메뉴 건너뛰기




Volumn 580, Issue 8, 2006, Pages 1919-1924

Specificity in DNA recognition by a peptide from papillomavirus E2 protein

Author keywords

DNA; E2 protein; Molecular recognition; Papillomavirus; Peptide

Indexed keywords

ALPHA1E2 PEPTIDE; BINDING PROTEIN; GLYCOPROTEIN E2; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 33645220778     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.02.047     Document Type: Article
Times cited : (5)

References (30)
  • 1
    • 0000127073 scopus 로고
    • Sequence-specific recognition of double helical nucleic acids by proteins
    • N.C. Seeman, J.M. Rosenberg, and A. Rich Sequence-specific recognition of double helical nucleic acids by proteins Proc. Natl. Acad. Sci. USA 73 1976 804 808
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 804-808
    • Seeman, N.C.1    Rosenberg, J.M.2    Rich, A.3
  • 2
    • 0028839860 scopus 로고
    • Comprehensive analysis of hydrogen bonds in regulatory protein DNA-complexes: In search of common principles
    • Y. Mandel-Gutfreund, O. Schueler, and H. Margalit Comprehensive analysis of hydrogen bonds in regulatory protein DNA-complexes: in search of common principles J. Mol. Biol. 253 1995 370 382
    • (1995) J. Mol. Biol. , vol.253 , pp. 370-382
    • Mandel-Gutfreund, Y.1    Schueler, O.2    Margalit, H.3
  • 3
    • 0035393302 scopus 로고    scopus 로고
    • Amino-acid-base interactions: A three-dimensional analysis of protein-DNA interactions at an atomic level
    • N.M. Luscombe, R.A. Laskowski, and J.M. Thorton Amino-acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level Nucleic Acids Res. 29 2001 2860 2874
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2860-2874
    • Luscombe, N.M.1    Laskowski, R.A.2    Thorton, J.M.3
  • 4
    • 0025953354 scopus 로고
    • The papillomavirus E2 regulatory proteins
    • A.A. McBride, H. Romanczuk, and P.M. Howley The papillomavirus E2 regulatory proteins J. Biol. Chem. 266 1991 18411 18414
    • (1991) J. Biol. Chem. , vol.266 , pp. 18411-18414
    • McBride, A.A.1    Romanczuk, H.2    Howley, P.M.3
  • 5
    • 0345304716 scopus 로고    scopus 로고
    • Comparison of the structure and DNA-binding properties of the E2 proteins from an oncogenic and a non-oncogenic human papillomavirus
    • G. Dell, K.W. Wilkinson, R. Tranter, J. Parish, R. Leo-Brady, and K. Gaston Comparison of the structure and DNA-binding properties of the E2 proteins from an oncogenic and a non-oncogenic human papillomavirus J. Mol. Biol. 334 2003 979 991
    • (2003) J. Mol. Biol. , vol.334 , pp. 979-991
    • Dell, G.1    Wilkinson, K.W.2    Tranter, R.3    Parish, J.4    Leo-Brady, R.5    Gaston, K.6
  • 6
    • 0036086459 scopus 로고    scopus 로고
    • The papillomavirus E2 proteins: Structure, function, and biology
    • R.S. Hegde The papillomavirus E2 proteins: structure, function, and biology Annu. Rev. Biophys. Biomol. Struct. 31 2002 343 360
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 343-360
    • Hegde, R.S.1
  • 7
    • 0026335812 scopus 로고
    • Structural analysis of the human papillomavirus type16-E2 transactivator with antipeptide antibodies reveals a high mobility region linking the transactivation and the DNA-binding domains
    • J.M. Gauthier, J. Dillner, and M. Yaniv Structural analysis of the human papillomavirus type16-E2 transactivator with antipeptide antibodies reveals a high mobility region linking the transactivation and the DNA-binding domains Nucleic Acids Res. 19 1991 7073 7079
    • (1991) Nucleic Acids Res. , vol.19 , pp. 7073-7079
    • Gauthier, J.M.1    Dillner, J.2    Yaniv, M.3
  • 8
    • 2542423588 scopus 로고    scopus 로고
    • Casein kinase II phosphorylation-induced conformational switch triggers degradation of the papillomavirus E2 protein
    • K.J. Penrose, M. Garcia-Alai, G. Prat-Gay, and A.A. McBride Casein kinase II phosphorylation-induced conformational switch triggers degradation of the papillomavirus E2 protein J. Biol. Chem. 279 2004 22430 22439
    • (2004) J. Biol. Chem. , vol.279 , pp. 22430-22439
