메뉴 건너뛰기




Volumn 43, Issue 22, 2004, Pages 6928-6936

T antigen origin-binding domain of simian virus 40: Determinants of specific DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

ANTIGENS; CATALYSIS; DNA; GENETIC ENGINEERING; NUCLEAR MAGNETIC RESONANCE; OLIGOMERS; PH EFFECTS; VIRUSES;

EID: 2642580884     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi030228+     Document Type: Article
Times cited : (10)

References (41)
  • 2
    • 0028226183 scopus 로고
    • Initiation of chromosomal DNA replication in eukaryotes. Lessons from λ
    • Stillman, B. (1994) Initiation of chromosomal DNA replication in eukaryotes. Lessons from λ, J. Biol. Chem. 269, 7047-7050.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7047-7050
    • Stillman, B.1
  • 3
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell, S. P., and Dutta, A. (2002) DNA replication in eukaryotic cells, Annu. Rev. Biochem. 71, 333-374.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 4
    • 0030443808 scopus 로고    scopus 로고
    • Solution structure of the origin DNA-binding domain of SV40 T-antigen
    • Luo, X., Sanford, D. G., Bullock, P. A., and Bachovchin, W. W. (1996) Solution structure of the origin DNA-binding domain of SV40 T-antigen, Nat. Struct. Biol. 3, 1034-1039.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1034-1039
    • Luo, X.1    Sanford, D.G.2    Bullock, P.A.3    Bachovchin, W.W.4
  • 5
    • 0033634815 scopus 로고    scopus 로고
    • Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus
    • Enemark, E. J., Chen, G., Vaughn, D. E., Stenlund, A., and Joshua-Tor, L. (2000) Crystal structure of the DNA binding domain of the replication initiation protein E1 from papillomavirus, Mol. Cell 6, 149-158.
    • (2000) Mol. Cell , vol.6 , pp. 149-158
    • Enemark, E.J.1    Chen, G.2    Vaughn, D.E.3    Stenlund, A.4    Joshua-Tor, L.5
  • 6
    • 0036671409 scopus 로고    scopus 로고
    • Structural unity among viral origin binding proteins. Crystal structure of the nuclease domain of adeno-associated Virus Rep
    • Hickman, A., Ronning, D., Kotin, R., and Dyda, F. (2002) Structural Unity among Viral Origin Binding Proteins. Crystal Structure of the Nuclease Domain of Adeno-Associated Virus Rep, Mol. Cell 10, 327.
    • (2002) Mol. Cell , vol.10 , pp. 327
    • Hickman, A.1    Ronning, D.2    Kotin, R.3    Dyda, F.4
  • 7
    • 0037086545 scopus 로고    scopus 로고
    • Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex
    • Enemark, E. J., Stenlund, A., and Joshua-Tor, L. (2002) Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex, EMBO J. 21, 1487-1496.
    • (2002) EMBO J. , vol.21 , pp. 1487-1496
    • Enemark, E.J.1    Stenlund, A.2    Joshua-Tor, L.3
  • 8
    • 0031405599 scopus 로고    scopus 로고
    • The initiation of simian virus 40 DNA replication in vitro
    • Bullock, P. A. (1997) The initiation of simian virus 40 DNA replication in vitro, Crit. Rev. Biochem. Mol. Biol. 32, 503-568.
    • (1997) Crit. Rev. Biochem. Mol. Biol. , vol.32 , pp. 503-568
    • Bullock, P.A.1
  • 9
    • 0034573640 scopus 로고    scopus 로고
    • SV40 large T antigen functions in DNA replication and transformation
    • Simmons, D. T. (2000) SV40 large T antigen functions in DNA replication and transformation, Adv. Virus Res. 55, 75-134.
    • (2000) Adv. Virus Res. , vol.55 , pp. 75-134
    • Simmons, D.T.1
  • 10
    • 0026540613 scopus 로고
    • Simian virus 40 large T antigen: The puzzle, the pieces, and the emerging picture
    • Fanning, E. (1992) Simian virus 40 large T antigen: the puzzle, the pieces, and the emerging picture, J. Virol. 66, 1289-1293.
