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Volumn 36, Issue 12, 2008, Pages 3939-3949

A RecB-family nuclease motif in the Type I restriction endonuclease EcoR124I

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; NUCLEASE; PROTEIN RECB; RESTRICTION ENDONUCLEASE; RESTRICTION ENDONUCLEASE TYPE 1;

EID: 47249088354     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn333     Document Type: Article
Times cited : (20)

References (38)
  • 1
    • 0029968248 scopus 로고    scopus 로고
    • The type I restriction endonuclease R.EcoR1241: Over-production and biochemical properties
    • Janscak,P., Abadjieva,A. and Firman,K. (1996) The type I restriction endonuclease R.EcoR1241: Over-production and biochemical properties. J. Mol. Biol., 257, 977-991.
    • (1996) J. Mol. Biol , vol.257 , pp. 977-991
    • Janscak, P.1    Abadjieva, A.2    Firman, K.3
  • 2
    • 0031559573 scopus 로고    scopus 로고
    • Selection of non-specific DNA cleavage sites by the type IC restriction endonuclease EcoR1241
    • Szczelkun,M.D., Janscak,P., Firman,K. and Halford,S.E. (1997) Selection of non-specific DNA cleavage sites by the type IC restriction endonuclease EcoR1241. J. Mol. Biol., 271, 112-123.
    • (1997) J. Mol. Biol , vol.271 , pp. 112-123
    • Szczelkun, M.D.1    Janscak, P.2    Firman, K.3    Halford, S.E.4
  • 4
    • 17444429639 scopus 로고    scopus 로고
    • Continuous assays for DNA translocation using fluorescent triplex dissociation: Application to type I restriction endonucleases
    • McClelland,S.E., Dryden,D.T. and Szczelkun,M.D. (2005) Continuous assays for DNA translocation using fluorescent triplex dissociation: application to type I restriction endonucleases. J. Mol. Biol., 348, 895-915.
    • (2005) J. Mol. Biol , vol.348 , pp. 895-915
    • McClelland, S.E.1    Dryden, D.T.2    Szczelkun, M.D.3
  • 6
    • 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., Ternent,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. Mol. Microbiol., 22, 437-447.
    • (1996) Mol. Microbiol , vol.22 , pp. 437-447
    • Titheradge, A.J.B.1    Ternent, D.2    Murray, N.E.3
  • 7
    • 0033168103 scopus 로고    scopus 로고
    • Single amino acid substitutions in the HsdR subunit of the type IB restriction enzyme EcoAI uncouple the DNA translocation and DNA cleavage activities of the enzyme
    • Janscak,P., Sandmeier,U. and Bickle,T.A. (1999) Single amino acid substitutions in the HsdR subunit of the type IB restriction enzyme EcoAI uncouple the DNA translocation and DNA cleavage activities of the enzyme. Nucleic Acids Res., 27, 2638-2643.
    • (1999) Nucleic Acids Res , vol.27 , pp. 2638-2643
    • Janscak, P.1    Sandmeier, U.2    Bickle, T.A.3
  • 9
    • 0033214565 scopus 로고    scopus 로고
    • The DNA translocation and ATPase activities of restriction-deficient mutants of Eco KI
    • Davies,G.P., Kemp,P., Molineux,I.J. and Murray,N.E. (1999) The DNA translocation and ATPase activities of restriction-deficient mutants of Eco KI. J. Mol. Biol., 292, 787-796.
    • (1999) J. Mol. Biol , vol.292 , pp. 787-796
    • Davies, G.P.1    Kemp, P.2    Molineux, I.J.3    Murray, N.E.4
  • 10
    • 0034664813 scopus 로고    scopus 로고
    • SURVEY AND SUMMARY: Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • Aravind,L., Makarova,K.S. and Koonin,E.V. (2000) SURVEY AND SUMMARY: Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res., 28, 3417-3432.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 11
    • 11344287431 scopus 로고    scopus 로고
    • Molecular phylogenetics of restriction endonucleases
    • Pingound,A, Ed, Springer, Germany, pp
    • Bujnicki,J.M. (2004) Molecular phylogenetics of restriction endonucleases. In Pingound,A. (Ed.), Restriction Endonucleases, Nucleic Acids and Molecular Biology, Vol. 14, Springer, Germany, pp. 63-93.
