메뉴 건너뛰기




Volumn 324, Issue 4, 2002, Pages 649-665

Attenuating functions of the C terminus of λ integrase

Author keywords

att sites; Integrase, topoisomerase; Protein DNA interactions; Site specific recombination

Indexed keywords

ALANINE; CORE PROTEIN; DNA TOPOISOMERASE; INTEGRASE; ISOLEUCINE; LYSINE; METHIONINE; MUTANT PROTEIN; TRYPTOPHAN; TYROSINE; VALINE; VIRUS ENZYME;

EID: 0036923312     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01108-7     Document Type: Article
Times cited : (21)

References (65)
  • 1
    • 0001931646 scopus 로고    scopus 로고
    • λ Int and the λ Int family
    • Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A., eds, ASM Press, Washington, DC
    • Azaro, M. A. & Landy, A. (2002). λ Int and the λ Int family. In Mobile DNA II (Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A., eds), pp. 118-148, ASM Press, Washington, DC.
    • (2002) Mobile DNA II , pp. 118-148
    • Azaro, M.A.1    Landy, A.2
  • 2
    • 0024295418 scopus 로고
    • Autonomous DNA binding domains of λ integrase recognize different sequence families
    • Moitoso de Vargas, L., Pargellis, C. A., Hasan, N. M., Bushman, E. W. & Landy, A. (1988). Autonomous DNA binding domains of λ integrase recognize different sequence families. Cell, 54, 923-929.
    • (1988) Cell , vol.54 , pp. 923-929
    • Moitoso de Vargas, L.1    Pargellis, C.A.2    Hasan, N.M.3    Bushman, E.W.4    Landy, A.5
  • 4
    • 0037133558 scopus 로고    scopus 로고
    • Arm-site binding by the lambda integrase protein: Solution structure and functional characterization of its amino-terminal domain
    • Wojciak, J. M., Sarkar, D., Landy, A. & Clubb, R. T. (2002). Arm-site binding by the lambda integrase protein: Solution structure and functional characterization of its amino-terminal domain. Proc. Natl Acad. Sci. USA, 99, 3434-3439.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3434-3439
    • Wojciak, J.M.1    Sarkar, D.2    Landy, A.3    Clubb, R.T.4
  • 5
    • 0036923454 scopus 로고    scopus 로고
    • Differential affinity and cooperativity functions of the amino-terminal 70 residues of λ integrase
    • In press
    • Sarkar, D., Azaro, M. A., Aihara, H., Papagiannis, C., Tirumalai, R. S., Nunes-Düby, S. E. et al. (2002). Differential affinity and cooperativity functions of the amino-terminal 70 residues of λ integrase. J. Mol. Biol. In press.
    • (2002) J. Mol. Biol.
    • Sarkar, D.1    Azaro, M.A.2    Aihara, H.3    Papagiannis, C.4    Tirumalai, R.S.5    Nunes-Düby, S.E.6
  • 6
    • 0023478505 scopus 로고
    • Mutational analysis of the lambda int gene: DNA sequence of dominant mutations
    • Bear, S. E., Clemens, J. B., Enquist, L. W. & Zagursky, R. J. (1987). Mutational analysis of the lambda int gene: DNA sequence of dominant mutations. J. Bacteriol. 169, 5880-5883.
    • (1987) J. Bacteriol. , vol.169 , pp. 5880-5883
    • Bear, S.E.1    Clemens, J.B.2    Enquist, L.W.3    Zagursky, R.J.4
  • 7
    • 0028125987 scopus 로고
    • Mapping the functional domains of bacteriophage lambda integrase protein
    • Han, Y. W., Gumport, R. I. & Gardner, J. F. (1994). Mapping the functional domains of bacteriophage lambda integrase protein. J. Mol. Biol. 235, 908-925.
    • (1994) J. Mol. Biol. , vol.235 , pp. 908-925
    • Han, Y.W.1    Gumport, R.I.2    Gardner, J.F.3
  • 9
    • 0001656001 scopus 로고    scopus 로고
    • Flexibility in DNA recombination: Structure of the λ integrase catalytic core
    • Kwon, H. J., Tirumalai, R. S., Landy, A. & Ellenberger, T. (1997). Flexibility in DNA recombination: Structure of the λ integrase catalytic core. Science, 276, 126-131.
