메뉴 건너뛰기




Volumn 62, Issue 12, 2010, Pages 1187-1195

DDE transposases: Structural similarity and diversity

Author keywords

DD E D transposase; DNA transposon; Structure; Transposase

Indexed keywords

CATALYTIC DOMAINS; CLOSE PROXIMITY; COMMON FEATURES; CONFORMATIONAL CHANGE; DNA MOLECULES; DNA-BINDING DOMAIN; GENETIC INFORMATION; HUMAN CHROMOSOMES; MAMMALIAN CELLS; RNASE H; STRUCTURAL DIVERSITY; STRUCTURAL FEATURE; STRUCTURAL SIMILARITY; STRUCTURAL VARIABILITY; STRUCTURE; THREE-DIMENSIONAL STRUCTURE; TRANSPOSASE;

EID: 78649326287     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.addr.2010.06.006     Document Type: Review
Times cited : (58)

References (78)
  • 1
    • 0035822038 scopus 로고    scopus 로고
    • The hemophilias - from royal genes to gene therapy
    • Mannucci P.M., Tuddenham E.G. The hemophilias - from royal genes to gene therapy. N. Eng. J. Med. 2001, 344:1773-1779.
    • (2001) N. Eng. J. Med. , vol.344 , pp. 1773-1779
    • Mannucci, P.M.1    Tuddenham, E.G.2
  • 3
    • 25144492340 scopus 로고    scopus 로고
    • Sleeping beauty transposon-mediated gene therapy for prolonged expression
    • Hackett P.B., Ekker S.C., Largaespada D.A., McIvor R.S. Sleeping beauty transposon-mediated gene therapy for prolonged expression. Adv. Genet. 2005, 54:189-232.
    • (2005) Adv. Genet. , vol.54 , pp. 189-232
    • Hackett, P.B.1    Ekker, S.C.2    Largaespada, D.A.3    McIvor, R.S.4
  • 4
    • 0030662074 scopus 로고    scopus 로고
    • Molecular reconstruction of Sleeping Beauty, a Tc1-like transposon from fish, and its transposition in human cells
    • Ivics Z., Hackett P.B., Plasterk R.H., Izsvak Z. Molecular reconstruction of Sleeping Beauty, a Tc1-like transposon from fish, and its transposition in human cells. Cell 1997, 91:501-510.
    • (1997) Cell , vol.91 , pp. 501-510
    • Ivics, Z.1    Hackett, P.B.2    Plasterk, R.H.3    Izsvak, Z.4
  • 6
    • 0344668818 scopus 로고    scopus 로고
    • The Frog Prince: a reconstructed transposon from Rana pipiens with high transpositional activity in vertebrate cells
    • Miskey C., Izsvak Z., Plasterk R.H., Ivics Z. The Frog Prince: a reconstructed transposon from Rana pipiens with high transpositional activity in vertebrate cells. Nucleic Acids Res. 2003, 31:6873-6881.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6873-6881
    • Miskey, C.1    Izsvak, Z.2    Plasterk, R.H.3    Ivics, Z.4
  • 7
    • 70349356638 scopus 로고    scopus 로고
    • Emerging potential of transposons for gene therapy and generation of induced pluripotent stem cells
    • VandenDriessche T., Ivics Z., Izsvak Z., Chuah M.K. Emerging potential of transposons for gene therapy and generation of induced pluripotent stem cells. Blood 2009, 114:1461-1468.
    • (2009) Blood , vol.114 , pp. 1461-1468
    • VandenDriessche, T.1    Ivics, Z.2    Izsvak, Z.3    Chuah, M.K.4
  • 8
    • 4744374701 scopus 로고    scopus 로고
    • Mutational analysis of the N-terminal DNA-binding domain of sleeping beauty transposase: critical residues for DNA binding and hyperactivity in mammalian cells
    • Yant S.R., Park J., Huang Y., Mikkelsen J.G., Kay M.A. Mutational analysis of the N-terminal DNA-binding domain of sleeping beauty transposase: critical residues for DNA binding and hyperactivity in mammalian cells. Mol. Cell Biol. 2004, 24:9239-9247.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 9239-9247
    • Yant, S.R.1    Park, J.2    Huang, Y.3    Mikkelsen, J.G.4    Kay, M.A.5
  • 9
    • 1342290203 scopus 로고    scopus 로고
    • Development of hyperactive sleeping beauty transposon vectors by mutational analysis
    • Zayed H., Izsvak Z., Walisko O., Ivics Z. Development of hyperactive sleeping beauty transposon vectors by mutational analysis. Mol. Ther. 2004, 9:292-304.
