic Acids Res. 19:3821-27
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3821-3827
    • Van Gent, D.C.1    Elgersma, Y.2    Bolk, M.W.3    Vink, C.4    Plasterk, R.H.5
  • 159
    • 0026668776 scopus 로고
    • Mutational analysis or the integrase protein of human immunodeficiency virus type 2
    • van Gent DC, Groeneger AA, Plasterk RH. 1992. Mutational analysis or the integrase protein of human immunodeficiency virus type 2. Proc. Natl. Acad. Sci. USA 89:9598-602
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9598-95602
    • Van Gent, D.C.1    Groeneger, A.A.2    Plasterk, R.H.3
  • 160
    • 0029967722 scopus 로고    scopus 로고
    • Similarities between initiation of V(D)J recombination and retroviral integration
    • van Gent DC, Mizuuchi K, Gellert M. 1996. Similarities between initiation of V(D)J recombination and retroviral integration. Science 271:1592-94
    • (1996) Science , vol.271 , pp. 1592-1594
    • Van Gent, D.C.1    Mizuuchi, K.2    Gellert, M.3
  • 161
    • 0027179416 scopus 로고
    • Identification of amino acids in HIV-2 integrase involved in site-specific hydrolysis and alcoholysis of viral DNA termini
    • van Gent DC, Oude Groeneger AA, Plasterk RH. 1993. Identification of amino acids in HIV-2 integrase involved in site-specific hydrolysis and alcoholysis of viral DNA termini. Nucleic Acids Res. 21:3373-77
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3373-3377
    • Van Gent, D.C.1    Oude Groeneger, A.A.2    Plasterk, R.H.3
  • 162
    • 0027246609 scopus 로고
    • Complementation between HIV integrase proteins mutated in different domains
    • van Gent DC, Vink C, Groeneger AA, Plasterk RH. 1993. Complementation between HIV integrase proteins mutated in different domains. EMBO J. 12:3261-67
    • (1993) EMBO J. , vol.12 , pp. 3261-3267
    • Van Gent, D.C.1    Vink, C.2    Groeneger, A.A.3    Plasterk, R.H.4
  • 163
    • 0028090258 scopus 로고
    • The mechanism of transposition of Tc3 in C. elegans
    • van Luenen HG, Colloms SD, Plasterk RH. 1994, The mechanism of transposition of Tc3 in C. elegans. Cell 7984:293-301
    • (1994) Cell , vol.7984 , pp. 293-301
    • Van Luenen, H.G.1    Colloms, S.D.2    Plasterk, R.H.3
  • 164
    • 0030779907 scopus 로고    scopus 로고
    • Crystal structure of the specific DNA-binding domain of Tc3 transposase of C. elegans in complex with transposon DNA
    • van Pouderoyen G, Ketting RF, Perrakis A, Plasterk RHA, Sixma TK. 1997. Crystal structure of the specific DNA-binding domain of Tc3 transposase of C. elegans in complex with transposon DNA, EMBO J. 16:6044-54
    • (1997) EMBO J. , vol.16 , pp. 6044-6054
    • Van Pouderoyen, G.1    Ketting, R.F.2    Perrakis, A.3    Plasterk, R.H.A.4    Sixma, T.K.5
  • 165
    • 0028125329 scopus 로고
    • Formation of a stable complex between the human immunodeficiency virus integrase protein and vital DNA
    • Vink C, Lutzke RA, Plasterk RH. 1994. Formation of a stable complex between the human immunodeficiency virus integrase protein and vital DNA. Nucleic Acids Res. 22:4103-10
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4103-4110
    • Vink, C.1    Lutzke, R.A.2    Plasterk, R.H.3
  • 166
    • 0027210608 scopus 로고
    • Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type 1 integrase protein
    • Vink C, Oude Groeneger AM, Plasterk RH. 1993. Identification of the catalytic and DNA-binding region of the human immunodeficiency virus type 1 integrase protein. Nucleic Acids Res. 21:1419-25
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1419-1425
    • Vink, C.1    Oude Groeneger, A.M.2    Plasterk, R.H.3
  • 167
    • 0026095906 scopus 로고
    • Human immunodeficiency virus integrase protein requires a subterminal position of its vital DNA recognition sequence for efficient cleavage
    • Vink C, van Gent DC, Elgersma Y, Plasterk RH. 1991. Human immunodeficiency virus integrase protein requires a subterminal position of its vital DNA recognition sequence for efficient cleavage. J. Virol. 65:4636-44