    • (1997) Science , vol.276 , pp. 126-131
    • Kwon, H.J.1    Tirumalai, R.S.2    Landy, A.3    Ellenberger, T.4
  • 10
    • 0024386798 scopus 로고
    • Dynamic, structural and regulatory aspects of lambda site-specific recombination
    • Landy, A. (1989). Dynamic, structural and regulatory aspects of lambda site-specific recombination. Annu. Rev. Biochem. 58, 913-949.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 913-949
    • Landy, A.1
  • 11
    • 0000078911 scopus 로고    scopus 로고
    • Site-specific recombination: Integration, excision, resolution, and inversion of defined DNA segments
    • Neidhardt, F. C., Curtiss, R. III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., et al. ASM Press, Washington
    • Nash, H. A. (1996). Site-specific recombination: Integration, excision, resolution, and inversion of defined DNA segments. Escherichia coli and Salmonella: Cellular and Molecular Biology (Neidhardt, F. C., Curtiss, R. III, Ingraham, J. L., Lin, E. C. C., Low, K. B., Magasanik, B., et al.), pp. 2363-2376, ASM Press, Washington.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 2363-2376
    • Nash, H.A.1
  • 12
    • 0029240229 scopus 로고
    • Swapping DNA strands and sensing homology without branch migration in λ site-specific recombination
    • Nunes-Düby, S., Azaro, M. & Landy, A. (1995). Swapping DNA strands and sensing homology without branch migration in λ site-specific recombination. Curr. Biol. 5, 139-148.
    • (1995) Curr. Biol. , vol.5 , pp. 139-148
    • Nunes-Düby, S.1    Azaro, M.2    Landy, A.3
  • 13
    • 0032528271 scopus 로고    scopus 로고
    • Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination
    • Gopaul, D. N., Guo, F. & Van Duyne, G. D. (1998). Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination. EMBO J. 17, 4175-4187.
    • (1998) EMBO J. , vol.17 , pp. 4175-4187
    • Gopaul, D.N.1    Guo, F.2    Van Duyne, G.D.3
  • 14
    • 0031260604 scopus 로고    scopus 로고
    • Site-specific recombination: Synapsis and strand exchange revealed
    • Grindley, N. D. F. (1997). Site-specific recombination: Synapsis and strand exchange revealed. Curr. Biol. 7, 608-612.
    • (1997) Curr. Biol. , vol.7 , pp. 608-612
    • Grindley, N.D.F.1
  • 15
    • 0020397021 scopus 로고
    • Site-specific DNA condensation and pairing mediated by the Int protein of bacteriophage lambda
    • Better, M., Lu, C., Williams, R. C. & Echols, H. (1982). Site-specific DNA condensation and pairing mediated by the Int protein of bacteriophage lambda. Proc. Natl Acad. Sci. USA, 79, 5837-5841.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5837-5841
    • Better, M.1    Lu, C.2    Williams, R.C.3    Echols, H.4
  • 16
    • 0020651375 scopus 로고
    • Role of the Xis protein of bacteriophage λ in a specific reactive complex at the attR prophage attachment site
    • Better, M., Wickner, S., Auerbach, J. & Echols, H. (1983). Role of the Xis protein of bacteriophage λ in a specific reactive complex at the attR prophage attachment site. Cell, 32, 161-168.
    • (1983) Cell , vol.32 , pp. 161-168
    • Better, M.1    Wickner, S.2    Auerbach, J.3    Echols, H.4
  • 17
    • 0021646260 scopus 로고
    • The role of specialized nucleoprotein structures in site-specific recombination and initiation of DNA replication
    • Echols, H., Dodson, M., Better, M., Roberts, J. D. & McMacken, R. (1984). The role of specialized nucleoprotein structures in site-specific recombination and initiation of DNA replication. Cold Spring Harbor Symp. Quant. Biol. 49, 727-733.
    • (1984) Cold Spring Harbor Symp. Quant. Biol. , vol.49 , pp. 727-733
    • Echols, H.1    Dodson, M.2    Better, M.3    Roberts, J.D.4    McMacken, R.5
  • 18
    • 0023854278 scopus 로고
    • Synapsis of attachment sites during lambda integrative recombination involves capture of a naked DNA by a protein-DNA complex
    • Richet, E., Abcarian, P. & Nash, H. A. (1988). Synapsis of attachment sites during lambda integrative recombination involves capture of a naked DNA by a protein-DNA complex. Cell, 52, 9-17.