    • (2004) Mol. Ther. , vol.9 , pp. 292-304
    • Zayed, H.1    Izsvak, Z.2    Walisko, O.3    Ivics, Z.4
  • 10
    • 77950525914 scopus 로고    scopus 로고
    • A transposon and transposase system for human application
    • Hackett P.B., Largaespada D.A., Cooper L.J. A transposon and transposase system for human application. Mol. Ther. 2010, 18:674-683.
    • (2010) Mol. Ther. , vol.18 , pp. 674-683
    • Hackett, P.B.1    Largaespada, D.A.2    Cooper, L.J.3
  • 12
    • 59649101866 scopus 로고    scopus 로고
    • Retroviral integrase superfamily: the structural perspective
    • Nowotny M. Retroviral integrase superfamily: the structural perspective. EMBO Rep. 2009, 10:144-151.
    • (2009) EMBO Rep. , vol.10 , pp. 144-151
    • Nowotny, M.1
  • 13
    • 65549105028 scopus 로고    scopus 로고
    • Piecing together the structure of retroviral integrase, an important target in AIDS therapy
    • Jaskolski M., Alexandratos J.N., Bujacz G., Wlodawer A. Piecing together the structure of retroviral integrase, an important target in AIDS therapy. FEBS J. 2009, 276:2926-2946.
    • (2009) FEBS J. , vol.276 , pp. 2926-2946
    • Jaskolski, M.1    Alexandratos, J.N.2    Bujacz, G.3    Wlodawer, A.4
  • 14
    • 0242636324 scopus 로고    scopus 로고
    • The outs and ins of transposition: from mu to kangaroo
    • Curcio M.J., Derbyshire K.M. The outs and ins of transposition: from mu to kangaroo. Nat. Rev. Mol. Cell Biol. 2003, 4:865-877.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 865-877
    • Curcio, M.J.1    Derbyshire, K.M.2
  • 15
    • 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. Nat. Struct. Biol. 2001, 8:302-307.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 302-307
    • Rice, P.A.1    Baker, T.A.2
  • 16
    • 21244451435 scopus 로고    scopus 로고
    • Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis
    • Nowotny M., Gaidamakov S.A., Crouch R.J., Yang W. Crystal structures of RNase H bound to an RNA/DNA hybrid: substrate specificity and metal-dependent catalysis. Cell 2005, 121:1005-1016.
    • (2005) Cell , vol.121 , pp. 1005-1016
    • Nowotny, M.1    Gaidamakov, S.A.2    Crouch, R.J.3    Yang, W.4
  • 19
    • 0026019625 scopus 로고
    • Structural basis for the 3?-5? exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism
    • Beese L.S., Steitz T.A. Structural basis for the 3?-5? exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J. 1991, 10:25-33.
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 20
    • 0028886688 scopus 로고
    • Unity in transposition reactions
    • Craig N.L. Unity in transposition reactions. Science 1995, 270:253-254.
    • (1995) Science , vol.270 , pp. 253-254
    • Craig, N.L.1
  • 21
    • 0026637325 scopus 로고
    • Transpositional recombination: mechanistic insights from studies of mu and other elements
    • Mizuuchi K. Transpositional recombination: mechanistic insights from studies of mu and other elements. Annu. Rev. Biochem. 1992, 61:1011-1051.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1011-1051
    • Mizuuchi, K.1
  • 24
    • 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., Craig N.L. Transposition of hAT elements links transposable elements and V(D)J recombination. Nature 2004, 432:995-1001.
    • (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
  • 25
    • 0034616993 scopus 로고    scopus 로고
    • Three-dimensional structure of the Tn5 synaptic complex transposition intermediate
    • Davies D.R., Goryshin I.Y., Reznikoff W.S., Rayment I. Three-dimensional structure of the Tn5 synaptic complex transposition intermediate. Science 2000, 289:77-85.
