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Volumn 42, Issue 8, 2014, Pages 5139-5150

Type III restriction endonucleases are heterotrimeric: Comprising one helicase-nuclease subunit and a dimeric methyltransferase that binds only one specific DNA

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DEOXYRIBONUCLEASE; DNA METHYLTRANSFERASE; ECOP15I PROTEIN; ECOPI PROTEIN; HELICASE; HOLOENZYME; MULTIENZYME COMPLEX; NUCLEASE; PSTII PROTEIN; TYPE III SITE SPECIFIC DEOXYRIBONUCLEASE; UNCLASSIFIED DRUG;

EID: 84899868534     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku122     Document Type: Article
Times cited : (26)

References (44)
  • 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
    • 0027324744 scopus 로고
    • Biology of DNA restriction
    • Bickle, T.A. and Kruger, D.H. (1993) Biology of DNA restriction. Microbiol. Rev., 57, 434-450.
    • (1993) Microbiol. Rev. , vol.57 , pp. 434-450
    • Bickle, T.A.1    Kruger, D.H.2
  • 4
    • 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. (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    Kruger, D.H.3    Schroeder, C.4
  • 5
    • 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. (2010) 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, 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
  • 6
    • 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
  • 7
    • 77952727817 scopus 로고    scopus 로고
    • Maintaining a sense of direction during long-range communication on DNA
    • Szczelkun, M.D., Friedhoff, P. and Seidel, R. (2010) Maintaining a sense of direction during long-range communication on DNA. Biochem. Soc. Trans., 38, 404-409.
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 404-409
    • Szczelkun, M.D.1    Friedhoff, P.2    Seidel, R.3
  • 8
    • 84891788027 scopus 로고    scopus 로고
    • Type III restriction-modification enzymes: A historical perspective
    • Rao, D.N., Dryden, D.T. and Bheemanaik, S. (2014) Type III restriction-modification enzymes: a historical perspective. Nucleic Acids Res., 42, 45-55.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 45-55
    • Rao, D.N.1    Dryden, D.T.2    Bheemanaik, S.3
  • 9
    • 0021111764 scopus 로고
    • DNA restriction-modification enzymes of phage P1 and plasmid p15B. Subunit functions and structural homologies
    • Hadi, S.M., Bachi, B., Iida, S. and Bickle, T.A. (1983) DNA restriction-modification enzymes of phage P1 and plasmid p15B. Subunit functions and structural homologies. J. Mol. Biol., 165, 19-34.
    • (1983) J. Mol. Biol. , vol.165 , pp. 19-34
    • Hadi, S.M.1    Bachi, B.2    Iida, S.3    Bickle, T.A.4
  • 10
    • 0024388203 scopus 로고
    • Cloning, over-expression and the catalytic properties of the EcoP15 modification methylase from Escherichia coli
    • Rao, D.N., Page, M.G. and Bickle, T.A. (1989) Cloning, over-expression and the catalytic properties of the EcoP15 modification methylase from Escherichia coli. J. Mol. Biol., 209, 599-606.
    • (1989) J. Mol. Biol. , vol.209 , pp. 599-606
    • Rao, D.N.1    Page, M.G.2    Bickle, T.A.3
  • 11
    • 84862189790 scopus 로고    scopus 로고
    • Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering
    • Gupta, Y.K., Yang, L., Chan, S.H., Samuelson, J.C., Xu, S.Y. and Aggarwal, A.K. (2012) Structural insights into the assembly and shape of Type III restriction-modification (R-M) EcoP15I complex by small-angle X-ray scattering. J. Mol. Biol., 420, 261-268.
    • (2012) J. Mol. Biol. , vol.420 , pp. 261-268
    • Gupta, Y.K.1    Yang, L.2    Chan, S.H.3    Samuelson, J.C.4    Xu, S.Y.5    Aggarwal, A.K.6
  • 12
    • 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
  • 13
    • 0029035548 scopus 로고
    • DNA recognition by the EcoP15I and EcoPI modification methyltransferases