    • (1988) Cell , vol.52 , pp. 9-17
    • Richet, E.1    Abcarian, P.2    Nash, H.A.3
  • 19
    • 0030924382 scopus 로고    scopus 로고
    • The catalytic domain of λ site-specific recombinase
    • Tirumalai, R. S., Healey, E. & Landy, A. (1997). The catalytic domain of λ site-specific recombinase. Proc. Natl Acad. Sci. USA, 94, 6104-6109.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6104-6109
    • Tirumalai, R.S.1    Healey, E.2    Landy, A.3
  • 20
    • 0037177824 scopus 로고    scopus 로고
    • Site-specific photo-crosslinking of lambda Int
    • Kovach, M. J., Tirumalai, R. S. & Landy, A. (2002). Site-specific photo-crosslinking of lambda Int. J. Biol. Chem. 277, 14530-14538.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14530-14538
    • Kovach, M.J.1    Tirumalai, R.S.2    Landy, A.3
  • 22
    • 0030904786 scopus 로고    scopus 로고
    • Molecular organization in site-specific recombination: The catalytic domain of bacteriophage HP1 integrase at 2.7 Å resolution
    • Hickman, A. B., Waninger, S., Scocca, J. J. & Dyda, F. (1997). Molecular organization in site-specific recombination: The catalytic domain of bacteriophage HP1 integrase at 2.7 Å resolution. Cell, 89, 227-237.
    • (1997) Cell , vol.89 , pp. 227-237
    • Hickman, A.B.1    Waninger, S.2    Scocca, J.J.3    Dyda, F.4
  • 23
    • 0030886293 scopus 로고    scopus 로고
    • Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse
    • Guo, F., Gopaul, D. N. & Van Duyne, G. D. (1997). Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Nature, 389, 40-46.
    • (1997) Nature , vol.389 , pp. 40-46
    • Guo, F.1    Gopaul, D.N.2    Van Duyne, G.D.3
  • 24
    • 0033637213 scopus 로고    scopus 로고
    • Crystal structure of a Flp recombinase-Holliday junction complex: Assembly of an active oligomer by helix swapping
    • Chen, Y., Narendra, U., Iype, L. E., Cox, M. M. & Rice, P. A. (2000). Crystal structure of a Flp recombinase-Holliday junction complex: Assembly of an active oligomer by helix swapping. Mol. Cell, 6, 885-897.
    • (2000) Mol. Cell , vol.6 , pp. 885-897
    • Chen, Y.1    Narendra, U.2    Iype, L.E.3    Cox, M.M.4    Rice, P.A.5
  • 25
    • 0038659759 scopus 로고    scopus 로고
    • Similarities and differences among 105 members of the Int family of site-specific recombinases
    • Nunes-Düby, S., Tirumalai, R. S., Kwon, H. J., Ellenberger, T. & Landy, A. (1998). Similarities and differences among 105 members of the Int family of site-specific recombinases. Nucl. Acids Res. 26, 391-406.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 391-406
    • Nunes-Düby, S.1    Tirumalai, R.S.2    Kwon, H.J.3    Ellenberger, T.4    Landy, A.5
  • 26
    • 0023660545 scopus 로고
    • A mutational analysis of the bacteriophage P1 recombinase Cre
    • Wierzbicki, A., Kendall, M., Abremski, K. & Hoess, R. (1987). A mutational analysis of the bacteriophage P1 recombinase Cre. J. Mol. Biol. 195, 785-794.
