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Volumn 379, Issue 4-5, 1998, Pages 497-504

Protein-Protein and Protein-DNA Interactions in the Type I Restriction Endonuclease R.EcoR124l

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; DNA; DNA METHYLTRANSFERASE; PHENANTHROLINE; RESTRICTION ENDONUCLEASE; THYMIDINE;

EID: 0031969570     PISSN: 01773593     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1998.379.4-5.497     Document Type: Article
Times cited : (42)

References (24)
  • 1
    • 0027324744 scopus 로고
    • Biology of DNA restriction
    • Bickle, T. A., and Krüger, D. H. (1993). Biology of DNA restriction. Microbiol. Rev. 57,434–450.
    • (1993) Microbiol. Rev. , vol.57 , pp. 434-450
    • Bickle, T.A.1    Krüger, D.H.2
  • 2
    • 0029942481 scopus 로고    scopus 로고
    • ATPase activity of the type IC restriction-modification system EcoR124ll
    • Dreier, J., and Bickle, T. A. (1996). ATPase activity of the type IC restriction-modification system EcoR124ll. J. Mol. Biol. 257, 960–969.
    • (1996) J. Mol. Biol. , vol.257 , pp. 960-969
    • Dreier, J.1    Bickle, T.A.2
  • 3
    • 0031049939 scopus 로고    scopus 로고
    • The in vitro assembly of the EcoKI type I DNA restriction/modification enzyme and its in vivo implications
    • Dryden, D. T. F., Cooper, L. R., Thorpe, P. H., and Byron, O. (1997). The in vitro assembly of the EcoKI type I DNA restriction/modification enzyme and its in vivo implications. Biochemistry 36, 1065–1076.
    • (1997) Biochemistry , vol.36 , pp. 1065-1076
    • Dryden, D.T.F.1    Cooper, L.R.2    Thorpe, P.H.3    Byron, O.4
  • 4
    • 0022384336 scopus 로고
    • EcoAand EcoE: Alternatives to the EcoK family of type I restriction and modification systems of Escherichia coli
    • Fuller-Pace, F. V., Cowan, G. M., and Murray, N. E. (1985). EcoAand EcoE: Alternatives to the EcoK family of type I restriction and modification systems of Escherichia coli. J. Mol. Biol. 786, 65–75.
    • (1985) J. Mol. Biol. , vol.786 , pp. 65-75
    • Fuller-Pace, F.V.1    Cowan, G.M.2    Murray, N.E.3
  • 6
    • 0028099459 scopus 로고
    • A symmetrical model for the domain structure of type I DNA methyltransferases
    • Kneale, G. G. (1994). A symmetrical model for the domain structure of type I DNA methyltransferases. J. Mol. Biol. 243,1–5.
    • (1994) J. Mol. Biol. , vol.243 , pp. 1-5
    • Kneale, G.G.1
  • 7
    • 0030596006 scopus 로고    scopus 로고
    • Regulation of the activity of the type IC EcoR124l restriction enzyme
    • Kulik, E. M., and Bickle, T. A. (1996). Regulation of the activity of the type IC EcoR124l restriction enzyme. J. Mol. Biol. 264, 891–906.
    • (1996) J. Mol. Biol. , vol.264 , pp. 891-906
    • Kulik, E.M.1    Bickle, T.A.2
  • 8
    • 0023052463 scopus 로고
    • Nuclease activity of 1,10 phenanthroline-copper ion: reaction with CGCGAATTCGCG and its complexes with netropsin and EcoR1
    • Kuwabara, M. D., Yoon, C., Goyne, T. E., Thederahn, T. B., and Sigman, D. S. (1986). Nuclease activity of 1,10 phenanthroline-copper ion: reaction with CGCGAATTCGCG and its complexes with netropsin and EcoR1. Biochemistry 25,7401–7408.
    • (1986) Biochemistry , vol.25 , pp. 7401-7408
    • Kuwabara, M.D.1    Yoon, C.2    Goyne, T.E.3    Thederahn, T.B.4    Sigman, D.S.5
  • 9
    • 0026490544 scopus 로고
    • Use of gel retardation to analyze protein-nucleic acid interactions
    • Lane, D., Prentki, P., and Chandler, M. (1992). Use of gel retardation to analyze protein-nucleic acid interactions. Microbiological Reviews 56,509–528.
    • (1992) Microbiological Reviews , vol.56 , pp. 509-528
    • Lane, D.1    Prentki, P.2    Chandler, M.3
  • 11
    • 0030457882 scopus 로고    scopus 로고
    • High resolution footprinting of a type I methyltransferase reveals a large structural distortion within the DNA recognition site
    • Mernagh, D. R., and Kneale, G. G. (1996). High resolution footprinting of a type I methyltransferase reveals a large structural distortion within the DNA recognition site. Nucleic Acids Res. 24, 4853–4858.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4853-4858
    • Mernagh, D.R.1    Kneale, G.G.2
  • 12
    • 0028185356 scopus 로고
    • Footprinting with Exonuclease III
    • In Totowa, New Jersey: Humana Press G. G. Kneale, ed.
    • Metzger, W., and Heumann, H. (1995). Footprinting with Exonuclease III. In: Methods in Molecular Biology: DNA-Protein Interactions, G. G. Kneale, ed. (Totowa, New Jersey: Humana Press), pp. 11–20.
    • (1995) Methods in Molecular Biology: DNA-Protein Interactions , pp. 11-20
    • Metzger, W.1    Heumann, H.2
  • 13
    • 0027239508 scopus 로고
    • Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes
    • Murray, N. E., Daniel, A. S., Cowan, G. M., and Sharp, P. M. (1993). Conservation of motifs within the unusually variable polypeptide sequences of type I restriction and modification enzymes. Mol. Microbiology 9,133–143.
    • (1993) Mol. Microbiology , vol.9 , pp. 133-143
    • Murray, N.E.1    Daniel, A.S.2    Cowan, G.M.3    Sharp, P.M.4
