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Volumn 347, Issue 1, 2005, Pages 11-25

The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases

Author keywords

DNA architectural protein; Excisionase; NMR structure; Tyrosine recombinase; Winged helix protein

Indexed keywords

EXCISIONASE; INTEGRASE; PROTEIN DERIVATIVE; RECOMBINASE; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 14144251267     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.019     Document Type: Article
Times cited : (21)

References (90)
  • 1
    • 2942689400 scopus 로고    scopus 로고
    • Shaping bacterial genomes with integrative and conjugative elements
    • V. Burrus, and M.K. Waldor Shaping bacterial genomes with integrative and conjugative elements Res. Microbiol. 155 2004 376 386
    • (2004) Res. Microbiol. , vol.155 , pp. 376-386
    • Burrus, V.1    Waldor, M.K.2
  • 2
    • 0031928701 scopus 로고    scopus 로고
    • Tn916 family conjugative transposons and dissemination of antimicrobial resistance determinants
    • L.B. Rice Tn916 family conjugative transposons and dissemination of antimicrobial resistance determinants Antimicrob. Agents Chemother. 42 1998 1871 1877
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1871-1877
    • Rice, L.B.1
  • 4
    • 0029046947 scopus 로고
    • Unconstrained bacterial promiscuity: The Tn916-Tn1545 family of conjugative transposons
    • D.B. Clewell, S.E. Flannagan, and D.D. Jaworski Unconstrained bacterial promiscuity: the Tn916-Tn1545 family of conjugative transposons Trends Microbiol. 3 1995 229 236
    • (1995) Trends Microbiol. , vol.3 , pp. 229-236
    • Clewell, D.B.1    Flannagan, S.E.2    Jaworski, D.D.3
  • 5
    • 0028889420 scopus 로고
    • Conjugative transposons: An unusual and diverse set of integrated gene transfer elements
    • A.A. Salyers, N.B. Shoemaker, A.M. Stevens, and L.Y. Li Conjugative transposons: an unusual and diverse set of integrated gene transfer elements Microbiol. Rev. 59 1995 579 590
    • (1995) Microbiol. Rev. , vol.59 , pp. 579-590
    • Salyers, A.A.1    Shoemaker, N.B.2    Stevens, A.M.3    Li, L.Y.4
  • 6
    • 0029986215 scopus 로고    scopus 로고
    • A new type of conjugative transposon encodes resistance to sulfamethoxazole, trimethoprim, and streptomycin in Vibrio cholerae O139
    • M.K. Waldor, H. Tschäpe, and J.J. Mekalanos A new type of conjugative transposon encodes resistance to sulfamethoxazole, trimethoprim, and streptomycin in Vibrio cholerae O139 J. Bacteriol. 178 1996 4157 4165
    • (1996) J. Bacteriol. , vol.178 , pp. 4157-4165
    • Waldor, M.K.1    Tschäpe, H.2    Mekalanos, J.J.3
  • 7
    • 0026078804 scopus 로고
    • Tn5253, the pneumococcal omega (cat tet) BM6001 element, is a composite structure of two conjugative transposons, Tn5251 and Tn5252
    • P. Ayoubi, A.O. Kilic, and M.N. Vijayakumar Tn5253, the pneumococcal omega (cat tet) BM6001 element, is a composite structure of two conjugative transposons, Tn5251 and Tn5252 J. Bacteriol. 173 1991 1617 1622
    • (1991) J. Bacteriol. , vol.173 , pp. 1617-1622
    • Ayoubi, P.1    Kilic, A.O.2    Vijayakumar, M.N.3
  • 8
    • 0034003481 scopus 로고    scopus 로고
    • Characterization of the Tn916-like transposon Tn3872 in a strain of Abiotrophia defectiva (Streptococcus defectivus) causing sequential episodes of endocarditis in a child
    • C. Poyart, G. Quesne, P. Acar, P. Berche, and P. Trieu-Cuot Characterization of the Tn916-like transposon Tn3872 in a strain of Abiotrophia defectiva (Streptococcus defectivus) causing sequential episodes of endocarditis in a child Antimicrob. Agents Chemother. 44 2000 790 793
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 790-793
    • Poyart, C.1    Quesne, G.2    Acar, P.3    Berche, P.4    Trieu-Cuot, P.5
  • 9
    • 0031783527 scopus 로고    scopus 로고
    • Genetic linkage and cotransfer of a novel, vanB-containing transposon (Tn5382) and a low-affinity penicillin-binding protein 5 gene in a clinical vancomycin-resistant Enterococcus faecium isolate
    • L.L. Carias, S.D. Rudin, C.J. Donskey, and L.B. Rice Genetic linkage and cotransfer of a novel, vanB-containing transposon (Tn5382) and a low-affinity penicillin-binding protein 5 gene in a clinical vancomycin-resistant Enterococcus faecium isolate J. Bacteriol. 180 1998 4426 4434
    • (1998) J. Bacteriol. , vol.180 , pp. 4426-4434
    • Carias, L.L.1    Rudin, S.D.2    Donskey, C.J.3    Rice, L.B.4
  • 10