    • (1987) J. Mol. Biol. , vol.195 , pp. 785-794
    • Wierzbicki, A.1    Kendall, M.2    Abremski, K.3    Hoess, R.4
  • 27
    • 0027159168 scopus 로고
    • Mechanism of cleavage and ligation by the FLP recombinase: Classification of mutations in the FLP protein using in vitro complementation analysis
    • Pan, G., Luetke, K. & Sadowski, P. D. (1993). Mechanism of cleavage and ligation by the FLP recombi-nase: Classification of mutations in the FLP protein using in vitro complementation analysis. Mol. Cell. Biol. 13, 3167-3175.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3167-3175
    • Pan, G.1    Luetke, K.2    Sadowski, P.D.3
  • 28
    • 0032984988 scopus 로고    scopus 로고
    • C-terminal interactions between the XerC and XerD site-specific recombinases
    • Spiers, A. J. & Sherratt, D. J. (1999). C-terminal interactions between the XerC and XerD site-specific recombinases. Mol. Microbiol. 32, 1031-1042.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1031-1042
    • Spiers, A.J.1    Sherratt, D.J.2
  • 29
    • 0030881917 scopus 로고    scopus 로고
    • Xer recombination in Escherichia coli
    • Cornet, F., Hallet, B. & Sherratt, D. J. (1997). Xer recombination in Escherichia coli. J. Biol. Chem. 272, 21927-21931.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21927-21931
    • Cornet, F.1    Hallet, B.2    Sherratt, D.J.3
  • 30
    • 0032549763 scopus 로고    scopus 로고
    • Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases
    • Cheng, C., Kussie, P., Pavletich, N. & Shuman, S. (1998). Conservation of structure and mechanism between eukaryotic topoisomerase I and site-specific recombinases. Cell, 92, 841-850.
    • (1998) Cell , vol.92 , pp. 841-850
    • Cheng, C.1    Kussie, P.2    Pavletich, N.3    Shuman, S.4
  • 31
    • 0024431718 scopus 로고
    • Half-att site substrates reveal the homology independence and minimal protein requirements for productive synapsis in λ excisive recombination
    • Nunes-Düby, S. E., Matsumoto, L. & Landy, A. (1989). Half-att site substrates reveal the homology independence and minimal protein requirements for productive synapsis in λ excisive recombination. Cell, 59, 197-206.
    • (1989) Cell , vol.59 , pp. 197-206
    • Nunes-Düby, S.E.1    Matsumoto, L.2    Landy, A.3
  • 32
    • 0025155363 scopus 로고
    • Interactions between λ Int molecules bound to sites in the region of strand exchange are required for efficient Holliday junction resolution
    • Franz, B. & Landy, A. (1990). Interactions between λ Int molecules bound to sites in the region of strand exchange are required for efficient Holliday junction resolution. J. Mol. Biol. 215, 523-535.
    • (1990) J. Mol. Biol. , vol.215 , pp. 523-535
    • Franz, B.1    Landy, A.2
  • 33
    • 0028244101 scopus 로고
    • Dissecting the resolution reaction of lambda integrase using suicide Holliday junction substrates
    • Kho, S. H. & Landy, A. (1994). Dissecting the resolution reaction of lambda integrase using suicide Holliday junction substrates. EMBO J. 13, 2714-2724.
    • (1994) EMBO J. , vol.13 , pp. 2714-2724
    • Kho, S.H.1    Landy, A.2
  • 34
    • 0017333366 scopus 로고
    • A genetic analysis of the att-int-xis region of coliphage λ
    • Enquist, L. W. & Weisberg, R. A. (1977). A genetic analysis of the att-int-xis region of coliphage λ. J. Mol. Biol. 111, 97-120.
    • (1977) J. Mol. Biol. , vol.111 , pp. 97-120
    • Enquist, L.W.1    Weisberg, R.A.2
  • 35
    • 0024278670 scopus 로고
    • Suicide recombination substrates yield covalent λ integrase-DNA complexes and lead to identification of the active site tyrosine
    • Pargellis, C. A., Nunes-Düby, S. E., Moitoso de Vargas, L. & Landy, A. (1988). Suicide recombination substrates yield covalent λ integrase-DNA complexes and lead to identification of the active site tyrosine. J. Biol. Chem. 263, 7678-7685.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7678-7685
    • Pargellis, C.A.1    Nunes-Düby, S.E.2    Moitoso de Vargas, L.3    Landy, A.4
  • 36
    • 0029411624 scopus 로고
    • Suicide substrates reveal properties of the homology-dependent steps during integrative recombination of bacteriophage λ
    • Burgin, A. B. & Nash, H. A. (1995). Suicide substrates reveal properties of the homology-dependent steps during integrative recombination of bacteriophage λ. Curr. Biol. 5, 1312-1321.
