메뉴 건너뛰기




Volumn 38, Issue 2, 2010, Pages 404-409

Maintaining a sense of direction during long-range communication on DNA

Author keywords

ATPase; DNA sliding; Helicase; Mismatch repair; Molecular switch; Restriction modification

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; DNA; HELICASE; RESTRICTION ENDONUCLEASE; TYPE III SITE SPECIFIC DEOXYRIBONUCLEASE;

EID: 77952727817     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0380404     Document Type: Review
Times cited : (24)

References (50)
  • 1
    • 0027971210 scopus 로고
    • Restriction enzymes in cells, not eppendorfs
    • King, G. and Murray, N.E. (1994) Restriction enzymes in cells, not eppendorfs. Trends Microbiol. 2, 465-469
    • (1994) Trends Microbiol. , vol.2 , pp. 465-469
    • King, G.1    Murray, N.E.2
  • 2
    • 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
  • 3
    • 0035883536 scopus 로고    scopus 로고
    • Nucleoside triphosphate-dependent restriction enzymes
    • Dryden, D.T., Murray, N.E. and Rao, D.N. (2001) Nucleoside triphosphate-dependent restriction enzymes. Nucleic Acids Res. 29, 3728-3741
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3728-3741
    • Dryden, D.T.1    Murray, N.E.2    Rao, D.N.3
  • 4
    • 0037040271 scopus 로고    scopus 로고
    • Many type IIs restriction endonucleases interact with two recognition sites before cleaving DNA
    • Bath, A.J., Milsom, S.E., Gormley, N.A. and Halford, S.E. (2002) Many type IIs restriction endonucleases interact with two recognition sites before cleaving DNA. J. Biol. Chem. 277, 4024-4033
    • (2002) J. Biol. Chem. , vol.277 , pp. 4024-4033
    • Bath, A.J.1    Milsom, S.E.2    Gormley, N.A.3    Halford, S.E.4
  • 5
    • 3042785825 scopus 로고    scopus 로고
    • One recognition sequence, seven restriction enzymes, five reaction mechanisms
    • Gowers, D.M., Bellamy, S.R. and Halford, S.E. (2004) One recognition sequence, seven restriction enzymes, five reaction mechanisms. Nucleic Acids Res. 32, 3469-3479
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3469-3479
    • Gowers, D.M.1    Bellamy, S.R.2    Halford, S.E.3
  • 6
    • 69849115232 scopus 로고    scopus 로고
    • The MmeI family: Type II restriction-modification enzymes that employ single-strand modification for host protection
    • Morgan, R.D., Dwinell, E.A., Bhatia, T.K., Lang, E.M. and Luyten, Y.A. (2009) The MmeI family: type II restriction-modification enzymes that employ single-strand modification for host protection. Nucleic Acids Res. 37, 5208-5221
    • (2009) Nucleic Acids Res. , vol.37 , pp. 5208-5221
    • Morgan, R.D.1    Dwinell, E.A.2    Bhatia, T.K.3    Lang, E.M.4    Luyten, Y.A.5
  • 8
    • 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. (2001) Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I. J. Mol. Biol. 306, 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
  • 9
    • 24144441025 scopus 로고    scopus 로고
    • Subunit assembly modulates the activities of the Type III restriction-modification enzyme PstII in vitro
    • Sears, A. and Szczelkun, M.D. (2005) Subunit assembly modulates the activities of the Type III restriction-modification enzyme PstII in vitro. Nucleic Acids Res. 33, 4788-4796
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4788-4796
    • Sears, A.1    Szczelkun, M.D.2
  • 10
    • 4043073592 scopus 로고    scopus 로고
    • DNA communications by Type III restriction endonucleases: Confirmation of 1D translocation over 3D looping
    • Peakman, L.J. and Szczelkun, M.D. (2004) DNA communications by Type III restriction endonucleases: confirmation of 1D translocation over 3D looping. Nucleic Acids Res. 32, 4166-4174
    • (2004) Nucleic Acids Res. , vol.32 , pp. 4166-4174
    • Peakman, L.J.1    Szczelkun, M.D.2
  • 11
    • 0026584744 scopus 로고
    • Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage
    • Meisel, A., Bickle, T.A., Krüger, D.H. and Schroeder, C. (1992) Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage. Nature 355, 467-469
    • (1992) Nature , vol.355 , pp. 467-469
    • Meisel, A.1    Bickle, T.A.2    Krüger, D.H.3    Schroeder, C.4
  • 12
    • 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. (1995) Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis. EMBO J. 14, 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
  • 13
