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Volumn 14, Issue 1, 2004, Pages 50-57

Structure/function insights into Tn5 transposition

Author keywords

Base pairs; bp; IE; Inside end; Non transferred strand; NTS; OE; Outside end; p csc; Post cleavage synaptic complex; Tn5; Tnp; Transferred strand; Transposase; Transposon 5; TS

Indexed keywords

TRANSPOSASE;

EID: 1342324024     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.01.008     Document Type: Review
Times cited : (75)

References (40)
  • 3
    • 0020523675 scopus 로고
    • DNA sequences at the ends of transposon Tn5 required for transposition
    • Johnson R.C., Reznikoff W.S. DNA sequences at the ends of transposon Tn5 required for transposition. Nature. 304:1983;280-282.
    • (1983) Nature , vol.304 , pp. 280-282
    • Johnson, R.C.1    Reznikoff, W.S.2
  • 4
    • 0021645751 scopus 로고
    • Role of the IS50 R proteins in the promotion and control of Tn5 transposition
    • Johnson R.C., Reznikoff W.S. Role of the IS50 R proteins in the promotion and control of Tn5 transposition. J. Mol. Biol. 177:1984;645-661.
    • (1984) J. Mol. Biol. , vol.177 , pp. 645-661
    • Johnson, R.C.1    Reznikoff, W.S.2
  • 5
    • 0020196971 scopus 로고
    • Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat
    • Johnson R.C., Yin J.C., Reznikoff W.S. Control of Tn5 transposition in Escherichia coli is mediated by protein from the right repeat. Cell. 30:1982;873-882.
    • (1982) Cell , vol.30 , pp. 873-882
    • Johnson, R.C.1    Yin, J.C.2    Reznikoff, W.S.3
  • 6
    • 0020197982 scopus 로고
    • Regulation of Tn5 by the right-repeat proteins: Control at the level of the transposition reaction?
    • Isberg R.R., Lazaar A.L., Syvanen M. Regulation of Tn5 by the right-repeat proteins: control at the level of the transposition reaction? Cell. 30:1982;883-892.
    • (1982) Cell , vol.30 , pp. 883-892
    • Isberg, R.R.1    Lazaar, A.L.2    Syvanen, M.3
  • 7
    • 0027380688 scopus 로고
    • Characterization of the Tn5 transposase and inhibitor proteins: A model for the inhibition of transposition
    • de la Cruz N.B., Weinreich M.D., Wiegand T.W., Krebs M.P., Reznikoff W.S. Characterization of the Tn5 transposase and inhibitor proteins: a model for the inhibition of transposition. J. Bacteriol. 175:1993;6932-6938.
    • (1993) J. Bacteriol. , vol.175 , pp. 6932-6938
    • De La Cruz, N.B.1    Weinreich, M.D.2    Wiegand, T.W.3    Krebs, M.P.4    Reznikoff, W.S.5
  • 8
    • 0032946089 scopus 로고    scopus 로고
    • A mechanism for Tn5 inhibition. Carboxyl-terminal dimerization
    • Braam L.A., Goryshin I.Y., Reznikoff W.S. A mechanism for Tn5 inhibition. carboxyl-terminal dimerization. J. Biol. Chem. 274:1999;86-92.
    • (1999) J. Biol. Chem. , vol.274 , pp. 86-92
    • Braam, L.A.1    Goryshin, I.Y.2    Reznikoff, W.S.3
  • 9
    • 85157999571 scopus 로고    scopus 로고
    • Tn5 transposition
    • Edited by Craig N, Craigie R, Gellert M, Lambowitz AM. Washington, DC: American Society of Microbiology
    • Reznikoff WS: Tn5 transposition. In Mobile DNA II. Edited by Craig N, Craigie R, Gellert M, Lambowitz AM. Washington, DC: American Society of Microbiology; 2002:403-421.
    • (2002) Mobile DNA II , pp. 403-421
    • Reznikoff, W.S.1
  • 11
    • 0028059193 scopus 로고
    • A functional analysis of the Tn5 transposase. Identification of domains required for DNA binding and multimerization
    • Weinreich M.D., Mahnke-Braam L., Reznikoff W.S. A functional analysis of the Tn5 transposase. Identification of domains required for DNA binding and multimerization. J. Mol. Biol. 241:1994;166-177.
    • (1994) J. Mol. Biol. , vol.241 , pp. 166-177
    • Weinreich, M.D.1    Mahnke-Braam, L.2    Reznikoff, W.S.3
  • 12
    • 0028113015 scopus 로고
    • Evidence that the cis preference of the Tn5 transposase is caused by nonproductive multimerization