    • (1995) Curr. Biol. , vol.5 , pp. 1312-1321
    • Burgin, A.B.1    Nash, H.A.2
  • 37
    • 0031551575 scopus 로고    scopus 로고
    • Sensing homology at the strand swapping step in λ excisive recombination
    • Nunes-Düby, S. E., Yu, D. & Landy, A. (1997). Sensing homology at the strand swapping step in λ excisive recombination. J. Mol. Biol. 272, 493-508.
    • (1997) J. Mol. Biol. , vol.272 , pp. 493-508
    • Nunes-Düby, S.E.1    Yu, D.2    Landy, A.3
  • 38
    • 0029165078 scopus 로고
    • A novel suicide substrate for DNA topoisomerases and site-specific recombinases
    • Burgin, A. B., Jr, Huizenga, B. N. & Nash, H. A. (1995). A novel suicide substrate for DNA topoisomerases and site-specific recombinases. Nucl. Acids Res. 23, 2973-2979.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2973-2979
    • Burgin A.B., Jr.1    Huizenga, B.N.2    Nash, H.A.3
  • 39
    • 0030601823 scopus 로고    scopus 로고
    • Mutations within a conserved region of vaccinia topoisomerase affect the DNA cleavage-religation equilibrium
    • Petersen, B. O., Wittschieben, J. & Shuman, S. (1996). Mutations within a conserved region of vaccinia topoisomerase affect the DNA cleavage-religation equilibrium. J. Mol. Biol. 263, 181-195.
    • (1996) J. Mol. Biol. , vol.263 , pp. 181-195
    • Petersen, B.O.1    Wittschieben, J.2    Shuman, S.3
  • 40
    • 0026651559 scopus 로고
    • DNA cleavage in trans by the active site tyrosine during Flp recombination: Switching protein partners before exchanging strands
    • Chen, J.-W., Lee, J. & Jayaram, M. (1992). DNA cleavage in trans by the active site tyrosine during Flp recombination: Switching protein partners before exchanging strands. Cell, 69, 647-658.
    • (1992) Cell , vol.69 , pp. 647-658
    • Chen, J.-W.1    Lee, J.2    Jayaram, M.3
  • 41
    • 0035282917 scopus 로고    scopus 로고
    • The small DNA binding domain of λ Int is a context-sensitive modulator of recombinase functions
    • Sarkar, D., Radman-Livaja, M. & Landy, A. (2001). The small DNA binding domain of λ Int is a context-sensitive modulator of recombinase functions. EMBO J. 20, 1203-1212.
    • (2001) EMBO J. , vol.20 , pp. 1203-1212
    • Sarkar, D.1    Radman-Livaja, M.2    Landy, A.3
  • 43
    • 0033594916 scopus 로고    scopus 로고
    • Asymmetric DNA-bending in the Cre-loxP site-specific recombination synapse
    • Guo, F., Gopaul, D. N. & Van Duyne, G. D. (1999). Asymmetric DNA-bending in the Cre-loxP site-specific recombination synapse. Proc. Natl Acad. Sci. USA, 96, 7143-7148.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7143-7148
    • Guo, F.1    Gopaul, D.N.2    Van Duyne, G.D.3
  • 44
    • 0033382191 scopus 로고    scopus 로고
    • Reciprocal control of catalysis by the tyrosine recombinases XerC and XerD: An enzymatic switch in site - Specific recombination
    • Hallet, B., Arciszewska, L. K. & Sherratt, D. J. (1999). Reciprocal control of catalysis by the tyrosine recom-binases XerC and XerD: An enzymatic switch in site - Specific recombination. Mol. Cell, 4, 949-959.
    • (1999) Mol. Cell , vol.4 , pp. 949-959
    • Hallet, B.1    Arciszewska, L.K.2    Sherratt, D.J.3
  • 45
    • 0030950350 scopus 로고    scopus 로고
    • The isomeric preference of Holliday junctions influences resolution bias by λ integrase
    • Azaro, M. A. & Landy, A. (1997). The isomeric preference of Holliday junctions influences resolution bias by λ integrase. EMBO J. 16, 3744-3755.