    • (1992) J. Virol. , vol.66 , pp. 1289-1293
    • Fanning, E.1
  • 11
    • 0022571136 scopus 로고
    • Domain structure of the simian virus 40 core origin of replication
    • Deb, S., DeLucia, A. L., Baur, C. P., Koff, A., and Tegtmeyer, P. (1986) Domain structure of the simian virus 40 core origin of replication, Mol. Cell. Biol. 6, 1663-1670.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1663-1670
    • Deb, S.1    DeLucia, A.L.2    Baur, C.P.3    Koff, A.4    Tegtmeyer, P.5
  • 12
    • 0030978204 scopus 로고    scopus 로고
    • Purification of the simian virus 40 (SV40) T antigen DNA-binding domain and characterization of its interactions with the SV40 origin
    • Joo, W. S., Luo, X., Denis, D., Kim, H. Y., Rainey, G. J., Jones, C., Sreekumar, K. R., and Bullock, P. A. (1997) Purification of the simian virus 40 (SV40) T antigen DNA-binding domain and characterization of its interactions with the SV40 origin, J. Virol. 71, 3972-3985.
    • (1997) J. Virol. , vol.71 , pp. 3972-3985
    • Joo, W.S.1    Luo, X.2    Denis, D.3    Kim, H.Y.4    Rainey, G.J.5    Jones, C.6    Sreekumar, K.R.7    Bullock, P.A.8
  • 13
    • 0037405947 scopus 로고    scopus 로고
    • Characterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropy
    • Titolo, S., Welchner, E., White, P. W., and Archambault, J. (2003) Characterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropy, J. Virol. 77, 5512-5518.
    • (2003) J. Virol. , vol.77 , pp. 5512-5518
    • Titolo, S.1    Welchner, E.2    White, P.W.3    Archambault, J.4
  • 14
    • 0025320032 scopus 로고
    • Four major sequence elements of simian virus 40 large T antigen coordinate its specific and nonspecific DNA binding
    • Simmons, D. T., Loeber, G., and Tegtmeyer, P. (1990) Four major sequence elements of simian virus 40 large T antigen coordinate its specific and nonspecific DNA binding, J. Virol. 64, 1973-1983.
    • (1990) J. Virol. , vol.64 , pp. 1973-1983
    • Simmons, D.T.1    Loeber, G.2    Tegtmeyer, P.3
  • 15
    • 0030736323 scopus 로고    scopus 로고
    • Protein-DNA recognition complexes: Conservation of structure and binding energy in the transition state
    • Jen-Jacobson, L. (1997) Protein-DNA recognition complexes: conservation of structure and binding energy in the transition state, Biopolymers 44, 153-180.
    • (1997) Biopolymers , vol.44 , pp. 153-180
    • Jen-Jacobson, L.1
  • 16
    • 0141891451 scopus 로고    scopus 로고
    • Initiation of DNA replication: Lessons from viral initiator proteins
    • Stenlund, A. (2003) Initiation of DNA replication: Lessons from viral initiator proteins, Nat. Rev. Mol. Cell. Biol. 4, 777-785.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 777-785
    • Stenlund, A.1
  • 17
    • 0015506470 scopus 로고
    • High-resolution nuclear magnetic resonance study of the histidine-aspartate hydrogen bond in chymotrypsin and chymotrypsinogen
    • Robillard, G., and Shulman, R. G. (1972) High-resolution nuclear magnetic resonance study of the histidine-aspartate hydrogen bond in chymotrypsin and chymotrypsinogen, J. Mol. Biol. 71, 507-511.
    • (1972) J. Mol. Biol. , vol.71 , pp. 507-511
    • Robillard, G.1    Shulman, R.G.2
  • 19
    • 0000706229 scopus 로고
    • The 1-1 hard pulse; a novel, simple, and effective method of water resonance suppressiion in FT-1H NMR
    • Clore, G. M., Kimber, B. J., and Gronenborn, A. M. (1983) The 1-1 hard pulse; a novel, simple, and effective method of water resonance suppressiion in FT-1H NMR, J. Magn. Reson. 54, 170-173.