    • Weinreich M.D., Gasch A., Reznikoff W.S. Evidence that the cis preference of the Tn5 transposase is caused by nonproductive multimerization. Genes Dev. 8:1994;2363-2374.
    • (1994) Genes Dev. , vol.8 , pp. 2363-2374
    • Weinreich, M.D.1    Gasch, A.2    Reznikoff, W.S.3
  • 13
    • 0034616993 scopus 로고    scopus 로고
    • Three-dimensional structure of the Tn5 synaptic complex transposition intermediate
    • The authors present the X-ray co-crystal structure of Tn5 Tnp with bound OE DNA. This is, to date, the most complete structure of any protein from the transposase/retroviral integrase superfamily of proteins and was the first protein-DNA co-crystal structure to be elucidated for this family. All aspects of the co-crystal structure are discussed.
    • Davies D.R., Goryshin I.Y., Reznikoff W.S., Rayment I. Three-dimensional structure of the Tn5 synaptic complex transposition intermediate. Science. 289:2000;77-85 The authors present the X-ray co-crystal structure of Tn5 Tnp with bound OE DNA. This is, to date, the most complete structure of any protein from the transposase/retroviral integrase superfamily of proteins and was the first protein-DNA co-crystal structure to be elucidated for this family. All aspects of the co-crystal structure are discussed.
    • (2000) Science , vol.289 , pp. 77-85
    • Davies, D.R.1    Goryshin, I.Y.2    Reznikoff, W.S.3    Rayment, I.4
  • 14
    • 0033597135 scopus 로고    scopus 로고
    • The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution
    • Davies D.R., Braam L.M., Reznikoff W.S., Rayment I. The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-A resolution. J. Biol. Chem. 274:1999;11904-11913.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11904-11913
    • Davies, D.R.1    Braam, L.M.2    Reznikoff, W.S.3    Rayment, I.4
  • 17
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247:1995;536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 18
    • 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. 82:1995;209-220.
    • (1995) Cell , vol.82 , pp. 209-220
    • Rice, P.1    Mizuuchi, K.2
  • 20
    • 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., Katz R.A., Skalka A.M. The catalytic domain of avian sarcoma virus integrase: conformation of the active-site residues in the presence of divalent cations. Structure. 4:1996;89-96.
    • (1996) Structure , vol.4 , pp. 89-96
    • Bujacz, G.1    Jaskolski, M.2    Alexandratos, J.3    Wlodawer, A.4    Merkel, G.5    Katz, R.A.6    Skalka, A.M.7
  • 22
    • 0031583470 scopus 로고    scopus 로고
    • Tn5 transposase mutants that alter DNA binding specificity
    • Zhou M., Reznikoff W.S. Tn5 transposase mutants that alter DNA binding specificity. J. Mol. Biol. 271:1997;362-373.
    • (1997) J. Mol. Biol. , vol.271 , pp. 362-373
    • Zhou, M.1    Reznikoff, W.S.2
  • 23
    • 0036134777 scopus 로고    scopus 로고
    • Tn5 transposase with an altered specificity for transposon ends
    • Naumann T.A., Reznikoff W.S. Tn5 transposase with an altered specificity for transposon ends. J. Bacteriol. 184:2002;233-240.
    • (2002) J. Bacteriol. , vol.184 , pp. 233-240
    • Naumann, T.A.1    Reznikoff, W.S.2
  • 24
    • 0035933813 scopus 로고    scopus 로고
    • Functional characterization of arginine 30, lysine 40, and arginine 62 in Tn5 transposase
    • Twining S.S., Goryshin I.Y., Bhasin A., Reznikoff W.S. Functional characterization of arginine 30, lysine 40, and arginine 62 in Tn5 transposase. J. Biol. Chem. 276:2001;23135-23143.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23135-23143
    • Twining, S.S.1    Goryshin, I.Y.2    Bhasin, A.3    Reznikoff, W.S.4
  • 25
    • 0034725642 scopus 로고    scopus 로고
    • The C-terminal alpha helix of Tn5 transposase is required for synaptic complex formation