    • (1997) EMBO J. , vol.16 , pp. 3744-3755
    • Azaro, M.A.1    Landy, A.2
  • 46
    • 0028048679 scopus 로고
    • Core-packing constraints, hydrophobicity and protein design
    • Baldwin, E. P. & Matthews, B. W. (1994). Core-packing constraints, hydrophobicity and protein design. Curr. Opin. Biotechnol. 5, 396-402.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 396-402
    • Baldwin, E.P.1    Matthews, B.W.2
  • 47
    • 0034991483 scopus 로고    scopus 로고
    • A structural view of creloxp site-specific recombination
    • Van Duyne, G. D. (2001). A structural view of creloxp site-specific recombination. Annu. Rev. Biophys. Biomol. Struct. 30, 87-104.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 87-104
    • Van Duyne, G.D.1
  • 48
    • 0029986069 scopus 로고    scopus 로고
    • Determinants of selectivity in Xer site-specific recombination
    • Blakely, G. & Sherratt, D. (1996). Determinants of selectivity in Xer site-specific recombination. Genes Dev. 10, 762-773.
    • (1996) Genes Dev. , vol.10 , pp. 762-773
    • Blakely, G.1    Sherratt, D.2
  • 49
    • 0031561801 scopus 로고    scopus 로고
    • Binding and cleavage of nicked substrates by site-specific recombinases XerC and XerD
    • Blakely, G. W., Davidson, A. O. & Sherratt, D. J. (1997). Binding and cleavage of nicked substrates by site-specific recombinases XerC and XerD. J. Mol. Biol. 265, 30-39.
    • (1997) J. Mol. Biol. , vol.265 , pp. 30-39
    • Blakely, G.W.1    Davidson, A.O.2    Sherratt, D.J.3
  • 50
    • 0035823229 scopus 로고    scopus 로고
    • Switching catalytic activity in the XerCD site-specific
    • Ferreira, H., Sherratt, D. & Arciszewska, L. (2001). Switching catalytic activity in the XerCD site-specific. J. Mol. Biol. 312, 45-57.
    • (2001) J. Mol. Biol. , vol.312 , pp. 45-57
    • Ferreira, H.1    Sherratt, D.2    Arciszewska, L.3
  • 51
    • 0030887269 scopus 로고    scopus 로고
    • Topological analysis of the role of homology in Flp-mediated recombination
    • Azam, N., Dixon, J. E. & Sadowski, P. D. (1997). Topological analysis of the role of homology in Flp-mediated recombination. J. Biol. Chem. 272, 8731-8738.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8731-8738
    • Azam, N.1    Dixon, J.E.2    Sadowski, P.D.3
  • 52
    • 0032037326 scopus 로고    scopus 로고
    • Unveiling two distinct ribonuclease activities and a topoisomerase activity in a site-specific DNA recombinase
    • Xu, C., Grainge, I., Lee, J., Harshey, R. M. & Jayaram, M. (1998). Unveiling two distinct ribonuclease activities and a topoisomerase activity in a site-specific DNA recombinase. Mol. Cell, 1, 729-739.
    • (1998) Mol. Cell , vol.1 , pp. 729-739
    • Xu, C.1    Grainge, I.2    Lee, J.3    Harshey, R.M.4    Jayaram, M.5
  • 53
    • 0020523314 scopus 로고
    • Studies on the properties of P1 site-specific recombination: Evidence for topologically unlinked products following recombination
    • Abremski, K., Hoess, R. & Sternberg, N. (1983). Studies on the properties of P1 site-specific recombination: Evidence for topologically unlinked products following recombination. Cell, 32, 1301-1311.
    • (1983) Cell , vol.32 , pp. 1301-1311
    • Abremski, K.1    Hoess, R.2    Sternberg, N.3
  • 54
    • 0002686249 scopus 로고
    • The lox-Cre site-specific recombination system of bacteriophage P1
    • McMacken, R. & Kelly, T. J., eds, Alan R. Liss, New York
    • Hoess, R., Abremski, K., Frommer, B., Wierzbicki, A. & Kendall, M. (1987). The lox-Cre site-specific recombination system of bacteriophage P1. In In DNA Replication and Recombination (McMacken, R. & Kelly, T. J., eds), pp. 745-756, Alan R. Liss, New York.