    • 0028098113 scopus 로고
    • Genetic and molecular studies of a composite chromosomal element (Tn3705) containing a Tn916-modified structure (Tn3704) in Streptococcus anginosus F22
    • D. Clermont, and T. Horaud Genetic and molecular studies of a composite chromosomal element (Tn3705) containing a Tn916-modified structure (Tn3704) in Streptococcus anginosus F22 Plasmid 31 1994 40 48
    • (1994) Plasmid , vol.31 , pp. 40-48
    • Clermont, D.1    Horaud, T.2
  • 11
    • 0027962445 scopus 로고
    • Nucleotide sequence of the 18-kb conjugative transposon Tn916 from Enterococcus faecalis
    • S.E. Flannagan, L.A. Zitzow, Y.A. Su, and D.B. Clewell Nucleotide sequence of the 18-kb conjugative transposon Tn916 from Enterococcus faecalis Plasmid 32 1994 350 354
    • (1994) Plasmid , vol.32 , pp. 350-354
    • Flannagan, S.E.1    Zitzow, L.A.2    Su, Y.A.3    Clewell, D.B.4
  • 12
    • 0024827010 scopus 로고
    • Excision and insertion of the conjugative transposon Tn916 involves a novel recombination mechanism
    • M.G. Caparon, and J.R. Scott Excision and insertion of the conjugative transposon Tn916 involves a novel recombination mechanism Cell 59 1989 1027 1034
    • (1989) Cell , vol.59 , pp. 1027-1034
    • Caparon, M.G.1    Scott, J.R.2
  • 13
    • 0029796617 scopus 로고    scopus 로고
    • Conjugative transposon Tn916: Evidence for excision with formation of 5′-protruding termini
    • R. Manganelli, S. Ricci, and G. Pozzi Conjugative transposon Tn916: evidence for excision with formation of 5′-protruding termini J. Bacteriol. 178 1996 5813 5816
    • (1996) J. Bacteriol. , vol.178 , pp. 5813-5816
    • Manganelli, R.1    Ricci, S.2    Pozzi, G.3
  • 14
    • 0028216655 scopus 로고
    • Conjugative transposition of Tn916: Preferred targets and evidence for conjugative transfer of a single strand and for a double-stranded circular intermediate
    • J.R. Scott, F. Bringel, D. Marra, G. Van Alstine, and C.K. Rudy Conjugative transposition of Tn916: preferred targets and evidence for conjugative transfer of a single strand and for a double-stranded circular intermediate Mol. Microbiol. 11 1994 1099 1108
    • (1994) Mol. Microbiol. , vol.11 , pp. 1099-1108
    • Scott, J.R.1    Bringel, F.2    Marra, D.3    Van Alstine, G.4    Rudy, C.K.5
  • 15
    • 0030796354 scopus 로고    scopus 로고
    • The joint of Tn916 circular intermediates is a homoduplex in Enterococcus faecalis
    • R. Manganelli, S. Ricci, and G. Pozzi The joint of Tn916 circular intermediates is a homoduplex in Enterococcus faecalis Plasmid 38 1997 71 78
    • (1997) Plasmid , vol.38 , pp. 71-78
    • Manganelli, R.1    Ricci, S.2    Pozzi, G.3
  • 16
    • 0031921950 scopus 로고    scopus 로고
    • Circularization of Tn916 is required for expression of the transposon-encoded transfer functions: Characterization of long tetracyclin-inducible transcripts reading through the attachment site
    • J. Celli, and P. Trieu-Cuot Circularization of Tn916 is required for expression of the transposon-encoded transfer functions: characterization of long tetracyclin-inducible transcripts reading through the attachment site Mol. Microbiol. 28 1998 103 117
    • (1998) Mol. Microbiol. , vol.28 , pp. 103-117
    • Celli, J.1    Trieu-Cuot, P.2
  • 17
    • 0024468976 scopus 로고
    • Molecular characterization of two proteins involved in the excision of the conjugative transposon Tn1545: Homologies with other site-specific recombinases
    • C. Poyart-Salmeron, P. Trieu-Cuot, C. Carlier, and P. Courvalin Molecular characterization of two proteins involved in the excision of the conjugative transposon Tn1545: homologies with other site-specific recombinases EMBO J. 8 1989 2425 2433
    • (1989) EMBO J. , vol.8 , pp. 2425-2433
    • Poyart-Salmeron, C.1    Trieu-Cuot, P.2    Carlier, C.3    Courvalin, P.4
  • 18
    • 0025815974 scopus 로고
    • Conjugative transposition of Tn916 requires the excisive and integrative activities of the transposon-encoded integrase
    • W.M. Storrs, C. Carlier, C. Poyart-Salmeron, P. Trieu-Cuot, and P. Courvalin Conjugative transposition of Tn916 requires the excisive and integrative activities of the transposon-encoded integrase J. Bacteriol. 173 1991 4347 4352
    • (1991) J. Bacteriol. , vol.173 , pp. 4347-4352
    • Storrs, W.M.1    Carlier, C.2    Poyart-Salmeron, C.3    Trieu-Cuot, P.4    Courvalin, P.5
  • 19
    • 0027368351 scopus 로고