    • (1991) J. Virol. , vol.65 , pp. 4636-4644
    • Vink, C.1    Van Gent, D.C.2    Elgersma, Y.3    Plasterk, R.H.4
  • 168
    • 0028598507 scopus 로고
    • Tcl transposase of Caenorhabditis elegans is an endonuclease with a bipartite DNA binding domain
    • Vos JC, Plasterk RH. 1994. Tcl transposase of Caenorhabditis elegans is an endonuclease with a bipartite DNA binding domain. EMBO J. 13:6125-32
    • (1994) EMBO J. , vol.13 , pp. 6125-6132
    • Vos, J.C.1    Plasterk, R.H.2
  • 169
    • 0027321357 scopus 로고
    • Characterization of the Caenorhabditis elegans Tcl transposase in vivo and in vitro
    • Vos JC, van Luenen HG, Plasterk RH. 1993. Characterization of the Caenorhabditis elegans Tcl transposase in vivo and in vitro. Genes Dev. 7:1244-53
    • (1993) Genes Dev. , vol.7 , pp. 1244-1253
    • Vos, J.C.1    Van Luenen, H.G.2    Plasterk, R.H.3
  • 170
    • 0027979780 scopus 로고
    • Crucial role for DNA supercoiling in Mu transposition: A kinetic study
    • Wang Z, Harshey RM. 1994. Crucial role for DNA supercoiling in Mu transposition: a kinetic study. Proc. Natl. Acad. Sci. USA 91:699-703
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 699-703
    • Wang, Z.1    Harshey, R.M.2
  • 171
    • 0029870895 scopus 로고    scopus 로고
    • Kinetic and structural probing of the precleavage synaptic complex (type 0) formed during phage Mu transposition. Action of metal ions and reagents specific to single-stranded DNA
    • Wang Z, Namgoong SY, Zhang X, Harshey RM. 1996. Kinetic and structural probing of the precleavage synaptic complex (type 0) formed during phage Mu transposition. Action of metal ions and reagents specific to single-stranded DNA. J. Biol. Chem. 271:9619-26
    • (1996) J. Biol. Chem. , vol.271 , pp. 9619-9626
    • Wang, Z.1    Namgoong, S.Y.2    Zhang, X.3    Harshey, R.M.4
  • 172
    • 0029941285 scopus 로고    scopus 로고
    • Three-site synapsis during Mu DNA transposition: A critical intermediate preceding engagement of the active site
    • Watson MA, Cbaconas G. 1996. Three-site synapsis during Mu DNA transposition: a critical intermediate preceding engagement of the active site. Cell 85:435-45
    • (1996) Cell , vol.85 , pp. 435-445
    • Watson, M.A.1    Cbaconas, G.2
  • 173
    • 0031449687 scopus 로고    scopus 로고
    • A large nucleoprotein assembly at the ends of the viral DNA mediates retroviral DNA integration
    • Wei SQ, Mizuuchi K, Craigie R. 1997. A large nucleoprotein assembly at the ends of the viral DNA mediates retroviral DNA integration. EMBO J. 16:7511-20
    • (1997) EMBO J. , vol.16 , pp. 7511-7520
    • Wei, S.Q.1    Mizuuchi, K.2    Craigie, R.3
  • 174
    • 0028059193 scopus 로고
    • A functional analysis of the Tn5 transposase. Identification of domains required for DNA binding and multimerization
    • Weinreich MD, Mahnke-Braam L, Reznikoff WS. 1994. A functional analysis of the Tn5 transposase. Identification of domains required for DNA binding and multimerization. J. Mol, Biol. 241:166-77
    • (1994) J. Mol. Biol. , vol.241 , pp. 166-177
    • Weinreich, M.D.1    Mahnke-Braam, L.2    Reznikoff, W.S.3
  • 175
    • 0025968510 scopus 로고
    • Gamma delta transposase. Purification and analysis of its interaction with a transposon end
    • Wiater LA, Grindley ND. 1991. Gamma delta transposase. Purification and analysis of its interaction with a transposon end. J. Biol. Chem. 266:1841-49
    • (1991) J. Biol. Chem. , vol.266 , pp. 1841-1849
    • Wiater, L.A.1    Grindley, N.D.2
  • 176
    • 0027976414 scopus 로고
    • Interaction of Tn5 transposase with the transposon termini
    • Wiegand TW, Reznikoff WS. 1994. Interaction of Tn5 transposase with the transposon termini. J. Mol. Biol. 235:486-95
    • (1994) J. Mol. Biol. , vol.235 , pp. 486-495
    • Wiegand, T.W.1    Reznikoff, W.S.2