    • Penrose, K.J.1    Garcia-Alai, M.2    Prat-Gay, G.3    McBride, A.A.4
  • 9
    • 0026656038 scopus 로고
    • Crystal structure at 1.7 a of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target
    • R.S. Hegde, S.R. Grossman, L.A. Laimins, and P.B. Sigler Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target Nature 359 1992 505 512
    • (1992) Nature , vol.359 , pp. 505-512
    • Hegde, R.S.1    Grossman, S.R.2    Laimins, L.A.3    Sigler, P.B.4
  • 10
    • 0034613274 scopus 로고    scopus 로고
    • The structural basis of DNA target discrimination by papillomavirus E2 proteins
    • S.-S. Kim, J.K. Tam, A.-F. Wang, and R.S. Hedge The structural basis of DNA target discrimination by papillomavirus E2 proteins J. Biol. Chem. 275 2000 31245 31254
    • (2000) J. Biol. Chem. , vol.275 , pp. 31245-31254
    • Kim, S.-S.1    Tam, J.K.2    Wang, A.-F.3    Hedge, R.S.4
  • 11
    • 25444493135 scopus 로고    scopus 로고
    • Free energy contributions to direct readout of a DNA sequence
    • D.U. Ferreiro, M. Dellarole, A.D. Nadra, and G. Prat-Gay Free energy contributions to direct readout of a DNA sequence J. Biol. Chem. 280 2005 32480 32484
    • (2005) J. Biol. Chem. , vol.280 , pp. 32480-32484
    • Ferreiro, D.U.1    Dellarole, M.2    Nadra, A.D.3    Prat-Gay, G.4
  • 12
    • 0032489497 scopus 로고    scopus 로고
    • DNA structure and flexibility in the sequence-specific binding of papillomavirus E2 proteins
    • C.S. Hines, C. Meghoo, S. Shetty, M. Biburger, M. Brenowits, and R.S. Hedge DNA structure and flexibility in the sequence-specific binding of papillomavirus E2 proteins J. Mol. Biol. 276 1998 809 818
    • (1998) J. Mol. Biol. , vol.276 , pp. 809-818
    • Hines, C.S.1    Meghoo, C.2    Shetty, S.3    Biburger, M.4    Brenowits, M.5    Hedge, R.S.6
  • 13
    • 2542421763 scopus 로고    scopus 로고
    • The role of DNA structure and dynamics in the recognition of bovine papillomavirus E2 protein target sequences
    • D. Djuranovic, C. Oguey, and B. Hartmann The role of DNA structure and dynamics in the recognition of bovine papillomavirus E2 protein target sequences J. Mol. Biol. 339 2004 785 796
    • (2004) J. Mol. Biol. , vol.339 , pp. 785-796
    • Djuranovic, D.1    Oguey, C.2    Hartmann, B.3
  • 15
    • 0034687674 scopus 로고    scopus 로고
    • DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume
    • L.M. Lima, D. Foguel, and J.L. Silva DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume Proc. Natl. Acad. Sci. USA 97 2000 14289 14294
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14289-14294
    • Lima, L.M.1    Foguel, D.2    Silva, J.L.3
  • 16
    • 0034681384 scopus 로고    scopus 로고
    • LexA repressor forms stable dimers in solution. the role of specific DNA in tightening protein-protein interactions
    • R. Mohana-Borges, A.B. Pacheco, F.J. Souza, D. Foguel, D.F. Almeida, and J.L. Silva LexA repressor forms stable dimers in solution. The role of specific DNA in tightening protein-protein interactions J. Biol. Chem. 275 2000 4708 4712
    • (2000) J. Biol. Chem. , vol.275 , pp. 4708-4712
    • Mohana-Borges, R.1    Pacheco, A.B.2    Souza, F.J.3    Foguel, D.4    Almeida, D.F.5    Silva, J.L.6
  • 17
    • 9144229585 scopus 로고    scopus 로고
    • Positive contribution of hydration on DNA binding by E2c protein from papillomavirus
    • L.M. Lima, and J.L. Silva Positive contribution of hydration on DNA binding by E2c protein from papillomavirus J. Biol. Chem. 279 2004 47968 47974
    • (2004) J. Biol. Chem. , vol.279 , pp. 47968-47974
    • Lima, L.M.1    Silva, J.L.2
  • 18
    • 0029737547 scopus 로고    scopus 로고
    • Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: Multiple conformers of single-stranded and double-stranded dye-DNA complexes
    • G. Vamosi, C. Gohlke, and R.M. Clegg Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes Biophys. J. 71 1996 972 994
    • (1996) Biophys. J. , vol.71 , pp. 972-994
    • Vamosi, G.1    Gohlke, C.2    Clegg, R.M.3
  • 20
  • 21
