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Volumn 387, Issue 5, 2009, Pages 1309-1319

Functional Characterization and Modulation of the DNA Cleavage Efficiency of Type III Restriction Endonuclease EcoP15I in Its Interaction with Two Sites in the DNA Target

Author keywords

AdoMet analogue; EcoP15I; flanking bases; SuperSAGE; Type III restriction endonuclease

Indexed keywords

ENDONUCLEASE; SINEFUNGIN;

EID: 63449097890     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.02.047     Document Type: Article
Times cited : (20)

References (30)
  • 1
  • 2
    • 0026584744 scopus 로고
    • Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage
    • Meisel A., Bickle T.A., Kruger D.H., and Schroeder C. Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage. Nature 355 (1992) 467-469
    • (1992) Nature , vol.355 , pp. 467-469
    • Meisel, A.1    Bickle, T.A.2    Kruger, D.H.3    Schroeder, C.4
  • 3
    • 0029045067 scopus 로고
    • Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis
    • Meisel A., Mackeldanz P., Bickle T.A., Kruger D.H., and Schroeder C. Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis. EMBO J. 14 (1995) 2958-2966
    • (1995) EMBO J. , vol.14 , pp. 2958-2966
    • Meisel, A.1    Mackeldanz, P.2    Bickle, T.A.3    Kruger, D.H.4    Schroeder, C.5
  • 4
    • 0035883536 scopus 로고    scopus 로고
    • Nucleoside triphosphate-dependent restriction enzymes
    • Dryden D.T.F., Murray N.E., and Rao D.N. Nucleoside triphosphate-dependent restriction enzymes. Nucleic Acids Res. 29 (2001) 3728-3741
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3728-3741
    • Dryden, D.T.F.1    Murray, N.E.2    Rao, D.N.3
  • 5
    • 0036880785 scopus 로고    scopus 로고
    • Complex restriction enzymes: NTP-driven molecular motors
    • Bourniquel A.A., and Bickle T.A. Complex restriction enzymes: NTP-driven molecular motors. Biochimie 84 (2002) 1047-1059
    • (2002) Biochimie , vol.84 , pp. 1047-1059
    • Bourniquel, A.A.1    Bickle, T.A.2
  • 7
    • 0035936699 scopus 로고    scopus 로고
    • Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I
    • Janscak P., Sandmeier U., Szczelkun M.D., and Bickle T.A. Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I. J. Mol. Biol. 306 (2001) 417-431
    • (2001) J. Mol. Biol. , vol.306 , pp. 417-431
    • Janscak, P.1    Sandmeier, U.2    Szczelkun, M.D.3    Bickle, T.A.4
  • 8
    • 33846277899 scopus 로고    scopus 로고
    • Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis
    • Wagenfuhr K., Pieper S., Mackeldanz P., Linscheid M., Kruger D.H., and Reuter M. Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis. J. Mol. Biol. 366 (2007) 93-102
    • (2007) J. Mol. Biol. , vol.366 , pp. 93-102
    • Wagenfuhr, K.1    Pieper, S.2    Mackeldanz, P.3    Linscheid, M.4    Kruger, D.H.5    Reuter, M.6
  • 9
    • 0035965141 scopus 로고    scopus 로고
    • DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sites
    • Mucke M., Reich S., Moncke-Buchner E., Reuter M., and Kruger D.H. DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sites. J. Mol. Biol. 312 (2001) 687-698
    • (2001) J. Mol. Biol. , vol.312 , pp. 687-698
    • Mucke, M.1    Reich, S.2    Moncke-Buchner, E.3    Reuter, M.4    Kruger, D.H.5
  • 10
    • 34547883904 scopus 로고    scopus 로고
    • Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping
    • Crampton N., Yokokawa M., Dryden D.T., Edwardson J.M., Rao D.N., Takeyasu K., et al. Fast-scan atomic force microscopy reveals that the type III restriction enzyme EcoP15I is capable of DNA translocation and looping. Proc. Natl. Acad. Sci. USA 104 (2007) 12755-12760