    • Characterization of the left 4 kb of conjugative transposon Tn916: Determinants involved in excision
    • Y.A. Su, and D.B. Clewell Characterization of the left 4 kb of conjugative transposon Tn916: determinants involved in excision Plasmid 30 1993 234 250
    • (1993) Plasmid , vol.30 , pp. 234-250
    • Su, Y.A.1    Clewell, D.B.2
  • 20
    • 0030816550 scopus 로고    scopus 로고
    • The integrase family of tyrosine recombinases: Evolution of a conserved active site domain
    • D. Esposito, and J.J. Scocca The integrase family of tyrosine recombinases: evolution of a conserved active site domain Nucl. Acids Res. 25 1997 3605 3614
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3605-3614
    • Esposito, D.1    Scocca, J.J.2
  • 21
    • 0038659759 scopus 로고    scopus 로고
    • Similarities and differences among 105 members of the Int family of site-specific recombinases
    • S.E. Nunes-Duby, H.J. Kwon, R.S. Tirumalai, T. Ellenberger, and A. Landy Similarities and differences among 105 members of the Int family of site-specific recombinases Nucl. Acids Res. 26 1998 391 406
    • (1998) Nucl. Acids Res. , vol.26 , pp. 391-406
    • Nunes-Duby, S.E.1    Kwon, H.J.2    Tirumalai, R.S.3    Ellenberger, T.4    Landy, A.5
  • 22
    • 85158019877 scopus 로고    scopus 로고
    • Lambda integrase and the lambda Int family
    • N.L. Craig R. Craigie M. Gellert A.M. Lambowitz ASM Press Washington, DC
    • M.A. Azaro, and A. Landy Lambda integrase and the lambda Int family N.L. Craig R. Craigie M. Gellert A.M. Lambowitz Mobile DNA II 2002 ASM Press Washington, DC 118 148
    • (2002) Mobile DNA II , pp. 118-148
    • Azaro, M.A.1    Landy, A.2
  • 23
    • 0028353171 scopus 로고
    • Conjugative transposition: Tn916 integrase contains two independent DNA binding domains that recognize different DNA sequences
    • F. Lu, and G. Churchward Conjugative transposition: Tn916 integrase contains two independent DNA binding domains that recognize different DNA sequences EMBO J. 13 1994 1541 1548
    • (1994) EMBO J. , vol.13 , pp. 1541-1548
    • Lu, F.1    Churchward, G.2
  • 24
    • 0036202271 scopus 로고    scopus 로고
    • Xis protein binding to the left arm stimulates excision of conjugative transposon Tn916
    • K.M. Connolly, M. Iwahara, and R.T. Clubb Xis protein binding to the left arm stimulates excision of conjugative transposon Tn916 J. Bacteriol. 184 2002 2088 2099
    • (2002) J. Bacteriol. , vol.184 , pp. 2088-2099
    • Connolly, K.M.1    Iwahara, M.2    Clubb, R.T.3
  • 25
    • 0032925508 scopus 로고    scopus 로고
    • Excision of the conjugative transposon Tn916 in Lactococcus lactis
    • D. Marra, J.G. Smith, and J.R. Scott Excision of the conjugative transposon Tn916 in Lactococcus lactis Appl. Environ. Microbiol. 65 1999 2230 2231
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 2230-2231
    • Marra, D.1    Smith, J.G.2    Scott, J.R.3
  • 26
    • 0032938505 scopus 로고    scopus 로고
    • Regulation of excision of the conjugative transposon Tn916
    • D. Marra, and J.R. Scott Regulation of excision of the conjugative transposon Tn916 Mol. Microbiol. 31 1999 609 621
    • (1999) Mol. Microbiol. , vol.31 , pp. 609-621
    • Marra, D.1    Scott, J.R.2
  • 27
    • 0030800329 scopus 로고    scopus 로고
    • Excision of a conjugative transposon in vitro by the Int and Xis proteins of Tn916
    • C. Rudy, K.L. Taylor, D. Hinerfeld, J.R. Scott, and G. Churchward Excision of a conjugative transposon in vitro by the Int and Xis proteins of Tn916 Nucl. Acids Res. 25 1997 4061 4066
    • (1997) Nucl. Acids Res. , vol.25 , pp. 4061-4066
    • Rudy, C.1    Taylor, K.L.2    Hinerfeld, D.3    Scott, J.R.4    Churchward, G.5
  • 28
    • 0031000745 scopus 로고    scopus 로고
    • DNA binding by the Xis protein of the conjugative transposon Tn916
    • C.K. Rudy, J.R. Scott, and G. Churchward DNA binding by the Xis protein of the conjugative transposon Tn916 J. Bacteriol. 179 1997 2567 2572
    • (1997) J. Bacteriol. , vol.179 , pp. 2567-2572
    • Rudy, C.K.1    Scott, J.R.2    Churchward, G.3
  • 29
    • 0023667024 scopus 로고
    • Site-specific recombination intermediates trapped with suicide substrates
    • S.E. Nunes-Düby, L. Matsumoto, and A. Landy Site-specific recombination intermediates trapped with suicide substrates Cell 50 1987 779 788
    • (1987) Cell , vol.50 , pp. 779-788
    • Nunes-Düby, S.E.1    Matsumoto, L.2    Landy, A.3
  • 30
    • 0024431718 scopus 로고