    • (2000) Science , vol.289 , pp. 77-85
    • Davies, D.R.1    Goryshin, I.Y.2    Reznikoff, W.S.3    Rayment, I.4
  • 27
    • 0033597135 scopus 로고    scopus 로고
    • The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution
    • Davies D.R., Mahnke Braam L., Reznikoff W.S., Rayment I. The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution. J. Biol. Chem. 1999, 274:11904-11913.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11904-11913
    • Davies, D.R.1    Mahnke Braam, L.2    Reznikoff, W.S.3    Rayment, I.4
  • 29
    • 70149109999 scopus 로고    scopus 로고
    • Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote
    • Richardson J.M., Colloms S.D., Finnegan D.J., Walkinshaw M.D. Molecular architecture of the Mos1 paired-end complex: the structural basis of DNA transposition in a eukaryote. Cell 2009, 138:1096-1108.
    • (2009) Cell , vol.138 , pp. 1096-1108
    • Richardson, J.M.1    Colloms, S.D.2    Finnegan, D.J.3    Walkinshaw, M.D.4
  • 31
    • 0029129435 scopus 로고
    • Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration
    • Rice P., Mizuuchi K. Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Cell 1995, 82:209-220.
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.1    Mizuuchi, K.2
  • 32
    • 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 R.F., Perrakis A., Plasterk R.H., Sixma T.K. Crystal structure of the specific DNA-binding domain of Tc3 transposase of C. elegans in complex with transposon DNA. EMBO J. 1997, 16:6044-6054.
    • (1997) EMBO J. , vol.16 , pp. 6044-6054
    • van Pouderoyen, G.1    Ketting, R.F.2    Perrakis, A.3    Plasterk, R.H.4    Sixma, T.K.5
  • 33
    • 4043107881 scopus 로고    scopus 로고
    • Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA
    • Watkins S., van Pouderoyen G., Sixma T.K. Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA. Nucleic Acids Res. 2004, 32:4306-4312.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4306-4312
    • Watkins, S.1    van Pouderoyen, G.2    Sixma, T.K.3
  • 35
    • 0031464544 scopus 로고    scopus 로고
    • Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains
    • Schumacher S., Clubb R.T., Cai M., Mizuuchi K., Clore G.M., Gronenborn A.M. Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains. EMBO J. 1997, 16:7532-7541.
    • (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
  • 36
    • 0031576325 scopus 로고    scopus 로고
    • Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase
    • Clubb R.T., Schumacher S., Mizuuchi K., Gronenborn A.M., Clore G.M. Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase. J. Mol. Biol. 1997, 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    Clore, G.M.5
  • 37
    • 0025129937 scopus 로고
    • Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein
    • Yang W., Hendrickson W.A., Crouch R.J., Satow Y. Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. Science 1990, 249:1398-1405.
    • (1990) Science , vol.249 , pp. 1398-1405
    • Yang, W.1    Hendrickson, W.A.2    Crouch, R.J.3    Satow, Y.4
  • 39
    • 0032536109 scopus 로고    scopus 로고
    • Mutational analysis of domain II beta of bacteriophage Mu transposase: domains II alpha and II beta belong to different catalytic complementation groups
    • Namgoong S.Y., Kim K., Saxena P., Yang J.Y., Jayaram M., Giedroc D.P., Harshey R.M. Mutational analysis of domain II beta of bacteriophage Mu transposase: domains II alpha and II beta belong to different catalytic complementation groups. J. Mol. Biol. 1998, 275:221-232.
    • (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    Giedroc, D.P.6    Harshey, R.M.7
  • 40
    • 0031010740 scopus 로고    scopus 로고
    • A helix-turn-helix DNA-binding motif predicted for transposases of DNA transposons
    • Pietrokovski S., Henikoff S. A helix-turn-helix DNA-binding motif predicted for transposases of DNA transposons. Mol. Gen. Genet. 1997, 254:689-695.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 689-695
    • Pietrokovski, S.1    Henikoff, S.2
  • 42
    • 0342934743 scopus 로고
    • Structural domains in phage Mu transposase: identification of the site-specific DNA-binding domain
    • Nakayama C., Teplow D.B., Harshey R.M. Structural domains in phage Mu transposase: identification of the site-specific DNA-binding domain. Proc. Nat. Acad. Sci. U.S.A. 1987, 84:1809-1813.