    • (2004) Restriction Endonucleases, Nucleic Acids and Molecular Biology , vol.14 , pp. 63-93
    • Bujnicki, J.M.1
  • 12
    • 0032486108 scopus 로고    scopus 로고
    • Structure-based redesign of the catalytic/metal binding site of Cfr101 restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues
    • Skirgaila,R., Grazulis,S., Bozic,D., Huber,R. and Siksnys,V. (1998) Structure-based redesign of the catalytic/metal binding site of Cfr101 restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues. J. Mol. Biol., 279, 473-481.
    • (1998) J. Mol. Biol , vol.279 , pp. 473-481
    • Skirgaila, R.1    Grazulis, S.2    Bozic, D.3    Huber, R.4    Siksnys, V.5
  • 13
    • 17044403057 scopus 로고    scopus 로고
    • Type II restriction endonucleases: Structure and mechanism
    • Pingoud,A., Fuxreiter,M., Pingoud,V. and Wende,W. (2005) Type II restriction endonucleases: Structure and mechanism. Cell Mol. Life Sci., 62, 685-707.
    • (2005) Cell Mol. Life Sci , vol.62 , pp. 685-707
    • Pingoud, A.1    Fuxreiter, M.2    Pingoud, V.3    Wende, W.4
  • 14
    • 38349125372 scopus 로고    scopus 로고
    • HsdR subunit of the type I restriction-modification enzyme EcoR124I: Biophysical characterisation and structural modelling
    • Obarska-Kosinska,A., Taylor,J.E.: Callow,P., Orlowski,J., Bujnicki,J.M. and Kneale,G.G. (2008) HsdR subunit of the type I restriction-modification enzyme EcoR124I: Biophysical characterisation and structural modelling. J. Mol. Biol., 376, 438-452.
    • (2008) J. Mol. Biol , vol.376 , pp. 438-452
    • Obarska-Kosinska, A.1    Taylor, J.E.2    Callow, P.3    Orlowski, J.4    Bujnicki, J.M.5    Kneale, G.G.6
  • 16
    • 0032491378 scopus 로고    scopus 로고
    • Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme
    • Yu,M., Souaya,J. and Julin,D.A. (1998) Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme,. J. Mol. Biol., 283, 797-808.
    • (1998) J. Mol. Biol , vol.283 , pp. 797-808
    • Yu, M.1    Souaya, J.2    Julin, D.A.3
  • 17
    • 0034614654 scopus 로고    scopus 로고
    • A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions
    • Wang,J., Chen,R. and Julin,D.A. (2000) A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions. J. Biol. Chem., 275, 507-513.
    • (2000) J. Biol. Chem , vol.275 , pp. 507-513
    • Wang, J.1    Chen, R.2    Julin, D.A.3
  • 18
    • 0034971260 scopus 로고    scopus 로고
    • In vivo evidence for two active nuclease motifs in the double-strand break repair enzyme RexAB of Lactococcus lactis
    • Quiberoni,A., Biswas,I., El Karoui,M., Rezaïki,L., Tailliez,P. and Gruss,A. (2001) In vivo evidence for two active nuclease motifs in the double-strand break repair enzyme RexAB of Lactococcus lactis. J. Bacteriol., 183, 4071-4078.
    • (2001) J. Bacteriol , vol.183 , pp. 4071-4078
    • Quiberoni, A.1    Biswas, I.2    El Karoui, M.3    Rezaïki, L.4    Tailliez, P.5    Gruss, A.6
  • 19
    • 0035824602 scopus 로고    scopus 로고
    • Structure and function of the Escherichia coli RecE protein, a member of the RecB nuclease domain family
    • Chang,H.W. and Julin,D.A. (2001) Structure and function of the Escherichia coli RecE protein, a member of the RecB nuclease domain family. J. Biol. Chem., 276, 46004-46010.