    • 0034727658 scopus 로고    scopus 로고
    • Distinctive cognate sequence discrimination, bound DNA conformation, and binding modes in the E2 C-terminal domains from prototype human and bovine papillomaviruses
    • D.U. Ferreiro, L.M. Lima, A.D. Nadra, L.G. Alonso, F.A. Goldbaum, and G. Prat-Gay Distinctive cognate sequence discrimination, bound DNA conformation, and binding modes in the E2 C-terminal domains from prototype human and bovine papillomaviruses Biochemistry 39 2000 14692 14701
    • (2000) Biochemistry , vol.39 , pp. 14692-14701
    • Ferreiro, D.U.1    Lima, L.M.2    Nadra, A.D.3    Alonso, L.G.4    Goldbaum, F.A.5    Prat-Gay, G.6
  • 23
    • 0030876594 scopus 로고    scopus 로고
    • Conformational changes and stabilization induced by ligand binding in the DNA-binding domain of the E2 protein from human papillomavirus
    • L.M. Lima, and G. Prat-Gay Conformational changes and stabilization induced by ligand binding in the DNA-binding domain of the E2 protein from human papillomavirus J. Biol. Chem. 272 1997 19295 19303
    • (1997) J. Biol. Chem. , vol.272 , pp. 19295-19303
    • Lima, L.M.1    Prat-Gay, G.2
  • 25
    • 0030068229 scopus 로고    scopus 로고
    • Solution structure of the DNA-binding domain of a human papillomavirus E2 protein: Evidence for flexible DNA-binding regions
    • H. Liang, A.M. Petros, R.P. Meadows, H.S. Yoon, D.A. Egan, K. Walter, T.F. Holzman, T. Robins, and S.W. Fesik Solution structure of the DNA-binding domain of a human papillomavirus E2 protein: evidence for flexible DNA-binding regions Biochemistry 35 1996 2095 2103
    • (1996) Biochemistry , vol.35 , pp. 2095-2103
    • Liang, H.1    Petros, A.M.2    Meadows, R.P.3    Yoon, H.S.4    Egan, D.A.5    Walter, K.6    Holzman, T.F.7    Robins, T.8    Fesik, S.W.9
  • 26
    • 0028589386 scopus 로고
    • Kinetic and equilibrium binding studies of the human papillomavirus type-16 transcription regulatory protein E2 interacting with core enhancer elements
    • C.M. Sanders, and N.J. Maitland Kinetic and equilibrium binding studies of the human papillomavirus type-16 transcription regulatory protein E2 interacting with core enhancer elements Nucleic Acids Res. 22 1994 4890 4897
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4890-4897
    • Sanders, C.M.1    Maitland, N.J.2
  • 27
    • 0030932572 scopus 로고    scopus 로고
    • DNA binding and bending by the human papillomavirus type 16 E2 protein. Recognition of an extended binding site
    • A. Thain, K. Webster, D. Emery, A.R. Clarke, and K. Gaston DNA binding and bending by the human papillomavirus type 16 E2 protein. Recognition of an extended binding site J. Biol. Chem. 272 1997 8236 8242
    • (1997) J. Biol. Chem. , vol.272 , pp. 8236-8242
    • Thain, A.1    Webster, K.2    Emery, D.3    Clarke, A.R.4    Gaston, K.5
  • 28
    • 0033544725 scopus 로고    scopus 로고
    • Magnesium ions enhance the transfer of human papillomavirus E2 protein from non-specific to specific binding sites
    • H. Lewis, and K. Gaston Magnesium ions enhance the transfer of human papillomavirus E2 protein from non-specific to specific binding sites J. Mol. Biol. 294 1999 885 896
    • (1999) J. Mol. Biol. , vol.294 , pp. 885-896
    • Lewis, H.1    Gaston, K.2
  • 29
    • 0345604432 scopus 로고    scopus 로고
    • Solution measurement of DNA curvature in papillomavirus E2 binding sites
    • J.M. Zimmerman, and L.J. Maher 3rd Solution measurement of DNA curvature in papillomavirus E2 binding sites Nucleic Acids Res. 31 2003 5134 5139
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5134-5139
    • Zimmerman, J.M.1    Maher III, L.J.2
  • 30
    • 0038161225 scopus 로고    scopus 로고
    • A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways
    • D.U. Ferreiro, and G. Prat-Gay A protein-DNA binding mechanism proceeds through multi-state or two-state parallel pathways J. Mol. Biol. 331 2003 89 99
    • (2003) J. Mol. Biol. , vol.331 , pp. 89-99
    • Ferreiro, D.U.1    Prat-Gay, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.