메뉴 건너뛰기




Volumn 274, Issue 4, 1997, Pages 491-504

Defining functional regions of the IS903 transposase

Author keywords

Catalytic residues; DNA transposition; DNA binding protein; Functional domains; Transposase

Indexed keywords

DNA; DNA BINDING PROTEIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MUTANT PROTEIN; TRANSPOSASE;

EID: 0031565988     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1410     Document Type: Article
Times cited : (16)

References (52)
  • 1
    • 0021362101 scopus 로고
    • Cleavage of the site-specific recombination protein gamma delta resolvase: The smaller of two fragments binds DNA specifically
    • Abdel-Meguid S. S., Grindley N. D., Templeton N. S., Steitz T. A. Cleavage of the site-specific recombination protein gamma delta resolvase: the smaller of two fragments binds DNA specifically. Proc. Natl Acad. Sci. USA. 81:1984;2001-2005.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2001-2005
    • Abdel-Meguid, S.S.1    Grindley, N.D.2    Templeton, N.S.3    Steitz, T.A.4
  • 2
    • 0028317055 scopus 로고
    • Identification of residues in the Mu transposase essential for catalysis
    • Baker T. A., Luo L. Identification of residues in the Mu transposase essential for catalysis. Proc. Natl Acad. Sci. USA. 91:1994;6654-6658.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6654-6658
    • Baker, T.A.1    Luo, L.2
  • 3
    • 0030050236 scopus 로고    scopus 로고
    • The three chemical steps of Tn1010
    • Bolland S., Kleckner N. The three chemical steps of Tn1010. Cell. 84:1996;223-233.
    • (1996) Cell , vol.84 , pp. 223-233
    • Bolland, S.1    Kleckner, N.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 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
  • 8
    • 0030199188 scopus 로고    scopus 로고
    • DNA transposition: Jumping gene machine, some assembly required
    • Chaconas G., Lavoie B. D., Watson M. A. DNA transposition: jumping gene machine, some assembly required. Curr. Biol. 6:1996;817-820.
    • (1996) Curr. Biol. , vol.6 , pp. 817-820
    • Chaconas, G.1    Lavoie, B.D.2    Watson, M.A.3
  • 9
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou P. Y., Fasman G. D. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47:1978;251-276.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 11
    • 85030303669 scopus 로고    scopus 로고
    • Transposition
    • Washington: American Society for Microbiology
    • Craig N. L. Transposition. InandCellular and Molecular Biology. 1996;American Society for Microbiology, Washington.
    • (1996) InandCellular and Molecular Biology
    • Craig, N.L.1
  • 12
    • 0026784161 scopus 로고
    • Binding of the IS903invitro
    • Derbyshire K. M., Grindley N. D. Binding of the IS903invitro. EMBO J. 11:1992;3449-3455.
    • (1992) EMBO J. , vol.11 , pp. 3449-3455
    • Derbyshire, K.M.1    Grindley, N.D.2
  • 14
    • 0023449783 scopus 로고
    • Genetic analysis of the interaction of the insertion sequence IS903
    • Derbyshire K. M., Hwang L., Grindley N. D. Genetic analysis of the interaction of the insertion sequence IS903. Proc. Natl Acad. Sci. USA. 84:1987;8049-8053.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8049-8053
    • Derbyshire, K.M.1    Hwang, L.2    Grindley, N.D.3
  • 15
    • 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. 266:1994;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
  • 16
    • 0001522673 scopus 로고
    • Starch-gel electrophoresis - application to the classification of pituitary proteins and polypeptides
    • Ferguson K. A. Starch-gel electrophoresis - application to the classification of pituitary proteins and polypeptides. Metabolism. 13:1964;985-1002.
    • (1964) Metabolism , vol.13 , pp. 985-1002
    • Ferguson, K.A.1
  • 17
    • 0025825895 scopus 로고
    • Modular structure of transcription factors: Implications for gene regulation
    • Frankel A. D., Kim P. S. Modular structure of transcription factors: implications for gene regulation. Cell. 65:1991;717-719.