    • Half-att site substrates reveal the homology independence and minimal protein requirements for productive synapsis in lambda excisive recombination
    • S.E. Nunes-Düby, L. Matsumoto, and A. Landy Half-att site substrates reveal the homology independence and minimal protein requirements for productive synapsis in lambda excisive recombination Cell 59 1989 197 206
    • (1989) Cell , vol.59 , pp. 197-206
    • Nunes-Düby, S.E.1    Matsumoto, L.2    Landy, A.3
  • 31
    • 0023644993 scopus 로고
    • Protein-protein interactions in a higher-order structure direct lambda site-specific recombination
    • J.F. Thompson, L.M. de Vargas, S.E. Skinner, and A. Landy Protein-protein interactions in a higher-order structure direct lambda site-specific recombination J. Mol. Biol. 195 1987 481 493
    • (1987) J. Mol. Biol. , vol.195 , pp. 481-493
    • Thompson, J.F.1    De Vargas, L.M.2    Skinner, S.E.3    Landy, A.4
  • 32
    • 0028893895 scopus 로고
    • The Holliday junction intermediates of lambda integrative and excisive recombination respond differently to the bending proteins integration host factor and excisionase
    • B. Franz, and A. Landy The Holliday junction intermediates of lambda integrative and excisive recombination respond differently to the bending proteins integration host factor and excisionase EMBO J. 14 1995 397 406
    • (1995) EMBO J. , vol.14 , pp. 397-406
    • Franz, B.1    Landy, A.2
  • 33
    • 0022351236 scopus 로고
    • Control of directionality in lambda site specific recombination
    • W. Bushman, J.F. Thompson, L. Vargas, and A. Landy Control of directionality in lambda site specific recombination Science 230 1985 906 911
    • (1985) Science , vol.230 , pp. 906-911
    • Bushman, W.1    Thompson, J.F.2    Vargas, L.3    Landy, A.4
  • 34
    • 0025223119 scopus 로고
    • Mapping of a higher order protein-DNA complex: Two kinds of long-range interactions in lambda attL
    • S. Kim, L. Moitoso de Vargas, S.E. Nunes-Duby, and A. Landy Mapping of a higher order protein-DNA complex: two kinds of long-range interactions in lambda attL Cell 63 1990 773 781
    • (1990) Cell , vol.63 , pp. 773-781
    • Kim, S.1    Moitoso De Vargas, L.2    Nunes-Duby, S.E.3    Landy, A.4
  • 35
    • 0026537332 scopus 로고
    • Lambda Int protein bridges between higher order complexes at distant chromosomal loci attL and attR
    • S. Kim, and A. Landy Lambda Int protein bridges between higher order complexes at distant chromosomal loci attL and attR Science 256 1992 198 203
    • (1992) Science , vol.256 , pp. 198-203
    • Kim, S.1    Landy, A.2
  • 36
    • 0020397021 scopus 로고
    • Site-specific DNA condensation and pairing mediated by the it protein of bacteriophage lambda
    • M. Better, C. Lu, R.C. Williams, and H. Echols Site-specific DNA condensation and pairing mediated by the it protein of bacteriophage lambda Proc. Natl Acad Sci. USA 79 1982 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
  • 37
    • 0020651375 scopus 로고
    • Role of the Xis protein of bacteriophage lambda in a specific reactive complex at the attR prophage attachment site
    • M. Better, S. Wickner, J. Auerbach, and H. Echols Role of the Xis protein of bacteriophage lambda in a specific reactive complex at the attR prophage attachment site Cell 32 1983 161 168
    • (1983) Cell , vol.32 , pp. 161-168
    • Better, M.1    Wickner, S.2    Auerbach, J.3    Echols, H.4
  • 38
    • 0026008164 scopus 로고
    • A switch in the formation of alternative DNA loops modulates lambda site-specific recombination
    • L. Moitoso de Vargas, and A. Landy A switch in the formation of alternative DNA loops modulates lambda site-specific recombination Proc. Natl Acad Sci. USA 88 1991 588 592
    • (1991) Proc. Natl Acad Sci. USA , vol.88 , pp. 588-592
    • Moitoso De Vargas, L.1    Landy, A.2
  • 39
    • 0023771741 scopus 로고
    • Empirical estimation of protein-induced DNA bending angles: Application to λ site-specific recombination complexes
    • J. Thompson, and A. Landy Empirical estimation of protein-induced DNA bending angles: application to λ site-specific recombination complexes Nucl. Acids Res. 16 1988 9687 9705
    • (1988) Nucl. Acids Res. , vol.16 , pp. 9687-9705
    • Thompson, J.1    Landy, A.2
  • 40
    • 0023651267 scopus 로고
    • Cellular factors couple recombination with growth phase: Characterization of a new component in the lambda site-specific recombination pathway