    • (1983) J. Magn. Reson. , vol.54 , pp. 170-173
    • Clore, G.M.1    Kimber, B.J.2    Gronenborn, A.M.3
  • 20
    • 46149134725 scopus 로고
    • Improvement of dynamic-range in NMR by oversampling
    • Delsuc, M. A., and Lallemand, J. Y. (1986) Improvement of Dynamic-Range in NMR by Oversampling, J. Magn. Reson. 69, 504-507.
    • (1986) J. Magn. Reson. , vol.69 , pp. 504-507
    • Delsuc, M.A.1    Lallemand, J.Y.2
  • 21
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectrocopy
    • Bodenhausen, G., and Ruben, D. J. (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectrocopy, Chem. Phys. Lett. 69, 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 22
    • 45249130688 scopus 로고
    • Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with aqueous solutions
    • Messerle, B., Wider, G., Otting, G., Weber, C., and Wuthrich, K. (1989) Solvent suppression using a spin lock in 2D and 3D NMR spectroscopy with aqueous solutions, J. Magn. Reson. 85, 608-613.
    • (1989) J. Magn. Reson. , vol.85 , pp. 608-613
    • Messerle, B.1    Wider, G.2    Otting, G.3    Weber, C.4    Wuthrich, K.5
  • 23
    • 0028934104 scopus 로고
    • Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin
    • Xia, B., Cheng, H., Skjeldal, L., Coghlan, V. M., Vickery, L. E., and Markley, J. L. (1995) Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin, Biochemistry 34, 180-187.
    • (1995) Biochemistry , vol.34 , pp. 180-187
    • Xia, B.1    Cheng, H.2    Skjeldal, L.3    Coghlan, V.M.4    Vickery, L.E.5    Markley, J.L.6
  • 24
    • 0000018782 scopus 로고
    • A proton-detected heteronuclear chemical-shift correlation experiment with improved resolution and sensitivity
    • Zuiderweg, E. R. P. (1990) A proton-detected heteronuclear chemical-shift correlation experiment with improved resolution and sensitivity, J. Magn. Reson. 86, 246-357.
    • (1990) J. Magn. Reson. , vol.86 , pp. 246-357
    • Zuiderweg, E.R.P.1
  • 25
    • 33947094423 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
    • Bachovchin, W. W., and Roberts, J. D. (1978) Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases, J. Am. Chem. Soc. 100, 8041-8047.
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 8041-8047
    • Bachovchin, W.W.1    Roberts, J.D.2
  • 28
    • 0025019702 scopus 로고
    • Binding and unwinding-How T antigen engages the SV40 origin of DNA replication
    • Borowiec, J. A., Dean, F. B., Bullock, P. A., and Hurwitz, J. (1990) Binding and unwinding-How T antigen engages the SV40 origin of DNA replication, Cell 60, 181-184.
    • (1990) Cell , vol.60 , pp. 181-184
    • Borowiec, J.A.1    Dean, F.B.2    Bullock, P.A.3    Hurwitz, J.4
  • 29
    • 0026223896 scopus 로고
    • A relational database for sequence-specific protein NMR data
    • Seavey, B. R., Farr, E. A., Westler, W. M., and Markley, J. L. (1991) A Relational Database for Sequence-Specific Protein NMR Data, J. Biomol. NMR 1, 217-236.
    • (1991) J. Biomol. NMR , vol.1 , pp. 217-236
    • Seavey, B.R.1    Farr, E.A.2    Westler, W.M.3    Markley, J.L.4
  • 31
    • 0027310940 scopus 로고
    • Biochemical analysis of mutants with changes in the origin-binding domain of simian virus 40 tumor antigen
    • Simmons, D. T., Upson, R., Wun-Kim, K., and Young, W. (1993) Biochemical analysis of mutants with changes in the origin-binding domain of simian virus 40 tumor antigen, J. Virol. 67, 4227-4236.
    • (1993) J. Virol. , vol.67 , pp. 4227-4236
    • Simmons, D.T.1    Upson, R.2    Wun-Kim, K.3    Young, W.4
  • 32
    • 0024095899 scopus 로고
    • Localized melting and structural changes in the SV40 origin of replication induced by T-antigen
    • Borowiec, J. A., and Hurwitz, J. (1988) Localized melting and structural changes in the SV40 origin of replication induced by T-antigen, EMBO J. 7, 3149-3158.