    • (2001) J. Biol. Chem , vol.276 , pp. 46004-46010
    • Chang, H.W.1    Julin, D.A.2
  • 20
    • 34447095032 scopus 로고    scopus 로고
    • A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases
    • Yeeles,J.T. and Dillingham,M.S. (2007) A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases. J. Mol. Biol., 371, 66-78.
    • (2007) J. Mol. Biol , vol.371 , pp. 66-78
    • Yeeles, J.T.1    Dillingham, M.S.2
  • 21
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressivemultiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson,J.D., Higgins,D.G. and Gibson,T.J. (1994) CLUSTAL W: Improving the sensitivity of progressivemultiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res., 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 22
    • 33846078626 scopus 로고    scopus 로고
    • REBASE-enzymes and genes for DNA restriction and modification
    • Roberts,R.J., Vincze,T., Posfai,J. and Macelis,D. (2007) REBASE-enzymes and genes for DNA restriction and modification. Nucleic Acids Res. 35, D269-D270.
    • (2007) Nucleic Acids Res , vol.35
    • Roberts, R.J.1    Vincze, T.2    Posfai, J.3    Macelis, D.4
  • 25
    • 0032190284 scopus 로고    scopus 로고
    • Analysis of the subunit assembly of the type IC restriction-modification enzyme EcoR124I
    • Janscak,P., Dryden,D.T.F. and Firman,K. (1998) Analysis of the subunit assembly of the type IC restriction-modification enzyme EcoR124I. Nucleic Acids Res., 26, 4439-4445.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4439-4445
    • Janscak, P.1    Dryden, D.T.F.2    Firman, K.3
  • 26
    • 0035957061 scopus 로고    scopus 로고
    • Binding and recognition of GATATC target sequences by the EcoRV restriction endonuclease: A study using fluorescent oligonucleotides and fluorescence polarization
    • Reid,S.L., Parry,D., Liu,H.H. and Connolly,B.A. (2001) Binding and recognition of GATATC target sequences by the EcoRV restriction endonuclease: A study using fluorescent oligonucleotides and fluorescence polarization. Biochemistry, 40, 2484-2494.
    • (2001) Biochemistry , vol.40 , pp. 2484-2494
    • Reid, S.L.1    Parry, D.2    Liu, H.H.3    Connolly, B.A.4
  • 27
    • 28644433100 scopus 로고    scopus 로고
    • Dynamics of initiation, termination and reinitiation of DNA translocation by the motor protein EcoR124I
    • Seidel,R., Bloom,J.G., van Noort,J., Dutta,C.F., Dekker,N.H., Firman,K., Szczelkun,M.D. and Dekker,C. (2005) Dynamics of initiation, termination and reinitiation of DNA translocation by the motor protein EcoR124I. EMBO J., 24, 4188-4197.
    • (2005) EMBO J , vol.24 , pp. 4188-4197
    • Seidel, R.1    Bloom, J.G.2    van Noort, J.3    Dutta, C.F.4    Dekker, N.H.5    Firman, K.6    Szczelkun, M.D.7    Dekker, C.8
  • 28
    • 33749983459 scopus 로고    scopus 로고
    • Direct and random routing of a molecular motor protein at a DNA junction
    • Stanley,L.K. and Szczelkun,M.D. (2006) Direct and random routing of a molecular motor protein at a DNA junction. Nucleic Acids Res., 34, 4387-4394.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4387-4394
    • Stanley, L.K.1    Szczelkun, M.D.2
  • 29
    • 0029910629 scopus 로고    scopus 로고
    • Repercussions of DNA tracking by the type IC restriction endonuclease EcoR124I 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 EcoR124I on linear, circular and catenated substrates. EMBO J., 15, 6335-6347.