    • J.F. Thompson, L. Moitoso de Vargas, C. Koch, R. Kahmann, and A. Landy Cellular factors couple recombination with growth phase: characterization of a new component in the lambda site-specific recombination pathway Cell 50 1987 901 908
    • (1987) Cell , vol.50 , pp. 901-908
    • Thompson, J.F.1    Moitoso De Vargas, L.2    Koch, C.3    Kahmann, R.4    Landy, A.5
  • 41
    • 0020355550 scopus 로고
    • Purification of the bacteriophage lambda xis gene product required for lambda excisive recombination
    • K. Abremski, and S. Gottesman Purification of the bacteriophage lambda xis gene product required for lambda excisive recombination J. Biol. Chem. 257 1982 9658 9662
    • (1982) J. Biol. Chem. , vol.257 , pp. 9658-9662
    • Abremski, K.1    Gottesman, S.2
  • 42
    • 0036928819 scopus 로고    scopus 로고
    • Regulation of directionality in bacteriophage lambda site-specific recombination: Structure of the Xis protein
    • M.D. Sam, C.V. Papagiannis, K.M. Connolly, L. Corselli, J. Iwahara, and J. Lee Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein J. Mol. Biol. 324 2002 791 805
    • (2002) J. Mol. Biol. , vol.324 , pp. 791-805
    • Sam, M.D.1    Papagiannis, C.V.2    Connolly, K.M.3    Corselli, L.4    Iwahara, J.5    Lee, J.6
  • 43
    • 0032881672 scopus 로고    scopus 로고
    • The frequency of conjugative transposition of Tn916 is not determined by the frequency of excision
    • D. Marra, B. Pethel, G.G. Churchward, and J.R. Scott The frequency of conjugative transposition of Tn916 is not determined by the frequency of excision J. Bacteriol. 181 1999 5414 5418
    • (1999) J. Bacteriol. , vol.181 , pp. 5414-5418
    • Marra, D.1    Pethel, B.2    Churchward, G.G.3    Scott, J.R.4
  • 44
    • 0034786513 scopus 로고    scopus 로고
    • Xis protein of the conjugative transposon Tn916 plays dual opposing roles in transposon excision
    • D. Hinerfeld, and G. Churchward Xis protein of the conjugative transposon Tn916 plays dual opposing roles in transposon excision Mol. Microbiol. 41 2001 1459 1467
    • (2001) Mol. Microbiol. , vol.41 , pp. 1459-1467
    • Hinerfeld, D.1    Churchward, G.2
  • 45
    • 0035368920 scopus 로고    scopus 로고
    • Control of directionality in integrase-mediated recombination: Examination of recombination directionality factors (RDFs) including Xis and Cox proteins
    • J.A. Lewis, and G.F. Hatfull Control of directionality in integrase-mediated recombination: examination of recombination directionality factors (RDFs) including Xis and Cox proteins Nucl. Acids Res. 29 2001 2205 2216
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2205-2216
    • Lewis, J.A.1    Hatfull, G.F.2
  • 46
    • 0030991671 scopus 로고    scopus 로고
    • Purification and characterization of HP1 Cox and definition of its role in controlling the direction of site-specific recombination
    • D. Esposito, and J.J. Scocca Purification and characterization of HP1 Cox and definition of its role in controlling the direction of site-specific recombination J. Biol. Chem. 272 1997 8660 8670
    • (1997) J. Biol. Chem. , vol.272 , pp. 8660-8670
    • Esposito, D.1    Scocca, J.J.2
  • 47
    • 0037459040 scopus 로고    scopus 로고
    • Control of directionality in L5 integrase-mediated site-specific recombination
    • J.A. Lewis, and G.F. Hatfull Control of directionality in L5 integrase-mediated site-specific recombination J. Mol. Biol. 326 2003 805 821
    • (2003) J. Mol. Biol. , vol.326 , pp. 805-821
    • Lewis, J.A.1    Hatfull, G.F.2
  • 48
    • 1842505115 scopus 로고    scopus 로고
    • Crystal structure of the excisionase-DNA complex from bacteriophage lambda
    • M.D. Sam, D. Cascio, R.C. Johnson, and R.T. Clubb Crystal structure of the excisionase-DNA complex from bacteriophage lambda J. Mol. Biol. 338 2004 229 240
    • (2004) J. Mol. Biol. , vol.338 , pp. 229-240
    • Sam, M.D.1    Cascio, D.2    Johnson, R.C.3    Clubb, R.T.4
  • 49
    • 0346880111 scopus 로고    scopus 로고
    • Solution structure and stability of the full-length excisionase from bacteriophage HK022
    • V.V. Rogov, C. Lucke, L. Muresanu, H. Wienk, I. Kleinhaus, and K. Werner Solution structure and stability of the full-length excisionase from bacteriophage HK022 Eur. J. Biochem. 270 2003 4846 4858
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4846-4858
    • Rogov, V.V.1    Lucke, C.2    Muresanu, L.3    Wienk, H.4    Kleinhaus, I.5    Werner, K.6
  • 50
    • 0026700238 scopus 로고