    • (1991) Cell , vol.65 , pp. 717-719
    • Frankel, A.D.1    Kim, P.S.2
  • 18
    • 0019510123 scopus 로고
    • Analysis of the structure and function of the kanamycin-resistance transposon Tn903
    • Grindley N., Joyce C. M. Analysis of the structure and function of the kanamycin-resistance transposon Tn903. Cold Spring Harbor Symp. Quant. Biol. 45:1981;125-133.
    • (1981) Cold Spring Harbor Symp. Quant. Biol. , vol.45 , pp. 125-133
    • Grindley, N.1    Joyce, C.M.2
  • 19
    • 0029609126 scopus 로고
    • DNA transposition: From a black box to a color monitor
    • Grindley N. D., Leschziner A. E. DNA transposition: from a black box to a color monitor. Cell. 83:1995;1063-1066.
    • (1995) Cell , vol.83 , pp. 1063-1066
    • Grindley, N.D.1    Leschziner, A.E.2
  • 21
    • 0026752686 scopus 로고
    • PCR-generated probes for the study of DNA-protein interactions
    • Hooft van Huijsduijen R. A. M. PCR-generated probes for the study of DNA-protein interactions. BioTechniques. 12:1992;830-832.
    • (1992) BioTechniques , vol.12 , pp. 830-832
    • Hooft Van Huijsduijen, R.A.M.1
  • 22
    • 0029960810 scopus 로고    scopus 로고
    • Isolation and characterization of IS10
    • Kennedy A. K., Haniford D. B. Isolation and characterization of IS10. J. Mol. Biol. 256:1996;533-547.
    • (1996) J. Mol. Biol. , vol.256 , pp. 533-547
    • Kennedy, A.K.1    Haniford, D.B.2
  • 23
    • 0028883476 scopus 로고
    • Mutational analysis of theatt
    • Kim K., Harshey R. M. Mutational analysis of theatt. Nucl. Acids Res. 23:1995;3937-3943.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 3937-3943
    • Kim, K.1    Harshey, R.M.2
  • 24
    • 0028883169 scopus 로고
    • Step-arrest mutants of phage Mu transposase. Implications in DNA-protein assembly, Mu end cleavage, and strand transfer
    • Kim K., Namgoong S. Y., Jayaram M., Harshey R. M. Step-arrest mutants of phage Mu transposase. Implications in DNA-protein assembly, Mu end cleavage, and strand transfer. J. Biol. Chem. 270:1995;1472-1479.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1472-1479
    • Kim, K.1    Namgoong, S.Y.2    Jayaram, M.3    Harshey, R.M.4
  • 25
    • 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 K. S., Katz R. A., Mack J. P., Skalka A. M. 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. 12:1992;2331-2338.
    • (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
  • 26
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel T. A., Bebenek K., McClary J. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204:1991;125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 28
    • 0024602375 scopus 로고
    • Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer
    • Leung P. C., Teplow D. B., Harshey R. M. Interaction of distinct domains in Mu transposase with Mu DNA ends and an internal transpositional enhancer. Nature. 338:1989;656-658.
    • (1989) Nature , vol.338 , pp. 656-658
    • Leung, P.C.1    Teplow, D.B.2    Harshey, R.M.3
  • 29
    • 0030908043 scopus 로고    scopus 로고
    • ClpX and MuB interact with overlapping regions of Mu transposase: Implications for control of the transposition pathway
    • Levchenko I., Yamauchi M., Baker T. A. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11:1997;1561-1572.
    • (1997) Genes Dev. , vol.11 , pp. 1561-1572
    • Levchenko, I.1    Yamauchi, M.2    Baker, T.A.3
  • 31
    • 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. 61:1992a;1011-1051.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1011-1051
    • Mizuuchi, K.1
  • 32
    • 0026799383 scopus 로고
    • Polynucleotidyl transfer reactions in transpositional DNA recombination
    • Mizuuchi K. Polynucleotidyl transfer reactions in transpositional DNA recombination. J. Biol. Chem. 267:1992b;21273-21276.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21273-21276
    • Mizuuchi, K.1
  • 33
    • 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. 70:1992;303-311.