    • (1987) Proc. Nat. Acad. Sci. U.S.A. , vol.84 , pp. 1809-1813
    • Nakayama, C.1    Teplow, D.B.2    Harshey, R.M.3
  • 44
    • 0028608962 scopus 로고
    • DNA binding activities of the Caenorhabditis elegans Tc3 transposase
    • Colloms S.D., van Luenen H.G., Plasterk R.H. DNA binding activities of the Caenorhabditis elegans Tc3 transposase. Nucleic Acids Res. 1994, 22:5548-5554.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5548-5554
    • Colloms, S.D.1    van Luenen, H.G.2    Plasterk, R.H.3
  • 45
    • 0027426925 scopus 로고
    • DNA sequence recognition by Pax proteins: bipartite structure of the paired domain and its binding site
    • Czerny T., Schaffner G., Busslinger M. DNA sequence recognition by Pax proteins: bipartite structure of the paired domain and its binding site. Genes Dev. 1993, 7:2048-2061.
    • (1993) Genes Dev. , vol.7 , pp. 2048-2061
    • Czerny, T.1    Schaffner, G.2    Busslinger, M.3
  • 46
    • 0037072818 scopus 로고    scopus 로고
    • Involvement of a bifunctional, paired-like DNA-binding domain and a transpositional enhancer in Sleeping Beauty transposition
    • Izsvak Z., Khare D., Behlke J., Heinemann U., Plasterk R.H., Ivics Z. Involvement of a bifunctional, paired-like DNA-binding domain and a transpositional enhancer in Sleeping Beauty transposition. J. Biol. Chem. 2002, 277:34581-34588.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34581-34588
    • Izsvak, Z.1    Khare, D.2    Behlke, J.3    Heinemann, U.4    Plasterk, R.H.5    Ivics, Z.6
  • 47
    • 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. The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site. Cell 1996, 84:223-233.
    • (1996) Cell , vol.84 , pp. 223-233
    • Bolland, S.1    Kleckner, N.2
  • 48
    • 0029143391 scopus 로고
    • Identification and characterization of a pre-cleavage synaptic complex that is an early intermediate in Tn10 transposition
    • Sakai J., Chalmers R.M., Kleckner N. Identification and characterization of a pre-cleavage synaptic complex that is an early intermediate in Tn10 transposition. EMBO J. 1995, 14:4374-4383.
    • (1995) EMBO J. , vol.14 , pp. 4374-4383
    • Sakai, J.1    Chalmers, R.M.2    Kleckner, N.3
  • 49
    • 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 B.D., Chan B.S., Allison R.G., Chaconas G. 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. 1991, 10:3051-3059.
    • (1991) EMBO J. , vol.10 , pp. 3051-3059
    • Lavoie, B.D.1    Chan, B.S.2    Allison, R.G.3    Chaconas, G.4
  • 50
    • 0026708067 scopus 로고
    • Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition
    • Mizuuchi M., Baker T.A., Mizuuchi K. Assembly of the active form of the transposase-Mu DNA complex: a critical control point in Mu transposition. Cell 1992, 70:303-311.
    • (1992) Cell , vol.70 , pp. 303-311
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 51
    • 17044421342 scopus 로고    scopus 로고
    • 3D reconstruction of the Mu transposase and the Type 1 transpososome: a structural framework for Mu DNA transposition
    • Yuan J.F., Beniac D.R., Chaconas G., Ottensmeyer F.P. 3D reconstruction of the Mu transposase and the Type 1 transpososome: a structural framework for Mu DNA transposition. Genes Dev. 2005, 19:840-852.