    • (1996) EMBO J , vol.15 , pp. 6335-6347
    • Szczelkun, M.D.1    Dillingham, M.S.2    Janscak, P.3    Firman, K.4    Halford, S.E.5
  • 30
    • 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
  • 31
    • 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., Cooper,L.P., 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.1    Cooper, L.P.2    Thorpe, P.H.3    Byron, O.4
  • 32
    • 0037065729 scopus 로고    scopus 로고
    • Kinetic models of translocation, head-on collision, and DNA cleavage by type I restriction endonucleases
    • Szczelkun,M.D. (2002) Kinetic models of translocation, head-on collision, and DNA cleavage by type I restriction endonucleases. Biochemistry, 41, 2067-2074.
    • (2002) Biochemistry , vol.41 , pp. 2067-2074
    • Szczelkun, M.D.1
  • 33
    • 0033579567 scopus 로고    scopus 로고
    • Reactions of type II restriction endonucleases with 8-base pair recognition sites
    • Bilcock,D.T., Daniels,L.E., Bath,A.J. and Halford,S.E. (1999) Reactions of type II restriction endonucleases with 8-base pair recognition sites. J. Biol. Chem., 274, 36379-36386.
    • (1999) J. Biol. Chem , vol.274 , pp. 36379-36386
    • Bilcock, D.T.1    Daniels, L.E.2    Bath, A.J.3    Halford, S.E.4
  • 34
    • 0030035503 scopus 로고    scopus 로고
    • Chiral phosphorothioates as probes of protein interactions with individual DNA phosphoryl oxygens: Essential interactions of EcoRI endonuclease with the phosphate at pGAATTC
    • Kurpiewski,M.R., Koziolkiewicz,M., Wilk,A., Stec,W.J. and Jen-Jacobson,L. (1996) Chiral phosphorothioates as probes of protein interactions with individual DNA phosphoryl oxygens: Essential interactions of EcoRI endonuclease with the phosphate at pGAATTC. Biochemistry, 35, 8846-8854.
    • (1996) Biochemistry , vol.35 , pp. 8846-8854
    • Kurpiewski, M.R.1    Koziolkiewicz, M.2    Wilk, A.3    Stec, W.J.4    Jen-Jacobson, L.5
  • 35
    • 16244399036 scopus 로고    scopus 로고
    • The integration of recognition and cleavage: X-ray structures of pre-transition state complex, post-reactive complex and the DNA-free endonuclease
    • Pingound,A, Ed, Springer, Germany, pp
    • Grigorescu,A., Horvath,M., Wilkosz,K., Chandrasekhar,K. and Rosenberg,J.M. (2004) The integration of recognition and cleavage: X-ray structures of pre-transition state complex, post-reactive complex and the DNA-free endonuclease. In Pingound,A. (Ed.), Restriction Endonucleases, Nucleic Acids and Molecular Biology, Vol. 14, Springer, Germany, pp. 137-177.
    • (2004) Restriction Endonucleases, Nucleic Acids and Molecular Biology , vol.14 , pp. 137-177
    • Grigorescu, A.1    Horvath, M.2    Wilkosz, K.3    Chandrasekhar, K.4    Rosenberg, J.M.5
  • 36
    • 0032564447 scopus 로고    scopus 로고
    • Stretched and overwound DNA forms a Pauling-like structure with exposed bases
    • Allemand,J.F., Bensimon,D., Lavery,R. and Croquette,V. (1998) Stretched and overwound DNA forms a Pauling-like structure with exposed bases. Proc. Natl Acad. Sci. USA, 95, 14152-14157.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14152-14157
    • Allemand, J.F.1    Bensimon, D.2    Lavery, R.3    Croquette, V.4
  • 38
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton,M.R., Dillingham,M.S. and Wigley,D.B. (2007) Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem., 76, 23-50.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3


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