  • 177
    • 0030051081 scopus 로고    scopus 로고
    • The role of manganese in promoting multimerization and assembly of human immunodeficiency virus type 1 integrase as a catalytically active complex on immobilized long terminal repeat substrates
    • Wolfe AL, Felock PJ, Hastings JC, Blau CU, Hazuda DJ. 1996. The role of manganese in promoting multimerization and assembly of human immunodeficiency virus type 1 integrase as a catalytically active complex on immobilized long terminal repeat substrates. J. Virol. 70:1424-32
    • (1996) J. Virol. , vol.70 , pp. 1424-1432
    • Wolfe, A.L.1    Felock, P.J.2    Hastings, J.C.3    Blau, C.U.4    Hazuda, D.J.5
  • 178
    • 0029151254 scopus 로고
    • A novel DNA binding and nuclease activity in domain III of Mu transposase: Evidence for a catalytic region involved in donor cleavage
    • Wu Z, Chaconas G. 1995. A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage. EMBO J. 14:3835-43
    • (1995) EMBO J. , vol.14 , pp. 3835-3843
    • Wu, Z.1    Chaconas, G.2
  • 179
    • 0032530649 scopus 로고    scopus 로고
    • An ATP-ADP switch in MuB controls progression of the Mu transposition pathway
    • Yamauchi M, Baker TA. 1998. An ATP-ADP switch in MuB controls progression of the Mu transposition pathway. EMBO J. 17:5509-18
    • (1998) EMBO J. , vol.17 , pp. 5509-5518
    • Yamauchi, M.1    Baker, T.A.2
  • 180
    • 0029048507 scopus 로고
    • A domain sharing model for active site assembly within the Mu A tetramer during transposition: The enhancer may specify domain contributions
    • Yang JY, Kim K, Jayaram M, Harshey RM. 1995. A domain sharing model for active site assembly within the Mu A tetramer during transposition: the enhancer may specify domain contributions. EMBO J. 14:2374-84
    • (1995) EMBO J. , vol.14 , pp. 2374-2384
    • Yang, J.Y.1    Kim, K.2    Jayaram, M.3    Harshey, R.M.4
  • 181
    • 0029643952 scopus 로고
    • Recombining the structures of HIV integrase, RuvC and RNase H
    • Yang W, Steitz TA. 1995. Recombining the structures of HIV integrase, RuvC and RNase H. Structure 3:131-34
    • (1995) Structure , vol.3 , pp. 131-134
    • Yang, W.1    Steitz, T.A.2
  • 182
    • 0024278075 scopus 로고
    • Effect of dam methylation on Tn5 transposition
    • Yin JC, Krebs MP, Reznikoff WS. 1988. Effect of dam methylation on Tn5 transposition. J. Mol. Biol. 199:35-45
    • (1988) J. Mol. Biol. , vol.199 , pp. 35-45
    • Yin, J.C.1    Krebs, M.P.2    Reznikoff, W.S.3
  • 183
    • 0029795972 scopus 로고    scopus 로고
    • Catalytic center quest: Comparison of transposases belonging to the Tn3 family reveals an invariant triad of acidic amino acid residues
    • Yurieva O, Nikiforov V. 1996. Catalytic center quest: comparison of transposases belonging to the Tn3 family reveals an invariant triad of acidic amino acid residues. Biochem. Mol. Biol. Int. 38:15-20
    • (1996) Biochem. Mol. Biol. Int. , vol.38 , pp. 15-20
    • Yurieva, O.1    Nikiforov, V.2
  • 184
    • 0023426836 scopus 로고
    • Expression of proteins essential for IS1 transposition: Specific binding of InsA to the ends of IS1
    • Zerbib D, Jakowec M, Prentki P, Galas DJ, Chandler M. 1987. Expression of proteins essential for IS1 transposition: specific binding of InsA to the ends of IS1. EMBO J. 6:3163-69
    • (1987) EMBO J. , vol.6 , pp. 3163-3169
    • Zerbib, D.1    Jakowec, M.2    Prentki, P.3    Galas, D.J.4    Chandler, M.5
  • 185
    • 0030478950 scopus 로고    scopus 로고
    • Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity
    • Zheng R, Jenkins TM, Craigie R. 1996. Zinc folds the N-terminal domain of HIV-1 integrase, promotes multimerization, and enhances catalytic activity. Proc. Natl. Acad. Sci. USA 93:13659-64
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13659-13664
    • Zheng, R.1    Jenkins, T.M.2    Craigie, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.