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12755-12760
    • Crampton, N.1    Yokokawa, M.2    Dryden, D.T.3    Edwardson, J.M.4    Rao, D.N.5    Takeyasu, K.6
  • 11
    • 34548105170 scopus 로고    scopus 로고
    • DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes
    • Crampton N., Roes S., Dryden D.T., Rao D.N., Edwardson J.M., and Henderson R.M. DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes. EMBO J. 26 (2007) 3815-3825
    • (2007) EMBO J. , vol.26 , pp. 3815-3825
    • Crampton, N.1    Roes, S.2    Dryden, D.T.3    Rao, D.N.4    Edwardson, J.M.5    Henderson, R.M.6
  • 12
    • 3342967880 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA translocation by the type III restriction enzyme EcoP15I
    • Reich S., Gossl I., Reuter M., Rabe J.P., and Kruger D.H. Scanning force microscopy of DNA translocation by the type III restriction enzyme EcoP15I. J. Mol. Biol. 341 (2004) 337-343
    • (2004) J. Mol. Biol. , vol.341 , pp. 337-343
    • Reich, S.1    Gossl, I.2    Reuter, M.3    Rabe, J.P.4    Kruger, D.H.5
  • 13
    • 6344287290 scopus 로고    scopus 로고
    • Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by type III restriction enzyme
    • Raghavendra N.K., and Rao D.N. Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by type III restriction enzyme. Nucleic Acids Res. 32 (2004) 5703-5711
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5703-5711
    • Raghavendra, N.K.1    Rao, D.N.2
  • 16
    • 0141645630 scopus 로고    scopus 로고
    • S-adenosyl methionine prevents promiscuous DNA cleavage by the EcoP1I type III restriction enzyme
    • Peakman L.J., Antognozzi M., Bickle T.A., Janscak P., and Szczelkun M.D. S-adenosyl methionine prevents promiscuous DNA cleavage by the EcoP1I type III restriction enzyme. J. Mol. Biol. 333 (2003) 321-335
    • (2003) J. Mol. Biol. , vol.333 , pp. 321-335
    • Peakman, L.J.1    Antognozzi, M.2    Bickle, T.A.3    Janscak, P.4    Szczelkun, M.D.5
  • 17
    • 22744453077 scopus 로고    scopus 로고
    • Exogenous AdoMet and its analogue sinefungin differentially influence DNA cleavage by R.EcoP15I-usefulness in SAGE
    • Raghavendra N.K., and Rao D.N. Exogenous AdoMet and its analogue sinefungin differentially influence DNA cleavage by R.EcoP15I-usefulness in SAGE. Biochem. Biophys. Res. Commun. 334 (2005) 803-811
    • (2005) Biochem. Biophys. Res. Commun. , vol.334 , pp. 803-811
    • Raghavendra, N.K.1    Rao, D.N.2
  • 20
    • 0016614406 scopus 로고
    • Studies on the cleavage of bacteriophage lambda DNA with EcoRI restriction endonuclease
    • Thomas M., and Davis R.W. Studies on the cleavage of bacteriophage lambda DNA with EcoRI restriction endonuclease. J. Mol. Biol. 91 (1975) 315-328
    • (1975) J. Mol. Biol. , vol.91 , pp. 315-328
    • Thomas, M.1    Davis, R.W.2
  • 21
    • 0020688831 scopus 로고
    • Cloned restriction/modification system from Pseudomonas aeruginosa
    • Gingeras T.R., and Brooks J.E. Cloned restriction/modification system from Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 80 (1983) 402-406
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 402-406
    • Gingeras, T.R.1    Brooks, J.E.2
  • 22
    • 0026569359 scopus 로고
    • The activity of the EcoRV restriction endonuclease is influenced by flanking DNA sequences both inside and outside the DNA-protein complex
    • Taylor J.D., and Halford S.E. The activity of the EcoRV restriction endonuclease is influenced by flanking DNA sequences both inside and outside the DNA-protein complex. Biochemistry 31 (1992) 90-97
    • (1992) Biochemistry , vol.31 , pp. 90-97
    • Taylor, J.D.1    Halford, S.E.2
  • 23
