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Volumn 106, Issue 6, 2009, Pages 1748-1753

Type III restriction enzymes communicate in 1D without looping between their target sites

Author keywords

1D diffusion; ATPase; Helicase; Motor protein; Single molecule

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; TYPE III SITE SPECIFIC DEOXYRIBONUCLEASE;

EID: 60549086229     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0807193106     Document Type: Article
Times cited : (58)

References (31)
  • 3
    • 0023732866 scopus 로고
    • Model for how type I restriction enzymes select cleavage sites in DNA
    • Studier FW, Bandyopadhyay PK (1988) Model for how type I restriction enzymes select cleavage sites in DNA. Proc Natl Acad Sci USA 85:4677-4681.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4677-4681
    • Studier, F.W.1    Bandyopadhyay, P.K.2
  • 4
    • 0029045067 scopus 로고
    • Type III restriction endonucleases translocate DNA in a reaction driven by recognition site-specific ATP hydrolysis
    • Meisel A, Mackeldanz P, Bickle TA, Krüger DH, 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    Krüger, D.H.4    Schroeder, C.5
  • 5
    • 3042785825 scopus 로고    scopus 로고
    • One recognition sequence, seven restriction enzymes, five reaction mechanisms
    • Gowers DM, Bellamy SRW, Halford SE (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.W.2    Halford, S.E.3
  • 7
    • 0032212129 scopus 로고    scopus 로고
    • EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities
    • Davies GP, Powell LM, Webb JL, Cooper LP, Murray NE (1998) EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities. Nucleic Acids Res 26:4828-4836.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4828-4836
    • Davies, G.P.1    Powell, L.M.2    Webb, J.L.3    Cooper, L.P.4    Murray, N.E.5
  • 8
    • 17444429639 scopus 로고    scopus 로고
    • Continuous assays for DNA translocation using fluorescent triplex dissociation: Application to type I restriction endonucleases
    • McClelland SE, Dryden DTF, Szczelkun MD (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.F.2    Szczelkun, M.D.3
  • 9
    • 0034595208 scopus 로고    scopus 로고
    • Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement
    • Firman K, Szczelkun MD (2000) Measuring motion on DNA by the type I restriction endonuclease EcoR124I using triplex displacement. EMBO J 19:2094-2102.
    • (2000) EMBO J , vol.19 , pp. 2094-2102
    • Firman, K.1    Szczelkun, M.D.2
  • 10
    • 4344649856 scopus 로고    scopus 로고
    • Real-time observation of DNA translocation by the type I restriction modification enzyme EcoR124I
    • Seidel R, et al. (2004) Real-time observation of DNA translocation by the type I restriction modification enzyme EcoR124I. Nat Struct Mol Biol 11:838-843.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 838-843
    • Seidel, R.1
  • 11
    • 33646807817 scopus 로고    scopus 로고
    • When a helicase is not a helicase: DsDNA tracking by the motor protein EcoR124l
    • Stanley LK, et al. (2006) When a helicase is not a helicase: dsDNA tracking by the motor protein EcoR124l. EMBO J 25:2230-2239.
    • (2006) EMBO J , vol.25 , pp. 2230-2239
    • Stanley, L.K.1
  • 12
    • 43249131522 scopus 로고    scopus 로고
    • Motor step size and ATP coupling efficiency of the dsDNA translocase EcoR124I
    • Seidel R, Bloom JGP, Dekker C, Szczelkun MD (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.P.2    Dekker, C.3    Szczelkun, M.D.4
  • 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 NK, Rao DN (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
  • 14
    • 34548105170 scopus 로고    scopus 로고
    • DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes
    • Crampton N, et al. (2007) DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes. EMBO J 26:3815-3825.
    • (2007) EMBO J , vol.26 , pp. 3815-3825
    • Crampton, N.1
  • 15
    • 0026584744 scopus 로고
    • Type III restriction enzymes need two inversely oriented recognition sites for DNA cleavage
    • Meisel A, Bickle TA, Krüger DH, 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
  • 16
    • 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 JP, Krüger DH (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
  • 17
    • 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, et al. (2007) 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 104:12755-12760.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12755-12760
    • Crampton, N.1
  • 18
    • 24144454859 scopus 로고    scopus 로고
    • Characterization of the Type III restriction endonuclease PstII from Providencia stuartii
