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Volumn 420, Issue 4-5, 2012, Pages 261-268

Structural insights into the assembly and shape of type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering

Author keywords

ATP hydrolysis; DNA modification and cleavage; DNA translocation; molecular motor; Type III restriction enzyme

Indexed keywords

HOLOENZYME; RESTRICTION ENDONUCLEASE; TYPE III SITE SPECIFIC DEOXYRIBONUCLEASE;

EID: 84862189790     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.04.026     Document Type: Article
Times cited : (9)

References (31)
  • 1
    • 0037389511 scopus 로고    scopus 로고
    • A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes
    • Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A., and Bitinaite J. A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes Nucleic Acids Res. 31 2003 1805 1812
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1805-1812
    • Roberts, R.J.1    Belfort, M.2    Bestor, T.3    Bhagwat, A.S.4    Bickle, T.A.5    Bitinaite, J.6
  • 2
    • 0026338873 scopus 로고
    • Restriction and modification systems
    • Wilson G.G., and Murray N.E. Restriction and modification systems Annu. Rev. Genet. 25 1991 585 627
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 585-627
    • Wilson, G.G.1    Murray, N.E.2
  • 4
    • 0017579598 scopus 로고
    • Purification and properties of the P15 specific restriction endonuclease from Escherichia coli
    • Reiser J., and Yuan R. Purification and properties of the P15 specific restriction endonuclease from Escherichia coli J. Biol. Chem. 252 1977 451 456
    • (1977) J. Biol. Chem. , vol.252 , pp. 451-456
    • Reiser, J.1    Yuan, R.2
  • 5
    • 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
  • 6
    • 84860370801 scopus 로고    scopus 로고
    • Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity
    • Wyszomirski K.H., Curth U., Alves J., Mackeldanz P., Moncke-Buchner E., and Schutkowski M. Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity Nucleic Acids Res. 40 2012 3610 3622
    • (2012) Nucleic Acids Res. , vol.40 , pp. 3610-3622
    • Wyszomirski, K.H.1    Curth, U.2    Alves, J.3    MacKeldanz, P.4    Moncke-Buchner, E.5    Schutkowski, M.6
  • 8
    • 58149293709 scopus 로고    scopus 로고
    • SuperSAGE: A modern platform for genome-wide quantitative transcript profiling
    • Matsumura H., Kruger D.H., Kahl G., and Terauchi R. SuperSAGE: a modern platform for genome-wide quantitative transcript profiling Curr. Pharm. Biotechnol. 9 2008 368 374
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 368-374
    • Matsumura, H.1    Kruger, D.H.2    Kahl, G.3    Terauchi, R.4
  • 9
    • 77952722979 scopus 로고    scopus 로고
    • Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat
    • van Aelst K., Toth J., Ramanathan S.P., Schwarz F.W., Seidel R., and Szczelkun M.D. Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-to-head and tail-to-tail inverted repeat Proc. Natl Acad. Sci. USA 107 2010 9123 9128
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 9123-9128
    • Van Aelst, K.1    Toth, J.2    Ramanathan, S.P.3    Schwarz, F.W.4    Seidel, R.5    Szczelkun, M.D.6
  • 10
    • 79953191521 scopus 로고    scopus 로고
    • Translocation, switching and gating: Potential roles for ATP in long-range communication on DNA by type III restriction endonucleases
    • Szczelkun M.D. Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by type III restriction endonucleases Biochem. Soc. Trans. 39 2011 589 594
    • (2011) Biochem. Soc. Trans. , vol.39 , pp. 589-594
    • Szczelkun, M.D.1
  • 11
    • 77952727817 scopus 로고    scopus 로고
    • Maintaining a sense of direction during long-range communication on DNA
    • Szczelkun M.D., Friedhoff P., and Seidel R. Maintaining a sense of direction during long-range communication on DNA Biochem. Soc. Trans. 38 2010 404 409
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 404-409
    • Szczelkun, M.D.1    Friedhoff, P.2    Seidel, R.3
  • 12
    • 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