    • 0026792902 scopus 로고
    • Nonidentical DNA-binding sites of endonuclease NaeI recognize different families of sequences flanking the recognition site
    • Yang C.C., and Topal M.D. Nonidentical DNA-binding sites of endonuclease NaeI recognize different families of sequences flanking the recognition site. Biochemistry 31 (1992) 9657-9664
    • (1992) Biochemistry , vol.31 , pp. 9657-9664
    • Yang, C.C.1    Topal, M.D.2
  • 24
    • 0035297698 scopus 로고    scopus 로고
    • SfiI endonuclease activity is strongly influenced by the non-specific sequence in the middle of its recognition site
    • Williams S.A., and Halford S.E. SfiI endonuclease activity is strongly influenced by the non-specific sequence in the middle of its recognition site. Nucleic Acids Res. 29 (2001) 1476-1483
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1476-1483
    • Williams, S.A.1    Halford, S.E.2
  • 25
    • 24144454859 scopus 로고    scopus 로고
    • Characterization of the type III restriction endonuclease PstII from Providencia stuartii
    • Sears A., Peakman L.J., Wilson G.G., and Szczelkun M.D. Characterization of the type III restriction endonuclease PstII from Providencia stuartii. Nucleic Acids Res. 33 (2005) 4775-4787
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4775-4787
    • Sears, A.1    Peakman, L.J.2    Wilson, G.G.3    Szczelkun, M.D.4
  • 26
    • 0018800362 scopus 로고
    • Methylation and cleavage sequences of the EcoP1 restriction-modification enzyme
    • Bachi B., Reiser J., and Pirrotta V. Methylation and cleavage sequences of the EcoP1 restriction-modification enzyme. J. Mol. Biol. 128 (1979) 143-163
    • (1979) J. Mol. Biol. , vol.128 , pp. 143-163
    • Bachi, B.1    Reiser, J.2    Pirrotta, V.3
  • 27
    • 0019203695 scopus 로고
    • Role of ATP in the cleavage mechanism of the EcoP15 restriction endonuclease
    • Yuan R., Hamilton D.L., Hadi S.M., and Bickle T.A. Role of ATP in the cleavage mechanism of the EcoP15 restriction endonuclease. J. Mol. Biol. 144 (1980) 501-519
    • (1980) J. Mol. Biol. , vol.144 , pp. 501-519
    • Yuan, R.1    Hamilton, D.L.2    Hadi, S.M.3    Bickle, T.A.4
  • 28
    • 50649123011 scopus 로고    scopus 로고
    • Modulation of Escherichia coli DNA methyltransferase activity by biologically derived GATC-flanking sequences
    • Coffin S.R., and Reich N.O. Modulation of Escherichia coli DNA methyltransferase activity by biologically derived GATC-flanking sequences. J. Biol. Chem. 283 (2008) 20106-20116
    • (2008) J. Biol. Chem. , vol.283 , pp. 20106-20116
    • Coffin, S.R.1    Reich, N.O.2
  • 29
    • 0037388105 scopus 로고    scopus 로고
    • Functional cooperation between exonucleases and endonucleases-basis for the evolution of restriction enzymes
    • Raghavendra N.K., and Rao D.N. Functional cooperation between exonucleases and endonucleases-basis for the evolution of restriction enzymes. Nucleic Acids Res. 31 (2003) 1888-1896
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1888-1896
    • Raghavendra, N.K.1    Rao, D.N.2
  • 30
    • 4644272663 scopus 로고    scopus 로고
    • Overexpression and affinity chromatography purification of the type III restriction endonuclease EcoP15I for use in transcriptome analysis
    • Moncke-Buchner E., Mackeldanz P., Kruger D.H., and Reuter M. Overexpression and affinity chromatography purification of the type III restriction endonuclease EcoP15I for use in transcriptome analysis. J. Biotechnol. 114 (2004) 99-106
    • (2004) J. Biotechnol. , vol.114 , pp. 99-106
    • Moncke-Buchner, E.1    Mackeldanz, P.2    Kruger, D.H.3    Reuter, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.