    • (2005) Genes Dev. , vol.19 , pp. 840-852
    • Yuan, J.F.1    Beniac, D.R.2    Chaconas, G.3    Ottensmeyer, F.P.4
  • 53
    • 4444295114 scopus 로고    scopus 로고
    • Early intermediates of mariner transposition: catalysis without synapsis of the transposon ends suggests a novel architecture of the synaptic complex
    • Lipkow K., Buisine N., Lampe D.J., Chalmers R. Early intermediates of mariner transposition: catalysis without synapsis of the transposon ends suggests a novel architecture of the synaptic complex. Mol. Cell Biol. 2004, 24:8301-8311.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 8301-8311
    • Lipkow, K.1    Buisine, N.2    Lampe, D.J.3    Chalmers, R.4
  • 54
    • 0036317929 scopus 로고    scopus 로고
    • Structure-function analysis of the inverted terminal repeats of the sleeping beauty transposon
    • Cui Z., Geurts A.M., Liu G., Kaufman C.D., Hackett P.B. Structure-function analysis of the inverted terminal repeats of the sleeping beauty transposon. J. Mol. Biol. 2002, 318:1221-1235.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1221-1235
    • Cui, Z.1    Geurts, A.M.2    Liu, G.3    Kaufman, C.D.4    Hackett, P.B.5
  • 55
    • 34247491578 scopus 로고    scopus 로고
    • Assembly of the Tc1 and mariner transposition initiation complexes depends on the origins of their transposase DNA binding domains
    • Brillet B., Bigot Y., Auge-Gouillou C. Assembly of the Tc1 and mariner transposition initiation complexes depends on the origins of their transposase DNA binding domains. Genetica 2007, 130:105-120.
    • (2007) Genetica , vol.130 , pp. 105-120
    • Brillet, B.1    Bigot, Y.2    Auge-Gouillou, C.3
  • 57
  • 59
    • 0029871975 scopus 로고    scopus 로고
    • The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis
    • Aldaz H., Schuster E., Baker T.A. The interwoven architecture of the Mu transposase couples DNA synapsis to catalysis. Cell 1996, 85:257-269.
    • (1996) Cell , vol.85 , pp. 257-269
    • Aldaz, H.1    Schuster, E.2    Baker, T.A.3
  • 60
    • 0029986753 scopus 로고    scopus 로고
    • Mu transpositional recombination: donor DNA cleavage and strand transfer in trans by the Mu transposase
    • Savilahti H., Mizuuchi K. Mu transpositional recombination: donor DNA cleavage and strand transfer in trans by the Mu transposase. Cell 1996, 85:271-280.
    • (1996) Cell , vol.85 , pp. 271-280
    • Savilahti, H.1    Mizuuchi, K.2
  • 61
    • 0035168323 scopus 로고    scopus 로고
    • The DDE motif in RAG-1 is contributed in trans to a single active site that catalyzes the nicking and transesterification steps of V(D)J recombination
    • Swanson P.C. The DDE motif in RAG-1 is contributed in trans to a single active site that catalyzes the nicking and transesterification steps of V(D)J recombination. Mol. Cell Biol. 2001, 21:449-458.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 449-458
    • Swanson, P.C.1
  • 62
    • 0023663468 scopus 로고
    • Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA
    • Surette M.G., Buch S.J., Chaconas G. Transpososomes: stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA. Cell 1987, 49:253-262.
    • (1987) Cell , vol.49 , pp. 253-262
    • Surette, M.G.1    Buch, S.J.2    Chaconas, G.3
  • 63
    • 0035898687 scopus 로고    scopus 로고
    • Protein-DNA contacts and conformational changes in the Tn10 transpososome during assembly and activation for cleavage
    • Crellin P., Chalmers R. Protein-DNA contacts and conformational changes in the Tn10 transpososome during assembly and activation for cleavage. EMBO J. 2001, 20:3882-3891.
    • (2001) EMBO J. , vol.20 , pp. 3882-3891
    • Crellin, P.1    Chalmers, R.2
  • 64
    • 0033380262 scopus 로고    scopus 로고
    • Studies on a "jumping gene machine": higher-order nucleoprotein complexes in Mu DNA transposition
    • Chaconas G. Studies on a "jumping gene machine": higher-order nucleoprotein complexes in Mu DNA transposition. Biochem. Cell Biol. 1999, 77:487-491.
    • (1999) Biochem. Cell Biol. , vol.77 , pp. 487-491
    • Chaconas, G.1
  • 66
    • 0033569428 scopus 로고    scopus 로고
    • Organization and dynamics of the Mu transpososome: recombination by communication between two active sites
    • Williams T.L., Jackson E.L., Carritte A., Baker T.A. Organization and dynamics of the Mu transpososome: recombination by communication between two active sites. Genes Dev. 1999, 13:2725-2737.