    • Steiniger-White M., Reznikoff W.S. The C-terminal alpha helix of Tn5 transposase is required for synaptic complex formation. J. Biol. Chem. 275:2000;23127-23133.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23127-23133
    • Steiniger-White, M.1    Reznikoff, W.S.2
  • 27
    • 0037124064 scopus 로고    scopus 로고
    • Tn5 transposase active site mutants
    • Naumann T.A., Reznikoff W.S. Tn5 transposase active site mutants. J. Biol. Chem. 277:2002;17623-17629.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17623-17629
    • Naumann, T.A.1    Reznikoff, W.S.2
  • 28
    • 0037449821 scopus 로고    scopus 로고
    • Tn5 transposase active site mutations suggest position of donor backbone DNA in synaptic complex
    • Peterson G., Reznikoff W. Tn5 transposase active site mutations suggest position of donor backbone DNA in synaptic complex. J. Biol. Chem. 278:2003;1904-1909.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1904-1909
    • Peterson, G.1    Reznikoff, W.2
  • 29
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas S., Kumar S., Roberts R.J., Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell. 76:1994;357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 30
    • 0036443973 scopus 로고    scopus 로고
    • A base-flipping mechanism for the T4 phage beta-glucosyltransferase and identification of a transition-state analog
    • Lariviere L., Morera S. A base-flipping mechanism for the T4 phage beta-glucosyltransferase and identification of a transition-state analog. J. Mol. Biol. 324:2002;483-490.
    • (2002) J. Mol. Biol. , vol.324 , pp. 483-490
    • Lariviere, L.1    Morera, S.2
  • 31
    • 0036431531 scopus 로고    scopus 로고
    • Role of base flipping in specific recognition of damaged DNA by repair enzymes
    • Fuxreiter M., Luo N., Jedlovszky P., Simon I., Osman R. Role of base flipping in specific recognition of damaged DNA by repair enzymes. J. Mol. Biol. 323:2002;823-834.
    • (2002) J. Mol. Biol. , vol.323 , pp. 823-834
    • Fuxreiter, M.1    Luo, N.2    Jedlovszky, P.3    Simon, I.4    Osman, R.5
  • 33
    • 0037192801 scopus 로고    scopus 로고
    • Mutational analysis of the base flipping event found in Tn5 transposition
    • Ason B., Reznikoff W.S. Mutational analysis of the base flipping event found in Tn5 transposition. J. Biol. Chem. 277:2002;11284-11291.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11284-11291
    • Ason, B.1    Reznikoff, W.S.2
  • 34
    • 0032571245 scopus 로고    scopus 로고
    • Structural principles for the inhibition of the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates
    • Brautigam C.A., Steitz T.A. Structural principles for the inhibition of the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I by phosphorothioates. J. Mol. Biol. 277:1998;363-377.
    • (1998) J. Mol. Biol. , vol.277 , pp. 363-377
    • Brautigam, C.A.1    Steitz, T.A.2
  • 35
    • 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. 10:1991;25-33.
    • (1991) EMBO. J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 39
    • 0025899314 scopus 로고
    • Inversion of phosphate chirality at the target site of Mu DNA strand transfer: Evidence for a one-step transesterification mechanism
    • Mizuuchi K., Adzuman K. Inversion of phosphate chirality at the target site of Mu DNA strand transfer: evidence for a one-step transesterification mechanism. Cell. 66:1991;129-140.
    • (1991) Cell , vol.66 , pp. 129-140
    • Mizuuchi, K.1    Adzuman, K.2
  • 40
    • 0037336665 scopus 로고    scopus 로고
    • Tn5 as a model for understanding DNA transposition
    • Reznikoff W.S. Tn5 as a model for understanding DNA transposition. Mol. Microbiol. 47:2003;1199-1206.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1199-1206
    • Reznikoff, W.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.