    • Ahmad, I., Krishnamurthy, V. and Rao, D.N. (1995) DNA recognition by the EcoP15I and EcoPI modification methyltransferases. Gene, 157, 143-147.
    • (1995) Gene , vol.157 , pp. 143-147
    • Ahmad, I.1    Krishnamurthy, V.2    Rao, D.N.3
  • 15
    • 4544262040 scopus 로고    scopus 로고
    • The Type i and III restriction endonucleases: Structural elements in molecular motors that process DNA
    • Pingound, A. (ed.) Springer, Germany
    • McClelland, S.E. and Szczelkun, M.D. (2004) The Type I and III restriction endonucleases: structural elements in molecular motors that process DNA. In: Pingound, A. (ed.), Restriction Enzymes, Nucleic Acids and Molecular Biology, Vol. 14. Springer, Germany, pp. 111-135.
    • (2004) Restriction Enzymes, Nucleic Acids and Molecular Biology , vol.14 , pp. 111-135
    • McClelland, S.E.1    Szczelkun, M.D.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
  • 17
    • 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., Schutkowski, M., Kruger, D.H. and Reuter, M. (2012) 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, 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    Kruger, D.H.7    Reuter, M.8
  • 18
    • 0029979544 scopus 로고    scopus 로고
    • Posttranscriptional regulation of EcoP1I and EcoP15I restriction activity
    • Redaschi, N. and Bickle, T.A. (1996) Posttranscriptional regulation of EcoP1I and EcoP15I restriction activity. J. Mol. Biol., 257, 790-803.
    • (1996) J. Mol. Biol. , vol.257 , pp. 790-803
    • Redaschi, N.1    Bickle, T.A.2
  • 20
    • 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. (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
    • Mucke, M.1    Reich, S.2    Moncke-Buchner, E.3    Reuter, M.4    Kruger, D.H.5
  • 21
    • 0037474547 scopus 로고    scopus 로고
    • A dimer of Escherichia coli UvrD is the active form of the helicase in vitro
    • Maluf, N.K., Fischer, C.J. and Lohman, T.M. (2003) A dimer of Escherichia coli UvrD is the active form of the helicase in vitro. J. Mol. Biol., 325, 913-935.
    • (2003) J. Mol. Biol. , vol.325 , pp. 913-935
    • Maluf, N.K.1    Fischer, C.J.2    Lohman, T.M.3
  • 22
    • 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
  • 23
    • 70349448467 scopus 로고    scopus 로고
    • Dimeric/oligomeric DNA methyltransferases: An unfinished story
    • Malygin, E.G., Evdokimov, A.A. and Hattman, S. (2009) Dimeric/oligomeric DNA methyltransferases: an unfinished story. Biol. Chem., 390, 835-844.
    • (2009) Biol. Chem. , vol.390 , pp. 835-844
    • Malygin, E.G.1    Evdokimov, A.A.2    Hattman, S.3
  • 24
    • 84857437459 scopus 로고    scopus 로고
    • DNA methyltransferases: Mechanistic models derived from kinetic analysis
    • Malygin, E.G. and Hattman, S. (2012) DNA methyltransferases: mechanistic models derived from kinetic analysis. Crit. Rev. Biochem. Mol. Biol., 47, 97-193.
    • (2012) Crit. Rev. Biochem. Mol. Biol. , vol.47 , pp. 97-193
    • Malygin, E.G.1    Hattman, S.2
  • 26
    • 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. (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    Roes, S.2    Dryden, D.T.3    Rao, D.N.4    Edwardson, J.M.5    Henderson, R.M.6
  • 28
    • 84876346296 scopus 로고    scopus 로고
    • The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA
    • Schwarz, F.W., Toth, J., van Aelst, K., Cui, G., Clausing, S., Szczelkun, M.D. and Seidel, R. (2013) The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA. Science, 340, 353-356.
    • (2013) Science , vol.340 , pp. 353-356
    • Schwarz, F.W.1    Toth, J.2    Van Aelst, K.3    Cui, G.4    Clausing, S.5    Szczelkun, M.D.6    Seidel, R.7
  • 29
    • 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
  • 30
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott, F., Hernandez, H., McCammon, M.G., Tito, M.A. and Robinson, C.V. (2002) A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal Chem, 74, 1402-1407.