    • Sears A, Peakman LJ, Wilson GG, Szczelkun MD (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
  • 19
    • 23644449865 scopus 로고    scopus 로고
    • Single-molecule DNA nanomanipulation: Improved resolution through use of shorter DNA fragments
    • Revyakin A, Ebright RH, Strick TR (2005) Single-molecule DNA nanomanipulation: Improved resolution through use of shorter DNA fragments. Nat Methods 2:127-138.
    • (2005) Nat Methods , vol.2 , pp. 127-138
    • Revyakin, A.1    Ebright, R.H.2    Strick, T.R.3
  • 20
    • 33846898070 scopus 로고    scopus 로고
    • Single-molecule studies of nucleic acid motors
    • Seidel R, Dekker C (2007) Single-molecule studies of nucleic acid motors. Curr Opin Struct Biol 17:80-86.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 80-86
    • Seidel, R.1    Dekker, C.2
  • 21
    • 0141645630 scopus 로고    scopus 로고
    • S-adenosyl methionine prevents promiscuous DNA cleavage by the EcoP1I type III restriction enzyme
    • Peakman LJ, Antognozzi M, Bickle TA, Janscak P, Szczelkun MD (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
  • 22
    • 37649031368 scopus 로고    scopus 로고
    • Formation of loops in DNA under tension
    • Sankararaman S, Marko JF (2005) Formation of loops in DNA under tension. Phys Rev E 71:021911.
    • (2005) Phys Rev E , vol.71 , pp. 021911
    • Sankararaman, S.1    Marko, J.F.2
  • 23
    • 4043073592 scopus 로고    scopus 로고
    • DNA communications by Type III restriction endonucleases-confirmation of 1D translocation over 3D looping
    • Peakman LJ, Szczelkun MD (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
  • 24
    • 31544452261 scopus 로고    scopus 로고
    • Real-time observation of DNA looping dynamics of Type IIE restriction enzymes NaeI and NarI
    • van den Broek B, Vanzi F, Normanno D, Pavone FS, Wuite GJL (2006) Real-time observation of DNA looping dynamics of Type IIE restriction enzymes NaeI and NarI. Nucleic Acids Res 34:167-174.
    • (2006) Nucleic Acids Res , vol.34 , pp. 167-174
    • van den Broek, B.1    Vanzi, F.2    Normanno, D.3    Pavone, F.S.4    Wuite, G.J.L.5
  • 25
    • 33644676435 scopus 로고    scopus 로고
    • Volume-exclusion effects in tethered-particle experiments: Bead size matters
    • Segall DE, Nelson PC, Phillips R (2006) Volume-exclusion effects in tethered-particle experiments: Bead size matters. Phys Rev Lett 96:088306.
    • (2006) Phys Rev Lett , vol.96 , pp. 088306
    • Segall, D.E.1    Nelson, P.C.2    Phillips, R.3
  • 26
    • 33947362038 scopus 로고    scopus 로고
    • Development of fluorescent biosensors for probing the function of motor proteins
    • Webb MR (2007) Development of fluorescent biosensors for probing the function of motor proteins. Mol Biosyst 3:249-256.
    • (2007) Mol Biosyst , vol.3 , pp. 249-256
    • Webb, M.R.1
  • 27
    • 33746824311 scopus 로고    scopus 로고
    • Tension-dependent DNA cleavage by restriction endonucleases: Two-site enzymes are "switched off" at low force
    • Gemmen GJ, Millin R, Smith DE (2006) Tension-dependent DNA cleavage by restriction endonucleases: Two-site enzymes are "switched off" at low force. Proc Natl Acad Sci USA 103:11555-11560.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11555-11560
    • Gemmen, G.J.1    Millin, R.2    Smith, D.E.3
  • 28
    • 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 MD, Bickle TA (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
  • 29
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • Rivetti C, Guthold M, Bustamante C (1996) Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis. J Mol Biol 264:919-932.
    • (1996) J Mol Biol , vol.264 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 30
    • 0344875225 scopus 로고    scopus 로고
    • DNA supercoiling enables the type IIS restriction enzyme BspMI to recognise the relative orientation of two DNA sequences
    • Kingston IJ, Gormley NA, Halford SE (2003) DNA supercoiling enables the type IIS restriction enzyme BspMI to recognise the relative orientation of two DNA sequences. Nucleic Acids Res 31:5221-5228.
    • (2003) Nucleic Acids Res , vol.31 , pp. 5221-5228
    • Kingston, I.J.1    Gormley, N.A.2    Halford, S.E.3
  • 31
    • 35649018595 scopus 로고    scopus 로고
    • Dynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6
    • Gorman J, et al. (2007) Dynamic basis for one-dimensional DNA scanning by the mismatch repair complex Msh2-Msh6. Mol Cell 28:359-370.
    • (2007) Mol Cell , vol.28 , pp. 359-370
    • Gorman, J.1


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