    • (1987) In DNA Replication and Recombination , pp. 745-756
    • Hoess, R.1    Abremski, K.2    Frommer, B.3    Wierzbicki, A.4    Kendall, M.5
  • 56
    • 0033634688 scopus 로고    scopus 로고
    • Catalytic mechanism of DNA topoisomerase IB
    • Krogh, B. O. & Shuman, S. (2000). Catalytic mechanism of DNA topoisomerase IB. Mol. Cell, 5, 1035-1041.
    • (2000) Mol. Cell , vol.5 , pp. 1035-1041
    • Krogh, B.O.1    Shuman, S.2
  • 57
    • 0034711263 scopus 로고    scopus 로고
    • Characterization of a mutation of bacteriophage λ integrase: Putative role in core binding and strand exchange for a conserved residue
    • Bankhead, T. & Segall, A. M. (2000). Characterization of a mutation of bacteriophage λ integrase: Putative role in core binding and strand exchange for a conserved residue. J. Biol. Chem. 275, 36949-36956.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36949-36956
    • Bankhead, T.1    Segall, A.M.2
  • 58
    • 0034595513 scopus 로고    scopus 로고
    • Coordinated control of XerC and XerD catalytic activities during Holliday junction resolution
    • Arciszewska, L. K., Baker, R. A., Hallet, B. & Sherratt, D. J. (2000). Coordinated control of XerC and XerD catalytic activities during Holliday junction resolution. J. Mol. Biol. 299, 391-403.
    • (2000) J. Mol. Biol. , vol.299 , pp. 391-403
    • Arciszewska, L.K.1    Baker, R.A.2    Hallet, B.3    Sherratt, D.J.4
  • 59
    • 0019783899 scopus 로고
    • Purification and properties of the Escherichia coli protein factor required for λ integrative recombination
    • Nash, H. A. & Robertson, C. A. (1981). Purification and properties of the Escherichia coli protein factor required for λ integrative recombination. J. Biol. Chem. 256, 9246-9253.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9246-9253
    • Nash, H.A.1    Robertson, C.A.2
  • 60
    • 0023408583 scopus 로고
    • Overproduction of Escherichia coli integration host factor, a protein with nonidentical subunits
    • Nash, H. A., Robertson, C. A., Flamm, E., Weisberg, R. A. & Miller, H. I. (1987). Overproduction of Escherichia coli integration host factor, a protein with nonidentical subunits. J. Bacteriol. 169, 4124-4127.
    • (1987) J. Bacteriol. , vol.169 , pp. 4124-4127
    • Nash, H.A.1    Robertson, C.A.2    Flamm, E.3    Weisberg, R.A.4    Miller, H.I.5
  • 61
    • 0020355550 scopus 로고
    • Purification of the bacteriophage λ xis gene product required for λ excisive recombination
    • Abremski, K. & Gottesman, S. (1982). Purification of the bacteriophage λ xis gene product required for λ excisive recombination. J. Biol. Chem. 257, 9658-9662.
    • (1982) J. Biol. Chem. , vol.257 , pp. 9658-9662
    • Abremski, K.1    Gottesman, S.2
  • 62
    • 0021942310 scopus 로고
    • Interaction of λ site-specific recombination protein Xis with attachment site DNA
    • Yin, S., Bushman, W. & Landy, A. (1985). Interaction of λ site-specific recombination protein Xis with attachment site DNA. Proc. Natl Acad. Sci. USA, 82, 1040-1044.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1040-1044
    • Yin, S.1    Bushman, W.2    Landy, A.3
  • 63
    • 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. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 64
    • 0023667024 scopus 로고
    • Site-specific recombination intermediates trapped with suicide substrates
    • Nunes-Düby, S. E., Matsumoto, L. & Landy, A. (1987). Site-specific recombination intermediates trapped with suicide substrates. Cell, 50, 779-788.
    • (1987) Cell , vol.50 , pp. 779-788
    • Nunes-Düby, S.E.1    Matsumoto, L.2    Landy, A.3
  • 65
    • 0031473847 scopus 로고    scopus 로고
    • Swiss-model and the swiss-Pdb viewer: An environment for comparative protein modeling
    • Guex, N. & Peitsch, M. C. (1997). Swiss-model and the swiss-Pdb viewer: An environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.