    • (2002) Anal Chem , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 32
    • 84878106641 scopus 로고    scopus 로고
    • Native ion mobility-mass spectrometry and related methods in structural biology
    • Konijnenberg, A., Butterer, A. and Sobott, F. (2013) Native ion mobility-mass spectrometry and related methods in structural biology. Biochim et Biophys Acta, 1834, 1239-1256.
    • (2013) Biochim et Biophys Acta , vol.1834 , pp. 1239-1256
    • Konijnenberg, A.1    Butterer, A.2    Sobott, F.3
  • 33
    • 19944432588 scopus 로고    scopus 로고
    • The flight of macromolecular complexes in a mass spectrometer
    • discussion 389-391
    • Sobott, F., McCammon, M.G., Hernandez, H. and Robinson, C.V. (2005) The flight of macromolecular complexes in a mass spectrometer. Philos. T. Roy. Soc. A, 363, 379-389; discussion 389-391.
    • (2005) Philos. T. Roy. Soc. A , vol.363 , pp. 379-389
    • Sobott, F.1    McCammon, M.G.2    Hernandez, H.3    Robinson, C.V.4
  • 35
    • 0031877113 scopus 로고    scopus 로고
    • Submicrometer particle sizing by multiangle light scattering following fractionation
    • Wyatt, P.J. (1998) Submicrometer particle sizing by multiangle light scattering following fractionation. J. Colloid Interf. Sci., 197, 9-20.
    • (1998) J. Colloid Interf. Sci. , vol.197 , pp. 9-20
    • Wyatt, P.J.1
  • 36
    • 84865858205 scopus 로고    scopus 로고
    • Do charge state signatures guarantee protein conformations?
    • Hall, Z. and Robinson, C.V. (2012) Do charge state signatures guarantee protein conformations? J. Am. Soc. Mass Spectr., 23, 1161-1168.
    • (2012) J. Am. Soc. Mass Spectr. , vol.23 , pp. 1161-1168
    • Hall, Z.1    Robinson, C.V.2
  • 37
    • 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
  • 38
    • 62649172171 scopus 로고    scopus 로고
    • Dimerization of DNA methyltransferase 1 is mediated by its regulatory domain
    • Fellinger, K., Rothbauer, U., Felle, M., Langst, G. and Leonhardt, H. (2009) Dimerization of DNA methyltransferase 1 is mediated by its regulatory domain. J. Cell. Biochem., 106, 521-528.
    • (2009) J. Cell. Biochem. , vol.106 , pp. 521-528
    • Fellinger, K.1    Rothbauer, U.2    Felle, M.3    Langst, G.4    Leonhardt, H.5
  • 39
    • 0344443347 scopus 로고    scopus 로고
    • Crystal structure of MboIIA methyltransferase
    • Osipiuk, J., Walsh, M.A. and Joachimiak, A. (2003) Crystal structure of MboIIA methyltransferase. Nucleic Acids Res., 31, 5440-5448.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5440-5448
    • Osipiuk, J.1    Walsh, M.A.2    Joachimiak, A.3
  • 41
    • 33644870800 scopus 로고    scopus 로고
    • Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase
    • Thomas, C.B. and Gumport, R.I. (2006) Dimerization of the bacterial RsrI N6-adenine DNA methyltransferase. Nucleic Acids Res., 34, 806-815.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 806-815
    • Thomas, C.B.1    Gumport, R.I.2
  • 42
    • 0018800362 scopus 로고
    • Methylation and cleavage sequences of the EcoP1 restriction-modification enzyme
    • Bachi, B., Reiser, J. and Pirrotta, V. (1979) Methylation and cleavage sequences of the EcoP1 restriction-modification enzyme. J. Mol. Biol., 128, 143-163.
    • (1979) J. Mol. Biol. , vol.128 , pp. 143-163
    • Bachi, B.1    Reiser, J.2    Pirrotta, V.3
  • 43
    • 0025767319 scopus 로고
    • M. EcoP15 methylates the second adenine in its recognition sequence
    • Meisel, A., Kruger, D.H. and Bickle, T.A. (1991) M. EcoP15 methylates the second adenine in its recognition sequence. Nucleic Acids Res., 19, 3997.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3997
    • Meisel, A.1    Kruger, D.H.2    Bickle, T.A.3
  • 44
    • 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


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