    • (1988) EMBO J. , vol.7 , pp. 3149-3158
    • Borowiec, J.A.1    Hurwitz, J.2
  • 33
    • 0025096688 scopus 로고
    • Three domains in the simian virus 40 core origin orchestrate the binding, melting, and DNA helicase activities of T antigen
    • Parsons, R., Anderson, M. E., and Tegtmeyer, P. (1990) Three domains in the simian virus 40 core origin orchestrate the binding, melting, and DNA helicase activities of T antigen, J. Virol. 64, 509-518.
    • (1990) J. Virol. , vol.64 , pp. 509-518
    • Parsons, R.1    Anderson, M.E.2    Tegtmeyer, P.3
  • 34
    • 0032837332 scopus 로고    scopus 로고
    • Sequence requirements for the assembly of simian virus 40 T antigen and the T-antigen origin binding domain on the viral core origin of replication
    • Kim, H. Y., Barbaro, B. A., Joo, W. S., Prack, A. E., Sreekumar, K. R., and Bullock, P. A. (1999) Sequence requirements for the assembly of simian virus 40 T antigen and the T-antigen origin binding domain on the viral core origin of replication, J. Virol. 73, 7543-7555.
    • (1999) J. Virol. , vol.73 , pp. 7543-7555
    • Kim, H.Y.1    Barbaro, B.A.2    Joo, W.S.3    Prack, A.E.4    Sreekumar, K.R.5    Bullock, P.A.6
  • 35
    • 0031467141 scopus 로고    scopus 로고
    • Initiation of DNA replication in eukaryotic cells
    • Dutta, A., and Bell, S. P. (1997) Initiation of DNA replication in eukaryotic cells, Annu. Rev. Cell Dev. Biol. 13, 293-332.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 293-332
    • Dutta, A.1    Bell, S.P.2
  • 36
    • 0025151570 scopus 로고
    • Identification of simian virus 40 T-antigen residues important for specific and nonspecific binding to DNA and for helicase activity
    • Simmons, D. T., Wun-Kim, K., and Young, W. (1990) Identification of simian virus 40 T-antigen residues important for specific and nonspecific binding to DNA and for helicase activity, J. Virol. 64, 4858-4865.
    • (1990) J. Virol. , vol.64 , pp. 4858-4865
    • Simmons, D.T.1    Wun-Kim, K.2    Young, W.3
  • 38
    • 0027333348 scopus 로고
    • Tickling the TCR: Selective T-cell functions stimulated by altered peptide ligands
    • Evavold, B. D., Sloan-Lancaster, J., and Allen, P. M. (1993) Tickling the TCR: Selective T-cell functions stimulated by altered peptide ligands, Immunol. Today 14, 602-609.
    • (1993) Immunol. Today , vol.14 , pp. 602-609
    • Evavold, B.D.1    Sloan-Lancaster, J.2    Allen, P.M.3
  • 39
    • 0032968708 scopus 로고    scopus 로고
    • The dynamics of T cell receptor signaling: Complex orchestration and the key roles of tempo and cooperation
    • Germain, R. N., and Stefanova, I. (1999) The dynamics of T cell receptor signaling: complex orchestration and the key roles of tempo and cooperation, Annu. Rev. Immunol. 17, 467-522.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 467-522
    • Germain, R.N.1    Stefanova, I.2
  • 40
    • 0037450701 scopus 로고    scopus 로고
    • E1 initiator DNA binding specificity is unmasked by selective inhibition of nonspecific DNA binding
    • Stenlund, A. (2003) E1 initiator DNA binding specificity is unmasked by selective inhibition of nonspecific DNA binding, EMBO J. 22, 954-963.
    • (2003) EMBO J. , vol.22 , pp. 954-963
    • Stenlund, A.1
  • 41
    • 0029617680 scopus 로고
    • Cooperative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro
    • Sedman, J., and Stenlund, A. (1995) Cooperative interaction between the initiator E1 and the transcriptional activator E2 is required for replicator specific DNA replication of bovine papillomavirus in vivo and in vitro, EMBO J. 14, 6218-6228.
    • (1995) EMBO J. , vol.14 , pp. 6218-6228
    • Sedman, J.1    Stenlund, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.