    • Characterization of the bacteriophage lambda excisionase (Xis) protein: The C-terminus is required for Xis-integrase cooperativity but not for DNA binding
    • T.E. Numrych, R.I. Gumport, and J.F. Gardner Characterization of the bacteriophage lambda excisionase (Xis) protein: the C-terminus is required for Xis-integrase cooperativity but not for DNA binding EMBO J. 11 1992 3797 3806
    • (1992) EMBO J. , vol.11 , pp. 3797-3806
    • Numrych, T.E.1    Gumport, R.I.2    Gardner, J.F.3
  • 51
    • 0021676510 scopus 로고
    • Determinants of directionality in lambda site-specific recombination
    • W. Bushman, S. Yin, L.L. Thio, and A. Landy Determinants of directionality in lambda site-specific recombination Cell 39 1984 699 706
    • (1984) Cell , vol.39 , pp. 699-706
    • Bushman, W.1    Yin, S.2    Thio, L.L.3    Landy, A.4
  • 52
    • 0037133558 scopus 로고    scopus 로고
    • Arm-site binding by lambda-integrase: Solution structure and functional characterization of its amino-terminal domain
    • J.M. Wojciak, S. Sarkar, A. Landy, and R.T. Clubb Arm-site binding by lambda-integrase: solution structure and functional characterization of its amino-terminal domain Proc. Natl Acad Sci. USA 99 2002 3434 3439
    • (2002) Proc. Natl Acad Sci. USA , vol.99 , pp. 3434-3439
    • Wojciak, J.M.1    Sarkar, S.2    Landy, A.3    Clubb, R.T.4
  • 53
    • 0033614783 scopus 로고    scopus 로고
    • NMR structure and functional studies of the Mu repressor DNA-binding domain
    • U. Ilangovan, J.M. Wojciak, K.M. Connolly, and R.T. Clubb NMR structure and functional studies of the Mu repressor DNA-binding domain Biochemistry-USA 38 1999 8367 8376
    • (1999) Biochemistry-USA , vol.38 , pp. 8367-8376
    • Ilangovan, U.1    Wojciak, J.M.2    Connolly, K.M.3    Clubb, R.T.4
  • 55
    • 0030061917 scopus 로고    scopus 로고
    • The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition
    • R.T. Clubb, M. Mizuuchi, J.R. Huth, J.G. Omichinski, H. Savilahti, and K. Mizuuchi The wing of the enhancer-binding domain of Mu phage transposase is flexible and is essential for efficient transposition Proc. Natl Acad Sci. USA 93 1996 1146 1150
    • (1996) Proc. Natl Acad Sci. USA , vol.93 , pp. 1146-1150
    • Clubb, R.T.1    Mizuuchi, M.2    Huth, J.R.3    Omichinski, J.G.4    Savilahti, H.5    Mizuuchi, K.6
  • 56
    • 0024322147 scopus 로고
    • Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: Implications for regulation
    • M. Mizuuchi, and K. Mizuuchi Efficient Mu transposition requires interaction of transposase with a DNA sequence at the Mu operator: implications for regulation Cell 58 1989 399 408
    • (1989) Cell , vol.58 , pp. 399-408
    • Mizuuchi, M.1    Mizuuchi, K.2
  • 57
    • 0021942310 scopus 로고
    • Interaction of the lambda site-specific recombination protein Xis with attachment site DNA
    • S. Yin, W. Bushman, and A. Landy Interaction of the lambda site-specific recombination protein Xis with attachment site DNA Proc. Natl Acad Sci. USA 82 1985 1040 1044
    • (1985) Proc. Natl Acad Sci. USA , vol.82 , pp. 1040-1044
    • Yin, S.1    Bushman, W.2    Landy, A.3
  • 58
    • 0028023453 scopus 로고
    • Identification of an HP1 phage protein required for site-specific excision
    • D. Esposito, and J.J. Scocca Identification of an HP1 phage protein required for site-specific excision Mol. Microbiol. 13 1994 685 695
    • (1994) Mol. Microbiol. , vol.13 , pp. 685-695
    • Esposito, D.1    Scocca, J.J.2
  • 59
    • 0035170973 scopus 로고    scopus 로고
    • The Mu repressor-DNA complex contains an immobilized "wing" within the minor groove
    • J.M. Wojciak, J. Iwahara, and R.T. Clubb The Mu repressor-DNA complex contains an immobilized "wing" within the minor groove Nature Struct. Biol. 8 2001 84 90
    • (2001) Nature Struct. Biol. , vol.8 , pp. 84-90
    • Wojciak, J.M.1    Iwahara, J.2    Clubb, R.T.3
  • 60
    • 0030004953 scopus 로고    scopus 로고
    • Interactions between the repressor and the early operator region of bacteriophage Mu
    • P. Rousseau, M. Bétermier, M. Chandler, and R. Alazard Interactions between the repressor and the early operator region of bacteriophage Mu J. Biol. Chem. 271 1996 9739 9745
    • (1996) J. Biol. Chem. , vol.271 , pp. 9739-9745
    • Rousseau, P.1    Bétermier, M.2    Chandler, M.3    Alazard, R.4
  • 61
    • 0035282917 scopus 로고    scopus 로고
    • The small DNA binding domain of lambda integrase is a context-sensitive modulator of recombinase functions