  • 14
    • 0020341180 scopus 로고
    • Structural homologies among type I restriction-modification systems
    • Murray, N. E., Gough, J. A., Suri, B., and Bickle, T. A. (1982). Structural homologies among type I restriction-modification systems. EMBO J. 7, 535–539.
    • (1982) EMBO J. , vol.7 , pp. 535-539
    • Murray, N.E.1    Gough, J.A.2    Suri, B.3    Bickle, T.A.4
  • 15
    • 0042352903 scopus 로고
    • 1,10-Phenanthroline-copper ion nuclease footprinting of DNA-protein complexes in situ following mobility-shift
    • In Totowa, New Jersey: Humana Press G. G. Kneale, ed.
    • Papavassiliou, A. G. (1995). 1,10-Phenanthroline-copper ion nuclease footprinting of DNA-protein complexes in situ following mobility-shift. In: Methods in Molecular Biology: DNA-Protein Interactions, G. G. Kneale, ed. (Totowa, New Jersey: Humana Press), pp. 43–78.
    • (1995) Methods in Molecular Biology: DNA-Protein Interactions , pp. 43-78
    • Papavassiliou, A.G.1
  • 16
    • 0028955417 scopus 로고
    • S-adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase
    • Powell, L. M., and Murray, N. E. (1995). S-adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase. Nucleic Acids Res. 23,967–974.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 967-974
    • Powell, L.M.1    Murray, N.E.2
  • 17
    • 0027237522 scopus 로고
    • Delayed expression of in vivo restriction activity following conjugal transfer of Escherichia coli hsdk restriction-modification genes
    • Prakash-Cheng, A., and Ryu, J. (1993). Delayed expression of in vivo restriction activity following conjugal transfer of Escherichia coli hsdk restriction-modification genes. J. Bacteriol. 175, 4905–4906.
    • (1993) J. Bacteriol. , vol.175 , pp. 4905-4906
    • Prakash-Cheng, A.1    Ryu, J.2
  • 18
    • 0022357258 scopus 로고
    • EcoA: The first member of a new family of type I restriction modification systems - Gene organization and enzymatic activities
    • Suri, B., and Bickle, T. A. (1985). EcoA: The first member of a new family of type I restriction modification systems - Gene organization and enzymatic activities. J. Mol. Biol. 186,77–85.
    • (1985) J. Mol. Biol. , vol.186 , pp. 77-85
    • Suri, B.1    Bickle, T.A.2
  • 19
    • 0029910629 scopus 로고    scopus 로고
    • Repercussions of DNA tracking by the type IC restriction endonuclease EcoR124l on linear, circular and catenated substrates
    • Szczelkun, M. D., Dillingham, M. S., Janscak, P., Firman, K., and Halford, S. E. (1996). Repercussions of DNA tracking by the type IC restriction endonuclease EcoR124l on linear, circular and catenated substrates. EMBO J. 75,6335–6347.
    • (1996) EMBO J. , vol.75 , pp. 6335-6347
    • Szczelkun, M.D.1    Dillingham, M.S.2    Janscak, P.3    Firman, K.4    Halford, S.E.5
  • 20
    • 0026503940 scopus 로고
    • Purification and biochemical characterisation of the EcoR124 type I modification methylase
    • Taylor, I., Patel, J., Firman, K., and Kneale, G. (1992). Purification and biochemical characterisation of the EcoR124 type I modification methylase. Nucleic Acids Res. 20,179–186.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 179-186
    • Taylor, I.1    Patel, J.2    Firman, K.3    Kneale, G.4
  • 21
    • 0027427533 scopus 로고
    • Substrate recognition and selectivity in the type IC DNA modification methylase M
    • Taylor, I. A., Watts, D., and Kneale, G. G. (1993). Substrate recognition and selectivity in the type IC DNA modification methylase M. EcoRI 241. Nucleic Acids Res. 27,4929–4935.
    • (1993) EcoRI 241. Nucleic Acids Res. , vol.27 , pp. 4929-4935
    • Taylor, I.A.1    Watts, D.2    Kneale, G.G.3
  • 22
    • 0028029820 scopus 로고
    • DNA binding induces a major structural transition in a type I methyltransferase
    • Taylor, I. A., Davis, K. G., Watts, D., and Kneale, G. G. (1994). DNA binding induces a major structural transition in a type I methyltransferase. EMBO J. 73,5772–5778.
    • (1994) EMBO J. , vol.73 , pp. 5772-5778
    • Taylor, I.A.1    Davis, K.G.2    Watts, D.3    Kneale, G.G.4
  • 23
    • 0029845665 scopus 로고    scopus 로고
    • A third family of allelic hsd genes in Salmonella enterica: sequence comparisons with related proteins identify conserved regions implicated in restriction of DNA
    • Titheradge, A. J. B., Ternant, D., and Murray, N. E. (1996). A third family of allelic hsd genes in Salmonella enterica: sequence comparisons with related proteins identify conserved regions implicated in restriction of DNA. Molecular Microbiology 22, 437–447.
    • (1996) Molecular Microbiology , vol.22 , pp. 437-447
    • Titheradge, A.J.B.1    Ternant, D.2    Murray, N.E.3
  • 24
    • 0026338873 scopus 로고
    • Restriction and modification systems
    • Wilson, G. G., and Murray, N. E. (1991). Restriction and modification systems. Annu. Rev. Genet. 25,585–627.
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 585-627
    • Wilson, G.G.1    Murray, N.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.