    • (1999) Genes Dev. , vol.13 , pp. 2725-2737
    • Williams, T.L.1    Jackson, E.L.2    Carritte, A.3    Baker, T.A.4
  • 67
  • 68
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases
    • Dyda F., Hickman A.B., Jenkins T.M., Engelman A., Craigie R., Davies D.R. Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases. Science 1994, 266:1981-1986.
    • (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
  • 69
    • 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 Z.L., Clement-Mella C., Wlodawer A. The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant. FEBS Lett. 1996, 398:175-178.
    • (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
  • 70
    • 0033551443 scopus 로고    scopus 로고
    • The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity
    • Greenwald J., Le V., Butler S.L., Bushman F.D., Choe S. The mobility of an HIV-1 integrase active site loop is correlated with catalytic activity. Biochemistry 1999, 38:8892-8898.
    • (1999) Biochemistry , vol.38 , pp. 8892-8898
    • Greenwald, J.1    Le, V.2    Butler, S.L.3    Bushman, F.D.4    Choe, S.5
  • 73
    • 17844406393 scopus 로고    scopus 로고
    • Large-scale conformational dynamics of the HIV-1 integrase core domain and its catalytic loop mutants
    • Lee M.C., Deng J., Briggs J.M., Duan Y. Large-scale conformational dynamics of the HIV-1 integrase core domain and its catalytic loop mutants. Biophys J. 2005, 88:3133-3146.
    • (2005) Biophys J. , vol.88 , pp. 3133-3146
    • Lee, M.C.1    Deng, J.2    Briggs, J.M.3    Duan, Y.4
  • 74
    • 0035170973 scopus 로고    scopus 로고
    • The Mu repressor-DNA complex contains an immobilized 'wing' within the minor groove
    • Wojciak J.M., Iwahara J., Clubb R.T. The Mu repressor-DNA complex contains an immobilized 'wing' within the minor groove. Nat. Struct. Biol. 2001, 8:84-90.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 84-90
    • Wojciak, J.M.1    Iwahara, J.2    Clubb, R.T.3
  • 75
    • 0036192889 scopus 로고    scopus 로고
    • DNA-binding interactions and conformational fluctuations of Tc3 transposase DNA binding domain examined with single molecule fluorescence spectroscopy
    • Daniel D.C., Thompson M., Woodbury N.W. DNA-binding interactions and conformational fluctuations of Tc3 transposase DNA binding domain examined with single molecule fluorescence spectroscopy. Biophys. J. 2002, 82:1654-1666.
    • (2002) Biophys. J. , vol.82 , pp. 1654-1666
    • Daniel, D.C.1    Thompson, M.2    Woodbury, N.W.3
  • 76
    • 0034651857 scopus 로고    scopus 로고
    • Tn10 transpososome assembly involves a folded intermediate that must be unfolded for target capture and strand transfer
    • Sakai J.S., Kleckner N., Yang X., Guhathakurta A. Tn10 transpososome assembly involves a folded intermediate that must be unfolded for target capture and strand transfer. EMBO J. 2000, 19:776-785.
    • (2000) EMBO J. , vol.19 , pp. 776-785
    • Sakai, J.S.1    Kleckner, N.2    Yang, X.3    Guhathakurta, A.4
  • 77
    • 33750848802 scopus 로고    scopus 로고
    • Transpososome dynamics and regulation in Tn10 transposition
    • Haniford D.B. Transpososome dynamics and regulation in Tn10 transposition. Crit. Rev. Biochem. Mol. Biol. 2006, 41:407-424.
    • (2006) Crit. Rev. Biochem. Mol. Biol. , vol.41 , pp. 407-424
    • Haniford, D.B.1
  • 78
    • 0031026571 scopus 로고    scopus 로고
    • Mutations in the mariner transposase: the D, D(35)E consensus sequence is nonfunctional
    • Lohe A.R., De Aguiar D., Hartl D.L. Mutations in the mariner transposase: the D, D(35)E consensus sequence is nonfunctional. Proc. Nat. Acad. Sci. U.S.A. 1997, 94:1293-1297.
    • (1997) Proc. Nat. Acad. Sci. U.S.A. , vol.94 , pp. 1293-1297
    • Lohe, A.R.1    De Aguiar, D.2    Hartl, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.