    • D. Sarkar, M. Radman-Livaja, and A. Landy The small DNA binding domain of lambda integrase is a context-sensitive modulator of recombinase functions EMBO J. 20 2001 1203 1212
    • (2001) EMBO J. , vol.20 , pp. 1203-1212
    • Sarkar, D.1    Radman-Livaja, M.2    Landy, A.3
  • 62
    • 0036923454 scopus 로고    scopus 로고
    • Differential affinity and cooperativity functions of the amino-terminal 70 residues of lambda integrase
    • D. Sarkar, M.A. Azaro, H. Aihara, C.V. Papagiannis, R. Tirumalai, and S.E. Nunes-Duby Differential affinity and cooperativity functions of the amino-terminal 70 residues of lambda integrase J. Mol. Biol. 324 2002 775 789
    • (2002) J. Mol. Biol. , vol.324 , pp. 775-789
    • Sarkar, D.1    Azaro, M.A.2    Aihara, H.3    Papagiannis, C.V.4    Tirumalai, R.5    Nunes-Duby, S.E.6
  • 63
    • 0015188818 scopus 로고
    • Persistence length of DNA from hydrodynamic measurements
    • H. Triebel, K.E. Reinert, and J. Strassburger Persistence length of DNA from hydrodynamic measurements Biopolymers 10 1971 2619 2621
    • (1971) Biopolymers , vol.10 , pp. 2619-2621
    • Triebel, H.1    Reinert, K.E.2    Strassburger, J.3
  • 64
    • 0032575758 scopus 로고    scopus 로고
    • Defining the structural and functional roles of the carboxyl region of the bacteriophage lambda excisionase (Xis) protein
    • Z. Wu, R.I. Gumport, and J.F. Gardner Defining the structural and functional roles of the carboxyl region of the bacteriophage lambda excisionase (Xis) protein J. Mol. Biol. 281 1998 651 661
    • (1998) J. Mol. Biol. , vol.281 , pp. 651-661
    • Wu, Z.1    Gumport, R.I.2    Gardner, J.F.3
  • 65
    • 0021272019 scopus 로고
    • Regeneration of insertionally inactivated streptococcal DNA fragments after excision of transposon Tn916 in Escherichia coli: Strategy for targeting and cloning of genes from Gram-positive bacteria
    • C. Gawron-Burke, and D.B. Clewell Regeneration of insertionally inactivated streptococcal DNA fragments after excision of transposon Tn916 in Escherichia coli: strategy for targeting and cloning of genes from Gram-positive bacteria J. Bacteriol. 159 1984 214 221
    • (1984) J. Bacteriol. , vol.159 , pp. 214-221
    • Gawron-Burke, C.1    Clewell, D.B.2
  • 67
    • 0031849661 scopus 로고    scopus 로고
    • Site-specific DNA binding using a variation of the double stranded RNA binding motif
    • K.M. Connolly, J.M. Wojciak, and R.T. Clubb Site-specific DNA binding using a variation of the double stranded RNA binding motif Nature Struct. Biol. 5 1998 546 550
    • (1998) Nature Struct. Biol. , vol.5 , pp. 546-550
    • Connolly, K.M.1    Wojciak, J.M.2    Clubb, R.T.3
  • 68
    • 44049117010 scopus 로고
    • Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein
    • S. Grzesiek, and A. Bax Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein J. Magn. Reson. 96 1992 432 440
    • (1992) J. Magn. Reson. , vol.96 , pp. 432-440
    • Grzesiek, S.1    Bax, A.2
  • 69
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins
    • M. Wittekind, and L. Mueller HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha-carbon and beta-carbon resonances in proteins J. Magn. Reson. 101 1993 201 205
    • (1993) J. Magn. Reson. , vol.101 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 70
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR
    • S. Grzesiek, and A. Bax Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR J. Am. Chem. Soc. 114 1992 6291 6293
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 71
    • 43949175202 scopus 로고
    • Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization
    • S. Grzesiek, J. Anglister, and A. Bax Correlation of backbone amide and aliphatic side-chain resonances in C-13/N-15-enriched proteins by isotropic mixing of C-13 magnetization J. Magn. Reson. ser. B 101 1993 114 119
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 114-119
    • Grzesiek, S.1    Anglister, J.2    Bax, A.3
  • 73
    • 0026225733 scopus 로고
    • 13C-labeled protein using constant-time evolution
    • 13C-labeled protein using constant-time evolution J. Biomol. NMR 1 1991 299 304
    • (1991) J. Biomol. NMR , vol.1 , pp. 299-304
    • Ikura, I.1    Kay, L.E.2    Bax, A.3
  • 75
    • 12044259775 scopus 로고
    • Quantitative J correlation - A new approach for measuring homonuclear 3-bond J(H(N)H(Alpha)) coupling constants in N-15-enriched proteins