  • 13
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 14
    • 0025360667 scopus 로고
    • Construction of an efficient overproducer clone of HinfI restriction endonuclease using the polymerase chain reaction
    • Skoglund C.M., Smith H.O., and Chandrasegaran S. Construction of an efficient overproducer clone of HinfI restriction endonuclease using the polymerase chain reaction Gene 88 1990 1 5
    • (1990) Gene , vol.88 , pp. 1-5
    • Skoglund, C.M.1    Smith, H.O.2    Chandrasegaran, S.3
  • 15
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun D.I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing Biophys. J. 76 1999 2879 2886
    • (1999) Biophys. J. , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 16
    • 77955358961 scopus 로고    scopus 로고
    • Using Situs for the integration of multi-resolution structures
    • Wriggers W. Using Situs for the integration of multi-resolution structures Biophys. Rev. 2 2010 21 27
    • (2010) Biophys. Rev. , vol.2 , pp. 21-27
    • Wriggers, W.1
  • 17
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov M.V., and Svergun D.I. Global rigid body modeling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 18
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 21
    • 80054053723 scopus 로고    scopus 로고
    • Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSI
    • Shen B.W., Xu D., Chan S.H., Zheng Y., Zhu Z., Xu S.Y., and Stoddard B.L. Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSI Nucleic Acids Res. 39 2011 8223 8236
    • (2011) Nucleic Acids Res. , vol.39 , pp. 8223-8236
    • Shen, B.W.1    Xu, D.2    Chan, S.H.3    Zheng, Y.4    Zhu, Z.5    Xu, S.Y.6    Stoddard, B.L.7
  • 22
  • 23
    • 50849083544 scopus 로고    scopus 로고
    • Crystal structure of a putative DNA methylase TTHA0409 from Thermus thermophilus HB8
    • Morita R., Ishikawa H., Nakagawa N., Kuramitsu S., and Masui R. Crystal structure of a putative DNA methylase TTHA0409 from Thermus thermophilus HB8 Proteins 73 2008 259 264
    • (2008) Proteins , vol.73 , pp. 259-264
    • Morita, R.1    Ishikawa, H.2    Nakagawa, N.3    Kuramitsu, S.4    Masui, R.5
  • 24
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
    • Schuck P., Perugini M.A., Gonzales N.R., Howlett G.J., and Schubert D. Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems Biophys. J. 82 2002 1096 1111
    • (2002) Biophys. J. , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 25
    • 77950552976 scopus 로고    scopus 로고
    • The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule
    • Brookes E., Demeler B., Rosano C., and Rocco M. The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule Eur. Biophys. J. 39 2010 423 435
    • (2010) Eur. Biophys. J. , vol.39 , pp. 423-435
    • Brookes, E.1    Demeler, B.2    Rosano, C.3    Rocco, M.4
  • 26
    • 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. Subunit assembly modulates the activities of the type III restriction-modification enzyme PstII in vitro Nucleic Acids Res. 33 2005 4788 4796
    • (2005) Nucleic Acids Res. , vol.33 , pp. 4788-4796
    • Sears, A.1    Szczelkun, M.D.2
  • 27
    • 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
  • 28
    • 0028936127 scopus 로고
    • ATP hydrolysis is required for DNA cleavage by EcoPI restriction enzyme
    • Saha S., and Rao D.N. ATP hydrolysis is required for DNA cleavage by EcoPI restriction enzyme J. Mol. Biol. 247 1995 559 567
    • (1995) J. Mol. Biol. , vol.247 , pp. 559-567
    • Saha, S.1    Rao, D.N.2
  • 30
    • 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
  • 31
    • 79953283489 scopus 로고    scopus 로고
    • The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair
    • Lammens K., Bemeleit D.J., Mockel C., Clausing E., Schele A., and Hartung S. The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair Cell 145 2011 54 66
    • (2011) Cell , vol.145 , pp. 54-66
    • Lammens, K.1    Bemeleit, D.J.2    Mockel, C.3    Clausing, E.4    Schele, A.5    Hartung, S.6


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