    • (1992) Cell , vol.70 , pp. 303-311
    • Mizuuchi, M.1    Baker, T.A.2    Mizuuchi, K.3
  • 35
    • 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. Natl Acad. Sci. USA. 84:1987;1809-1813.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 1809-1813
    • Nakayama, C.1    Teplow, D.B.2    Harshey, R.M.3
  • 36
    • 0029144601 scopus 로고
    • Gibbs motif sampling: Detection of bacterial outer membrane protein repeats
    • Neuwald A. F., Liu J. S., Lawrence C. E. Gibbs motif sampling: Detection of bacterial outer membrane protein repeats. Protein Sci. 4:1995;1618-1632.
    • (1995) Protein Sci. , vol.4 , pp. 1618-1632
    • Neuwald, A.F.1    Liu, J.S.2    Lawrence, C.E.3
  • 37
    • 0027172331 scopus 로고
    • An EMSA-based method for determining the molecular weight of a protein-DNA complex
    • Orchard K., May G. E. An EMSA-based method for determining the molecular weight of a protein-DNA complex. Nucl. Acids Res. 21:1993;3335-3336.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 3335-3336
    • Orchard, K.1    May, G.E.2
  • 38
    • 0028928168 scopus 로고
    • Bacterial transposases and retroviral integrases
    • Polard P., Chandler M. Bacterial transposases and retroviral integrases. Mol. Microbiol. 15:1995;13-23.
    • (1995) Mol. Microbiol. , vol.15 , pp. 13-23
    • Polard, P.1    Chandler, M.2
  • 40
    • 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
  • 42
    • 0029861360 scopus 로고    scopus 로고
    • Two classes of Tn1010
    • Sakai J., Kleckner N. Two classes of Tn1010. Genetics. 144:1996;861-870.
    • (1996) Genetics , vol.144 , pp. 861-870
    • Sakai, J.1    Kleckner, N.2
  • 43
    • 0029143391 scopus 로고
    • Identification and characterization of a pre-cleavage synaptic complex that is an early intermediate in Tn10
    • Sakai J., Chalmers R. M., Kleckner N. Identification and characterization of a pre-cleavage synaptic complex that is an early intermediate in Tn10. EMBO J. 14:1995;4374-4383.
    • (1995) EMBO J. , vol.14 , pp. 4374-4383
    • Sakai, J.1    Chalmers, R.M.2    Kleckner, N.3
  • 45
    • 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. The N-terminal domain of the insertion sequence 30 transposase interacts specifically with the terminal inverted repeats of the element. J. Biol. Chem. 265:1990;3757-3762.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3757-3762
    • Stalder, R.1    Caspers, P.2    Olasz, F.3    Arber, W.4
  • 46
    • 0027429846 scopus 로고
    • Single amino acid substitutions uncouple the DNA binding and strand scission activities ofFok
    • Waugh D. S., Sauer R. T. Single amino acid substitutions uncouple the DNA binding and strand scission activities ofFok. Proc. Natl Acad. Sci. USA. 90:1993;9596-9600.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9596-9600
    • Waugh, D.S.1    Sauer, R.T.2
  • 49
    • 0021268779 scopus 로고
    • The locus of sequence-directed and protein-induced DNA bending
    • Wu H-M., Crothers D. M. The locus of sequence-directed and protein-induced DNA bending. Nature. 308:1984;509-513.
    • (1984) Nature , vol.308 , pp. 509-513
    • Wu, H.-M.1    Crothers, D.M.2
  • 50
    • 0028034518 scopus 로고
    • Characterization of a region in phage Mu transposase that is involved in interaction with the MuB protein
    • Wu Z., Chaconas G. Characterization of a region in phage Mu transposase that is involved in interaction with the MuB protein. J. Biol. Chem. 269:1994;28829-28833.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28829-28833
    • Wu, Z.1    Chaconas, G.2
  • 51
    • 0029789247 scopus 로고    scopus 로고
    • Purification and biochemical analyses of a monomeric form of Tn5
    • York D., Reznikoff W. S. Purification and biochemical analyses of a monomeric form of Tn5. Nucl. Acids Res. 24:1996;3790-3796.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 3790-3796
    • York, D.1    Reznikoff, W.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.