    • 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. (2003) S-Adenosyl methionine prevents promiscuous DNA cleavage by the EcoP1I type III restriction enzyme. J. Mol. Biol. 333, 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
  • 15
    • 0001037223 scopus 로고
    • Topological selectivity in site-specific recombination
    • (Sherratt, D.J., ed.), Oxford University Press, Oxford
    • Stark, W.M. and and Boocock, M.R. (1995) Topological selectivity in site-specific recombination. in Mobile Genetic Elements (Sherratt, D.J., ed.), pp. 101-129, Oxford University Press, Oxford
    • (1995) Mobile Genetic Elements , pp. 101-129
    • Stark, W.M.1    Boocock, M.R.2
  • 16
    • 0025995309 scopus 로고
    • Endonuclease (R) subunits of type-I and type-III restriction-modification enzymes contain a helicase-like domain
    • Gorbalenya, A.E. and Koonin, E.V. (1991) Endonuclease (R) subunits of type-I and type-III restriction-modification enzymes contain a helicase-like domain. FEBS Lett. 291, 277-281
    • (1991) FEBS Lett. , vol.291 , pp. 277-281
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 18
    • 73349100057 scopus 로고    scopus 로고
    • The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: Implications for DNA restriction and translocation activity
    • Uyen, N.T., Park, S.Y., Choi, J.W., Lee, H.J., Nishi, K. and Kim, J.S. (2009) The fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activity. Nucleic Acids Res. 37, 6960-6969
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6960-6969
    • Uyen, N.T.1    Park, S.Y.2    Choi, J.W.3    Lee, H.J.4    Nishi, K.5    Kim, J.S.6
  • 20
    • 0034130457 scopus 로고    scopus 로고
    • Type I restriction systems: Sophisticated molecular machines (a legacy of Bertani and Weigle)
    • Murray, N.E. (2000) Type I restriction systems: sophisticated molecular machines (a legacy of Bertani and Weigle). Microbiol. Mol. Biol. Rev. 64, 412-434
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 412-434
    • Murray, N.E.1
  • 21
    • 0031566426 scopus 로고    scopus 로고
    • Mutations in the Res subunit of the EcoPI restriction enzyme that affect ATP-dependent reactions
    • Saha, S. and Rao, D.N. (1997) Mutations in the Res subunit of the EcoPI restriction enzyme that affect ATP-dependent reactions. J. Mol. Biol. 269, 342-354
    • (1997) J. Mol. Biol. , vol.269 , pp. 342-354
    • Saha, S.1    Rao, D.N.2
  • 24
    • 43249131522 scopus 로고    scopus 로고
    • Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I
    • Seidel, R., Bloom, J.G., Dekker, C. and Szczelkun, M.D. (2008) Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I. EMBO J. 27, 1388-1398
    • (2008) EMBO J. , vol.27 , pp. 1388-1398
    • Seidel, R.1    Bloom, J.G.2    Dekker, C.3    Szczelkun, M.D.4
  • 26
    • 0028936127 scopus 로고
    • ATP hydrolysis is required for DNA cleavage by EcoPI restriction enzyme
    • Saha, S. and Rao, D.N. (1995) ATP hydrolysis is required for DNA cleavage by EcoPI restriction enzyme. J. Mol. Biol. 247, 559-567
    • (1995) J. Mol. Biol. , vol.247 , pp. 559-567
    • Saha, S.1    Rao, D.N.2
  • 27
    • 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. (2005) Characterization of the Type III restriction endonuclease PstII from Providencia stuartii. Nucleic Acids Res. 33, 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
  • 28
    • 3342967880 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA translocation by the Type III restriction enzyme EcoP15I
    • Reich, S., Gössl, I., Reuter, M., Rabe, J.P. and Krüger, D.H. (2004) Scanning force microscopy of DNA translocation by the Type III restriction enzyme EcoP15I. J. Mol. Biol. 341, 337-343
    • (2004) J. Mol. Biol. , vol.341 , pp. 337-343
    • Reich, S.1    Gössl, I.2    Reuter, M.3    Rabe, J.P.4    Krüger, D.H.5
  • 29
    • 34548105170 scopus 로고    scopus 로고
    • DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes
    • DOI 10.1038/sj.emboj.7601807, PII 7601807
    • Crampton, N., Roes, S., Dryden, D.T., Rao, D.N., Edwardson, J.M. and Henderson, R.M. (2007) DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes. EMBO J. 26, 3815-3825 (Pubitemid 47295874)
    • (2007) EMBO Journal , vol.26 , Issue.16 , pp. 3815-3825
    • Crampton, N.1    Roes, S.2    Dryden, D.T.F.3    Rao, D.N.4    Edwardson, J.M.5    Henderson, R.M.6
  • 31
    • 67651162118 scopus 로고    scopus 로고
    • S-adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI
    • Peakman, L.J. and Szczelkun, M.D. (2009) S-adenosyl homocysteine and DNA ends stimulate promiscuous nuclease activities in the Type III restriction endonuclease EcoPI. Nucleic Acids Res. 37, 3934-3945
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3934-3945
    • Peakman, L.J.1    Szczelkun, M.D.2
  • 32
    • 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. (2004) Unidirectional translocation from recognition site and a necessary interaction with DNA end for cleavage by Type III restriction enzyme. Nucleic Acids Res. 32, 5703-5711
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5703-5711
    • Raghavendra, N.K.1    Rao, D.N.2
  • 33
  • 34
    • 65549171477 scopus 로고    scopus 로고
    • An end to 40 years of mistakes in DNA-protein association kinetics?
    • Halford, S.E. (2009) An end to 40 years of mistakes in DNA-protein association kinetics? Biochem. Soc. Trans. 37, 343-348
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 343-348
    • Halford, S.E.1
  • 35
    • 10044223573 scopus 로고    scopus 로고
    • Kinetics of protein-DNA interaction: Facilitated target location in sequence-dependent potential
    • Slutsky, M. and Mirny, L.A. (2004) Kinetics of protein-DNA interaction: facilitated target location in sequence-dependent potential. Biophys. J. 87, 4021-4035
    • (2004) Biophys. J. , vol.87 , pp. 4021-4035
    • Slutsky, M.1    Mirny, L.A.2
  • 36
    • 33645807371 scopus 로고    scopus 로고
    • A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA
    • Blainey, P.C., van Oijen, A.M., Banerjee, A., Verdine, G.L. and Xie, X.S. (2006) A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA. Proc. Natl. Acad. Sci. U.S.A. 103, 5752-5757
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5752-5757
    • Blainey, P.C.1    Van Oijen, A.M.2    Banerjee, A.3    Verdine, G.L.4    Xie, X.S.5
  • 39
    • 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
    • Mücke, M., Reich, S., Möncke-Buchner, E., Reuter, M. and Krüger, D.H. (2001) 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, 687-698
    • (2001) J. Mol. Biol. , vol.312 , pp. 687-698
    • Mücke, M.1    Reich, S.2    Möncke-Buchner, E.3    Reuter, M.4    Krüger, D.H.5
  • 42
    • 0031456973 scopus 로고    scopus 로고
    • The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch
    • Gradia, S., Acharya, S. and Fishel, R. (1997) The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch. Cell 91, 995-1005
    • (1997) Cell , vol.91 , pp. 995-1005
    • Gradia, S.1    Acharya, S.2    Fishel, R.3
  • 43
    • 0029913452 scopus 로고    scopus 로고
    • Mutation detection with MutH, MutL, and MutS mismatch repair proteins
    • Smith, J. and Modrich, P. (1996) Mutation detection with MutH, MutL, and MutS mismatch repair proteins. Proc. Natl. Acad. Sci. U.S.A. 93, 4374-4379
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4374-4379
    • Smith, J.1    Modrich, P.2
  • 44
    • 34547882768 scopus 로고    scopus 로고
    • Protein roadblocks and helix discontinuities are barriers to the initiation of mismatch repair
    • Pluciennik, A. and Modrich, P. (2007) Protein roadblocks and helix discontinuities are barriers to the initiation of mismatch repair. Proc. Natl. Acad. Sci. U.S.A. 104, 12709-12713
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 12709-12713
    • Pluciennik, A.1    Modrich, P.2
  • 47
    • 2942627123 scopus 로고    scopus 로고
    • Signaling from DNA mispairs to mismatch-repair excision sites despite intervening blockades
    • Wang, H. and Hays, J.B. (2004) Signaling from DNA mispairs to mismatch-repair excision sites despite intervening blockades. EMBO J. 23, 2126-2133
    • (2004) EMBO J. , vol.23 , pp. 2126-2133
    • Wang, H.1    Hays, J.B.2
  • 48
    • 63549113890 scopus 로고    scopus 로고
    • Loading clamps for DNA replication and repair
    • Bloom, L.B. (2009) Loading clamps for DNA replication and repair. DNA Repair 8, 570-578
    • (2009) DNA Repair , vol.8 , pp. 570-578
    • Bloom, L.B.1
  • 49
    • 0033634983 scopus 로고    scopus 로고
    • Structure of BamHI bound to nonspecific DNA: A model for DNA sliding
    • Viadiu, H. and Aggarwal, A.K. (2000) Structure of BamHI bound to nonspecific DNA: a model for DNA sliding. Mol. Cell 5, 889-895
    • (2000) Mol. Cell , vol.5 , pp. 889-895
    • Viadiu, H.1    Aggarwal, A.K.2
  • 50
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle, A.M. (2008) Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys. 37, 317-336
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.