    • G.W. Vuister, and A. Bax Quantitative J correlation - a new approach for measuring homonuclear 3-bond J(H(N)H(Alpha)) coupling constants in N-15-enriched proteins J. Am. Chem. Soc. 115 1993 7772 7777
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 7772-7777
    • Vuister, G.W.1    Bax, A.2
  • 76
    • 0001654819 scopus 로고
    • An alternative 3D-NMR technique for correlating backbone N-15 with side-chain H-beta-resonances in larger proteins
    • S.J. Archer, M. Ikura, D.A. Torchia, and A. Bax An alternative 3D-NMR technique for correlating backbone N-15 with side-chain H-beta-resonances in larger proteins J. Magn. Reson. 95 1991 636 641
    • (1991) J. Magn. Reson. , vol.95 , pp. 636-641
    • Archer, S.J.1    Ikura, M.2    Torchia, D.A.3    Bax, A.4
  • 77
    • 0026159281 scopus 로고
    • Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartman-Hahn and C13-separated rotating frame Overhauser spectroscopy
    • G.M. Clore, A. Bax, and G.M. Gronenborn Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartman-Hahn and C13-separated rotating frame Overhauser spectroscopy J. Biomol. NMR 1 1991 13 22
    • (1991) J. Biomol. NMR , vol.1 , pp. 13-22
    • Clore, G.M.1    Bax, A.2    Gronenborn, G.M.3
  • 78
    • 0000470905 scopus 로고
    • Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra
    • S.W. Fesik, and E.R.P. Zuiderweg Heteronuclear three-dimensional NMR spectroscopy. A strategy for the simplification of homonuclear two-dimensional NMR spectra J. Magn. Reson. 78 1988 588 593
    • (1988) J. Magn. Reson. , vol.78 , pp. 588-593
    • Fesik, S.W.1    Zuiderweg, E.R.P.2
  • 79
    • 0013498057 scopus 로고
    • Increased resolution and improved spectral quality in 4-dimensional C-13/C-13-separated HMQC-NOESY-HMQC spectra using pulsed field gradients
    • G.W. Vuister, G.M. Clore, A.M. Gronenborn, R. Powers, D.S. Garrett, R. Tschudin, and A. Bax Increased resolution and improved spectral quality in 4-dimensional C-13/C-13-separated HMQC-NOESY-HMQC spectra using pulsed field gradients J. Magn. Reson. ser. B 101 1993 210 213
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 210-213
    • Vuister, G.W.1    Clore, G.M.2    Gronenborn, A.M.3    Powers, R.4    Garrett, D.S.5    Tschudin, R.6    Bax, A.7
  • 80
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenar Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J. Biomol. NMR 2 1992 661 665
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 82
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automated computer analysis of contour diagrams
    • D.S. Garrett, R. Powers, A.M. Gronenborn, and G.M. Clore A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automated computer analysis of contour diagrams J. Magn. Reson. 95 1991 214 220
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 84
    • 0028432974 scopus 로고
    • The impact of direct refinement against three-bond HN-CαH coupling constants on protein determination by NMR
    • D.S. Garrett The impact of direct refinement against three-bond HN-CαH coupling constants on protein determination by NMR J. Magn. Reson. ser. B 104 1994 99 103
    • (1994) J. Magn. Reson. Ser. B , vol.104 , pp. 99-103
    • Garrett, D.S.1
  • 85
    • 0030000912 scopus 로고    scopus 로고
    • Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
    • J. Kuszewski, A.M. Gronenborn, and G.M. Clore Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases Protein Sci. 5 1996 1067 1080
    • (1996) Protein Sci. , vol.5 , pp. 1067-1080
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 86
    • 0031083293 scopus 로고    scopus 로고
    • Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
    • J. Kuszewski, A.M. Gronenborn, and G.M. Clore Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids J. Magn. Reson. 125 1997 171 177
    • (1997) J. Magn. Reson. , vol.125 , pp. 171-177
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 87
    • 0023732144 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamic simulated annealing
    • M. Nilges, G.M. Clore, and A.M. Gronenborn Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamic simulated annealing FEBS Letters 229 1988 129 136
    • (1988) FEBS Letters , vol.229 , pp. 129-136
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 89
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 90
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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