메뉴 건너뛰기




Volumn 42, Issue 1, 2014, Pages 45-55

Type III restriction-modification enzymes: A historical perspective

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; METHIONINE; S ADENOSYLMETHIONINE; TYPE III SITE SPECIFIC DEOXYRIBONUCLEASE; ADENOSINE TRIPHOSPHATASE; DNA METHYLTRANSFERASE; OLIGOMER; RESTRICTION ENDONUCLEASE; TYPE III RESTRICTION MODIFICATION ENZYME; UNCLASSIFIED DRUG;

EID: 84891788027     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt616     Document Type: Review
Times cited : (112)

References (81)
  • 1
    • 0001875393 scopus 로고
    • Host specificity of DNA produced by Escherichia coli. I. Host controlled modification of bacteriophage lambda
    • Arber, W. and Dussoix, D. (1962) Host specificity of DNA produced by Escherichia coli. I. Host controlled modification of bacteriophage lambda. J. Mol. Biol., 5, 18-36
    • (1962) J. Mol. Biol , vol.5 , pp. 18-36
    • Arber, W.1    Dussoix, D.2
  • 3
    • 0007914542 scopus 로고
    • Host specificity of DNA produced by Escherichia coli VI Effects on bacterial conjugation
    • Arber, W. and Morse, M.L. (1965) Host specificity of DNA produced by Escherichia coli. VI. Effects on bacterial conjugation. Genetics., 51, 137-148
    • (1965) Genetics , vol.51 , pp. 137-148
    • Arber, W.1    Morse, M.L.2
  • 4
    • 0000461381 scopus 로고
    • Host-controlled modification of bacteriophage
    • Arber, W. (1965) Host-controlled modification of bacteriophage. Annu. Rev. Microbiol., 19, 365-378
    • (1965) Annu. Rev. Microbiol , vol.19 , pp. 365-378
    • Arber, W.1
  • 5
    • 76549165742 scopus 로고
    • Intracellular modification of nucleic acids
    • Stacey, K.A. (1965) Intracellular modification of nucleic acids. Br. Med. Bull., 21, 211-216
    • (1965) Br. Med. Bull , vol.21 , pp. 211-216
    • Stacey, K.A.1
  • 6
    • 0014462494 scopus 로고
    • DNA modification and restriction
    • Arber, W. and Linn, S. (1969) DNA modification and restriction. Annu. Rev. Biochem., 38, 467-500
    • (1969) Annu. Rev. Biochem , vol.38 , pp. 467-500
    • Arber, W.1    Linn, S.2
  • 7
    • 0014724993 scopus 로고
    • Host specificity of DNA produced by Escherichia coli. XII. The two restriction and modification systems of strain 15T
    • Arber, W. and Wauters-Willems, D. (1970) Host specificity of DNA produced by Escherichia coli. XII. The two restriction and modification systems of strain 15T-. Mol. Gen. Genet., 108, 203-217
    • (1970) Mol. Gen. Genet , vol.108 , pp. 203-217
    • Arber, W.1    Wauters-Willems, D.2
  • 8
    • 0001252170 scopus 로고
    • Suppression of the multiplication of heterologous bacteriophages in lysogenic bacteria
    • Lederberg, S. (1957) Suppression of the multiplication of heterologous bacteriophages in lysogenic bacteria. Virology., 3, 496-513
    • (1957) Virology , vol.3 , pp. 496-513
    • Lederberg, S.1
  • 9
    • 0001875394 scopus 로고
    • Host specificity of DNA produced by Escherichia coli II Control over acceptance of DNA from infecting phage lambda
    • Dussoix, D. and Arber, W. (1962) Host specificity of DNA produced by Escherichia coli. II. Control over acceptance of DNA from infecting phage lambda. J. Mol. Biol., 5, 37-49
    • (1962) J. Mol. Biol , vol.5 , pp. 37-49
    • Dussoix, D.1    Arber, W.2
  • 10
    • 0018216571 scopus 로고
    • Purification and properties of a new restriction endonuclease from Haemophilus influenzae Rf
    • Kauc, L. and Piekarowicz, A. (1978) Purification and properties of a new restriction endonuclease from Haemophilus influenzae Rf. Eur. J. Biochem., 92, 417-426
    • (1978) Eur. J. Biochem , vol.92 , pp. 417-426
    • Kauc, L.1    Piekarowicz, A.2
  • 11
    • 0014945320 scopus 로고
    • Host specificity of DNA produced by Escherichia coli 13 Breakdown of cellular DNA upon growth in ethionine of strains with r+ 15, r+ P1 or r+ N3 restriction phenotyees
    • Lark, C. and Arber, W. (1970) Host specificity of DNA produced by Escherichia coli. 13. Breakdown of cellular DNA upon growth in ethionine of strains with r+ 15, r+ P1 or r+ N3 restriction phenotypes. J. Mol. Biol., 52, 337-348
    • (1970) J. Mol. Biol , vol.52 , pp. 337-348
    • Lark, C.1    Arber, W.2
  • 12
    • 0014427164 scopus 로고
    • DNA restriction enzyme from E coli
    • Meselson, M. and Yuan, R. (1968) DNA restriction enzyme from E. coli. Nature, 217, 1110-1114
    • (1968) Nature , vol.217 , pp. 1110-1114
    • Meselson, M.1    Yuan, R.2
  • 13
    • 0016350498 scopus 로고
    • The bacteriophage P1 restriction endonuclease
    • Haberman, A. (1974) The bacteriophage P1 restriction endonuclease. J. Mol. Biol., 89, 545-563
    • (1974) J. Mol. Biol , vol.89 , pp. 545-563
    • Haberman, A.1
  • 14
    • 0015522466 scopus 로고
    • Host specificity of DNA in Haemophilus influenzae: Restriction and modification in strain Rd
    • Glover, S.W. and Piekarowicz, A. (1972) Host specificity of DNA in Haemophilus influenzae: Restriction and modification in strain Rd. Biochem. Biophys. Res. Commun., 46, 1610-1617
    • (1972) Biochem. Biophys. Res. Commun , vol.46 , pp. 1610-1617
    • Glover, S.W.1    Piekarowicz, A.2
  • 15
    • 0016234213 scopus 로고
    • Host specificity of DNA in Haemophilus influenzae: Similarity between host-specificity types of Haemophilus influenza Re and Rf
    • Piekarowicz, A. and Kalinowska, J. (1974) Host specificity of DNA in Haemophilus influenzae: Similarity between host-specificity types of Haemophilus influenza Re and Rf. J. Gen. Microbiol., 81, 405-411
    • (1974) J. Gen. Microbiol , vol.81 , pp. 405-411
    • Piekarowicz, A.1    Kalinowska, J.2
  • 16
    • 0016199958 scopus 로고
    • Host specificity of DNA in Haemophilus influenzae: The restriction and modification systems in strains Rb and Rf
    • Piekarowicz, A., Kauc, L. and Glover, S.W. (1974) Host specificity of DNA in Haemophilus influenzae: The restriction and modification systems in strains Rb and Rf. J. Gen. Microbiol., 81, 391-403
    • (1974) J. Gen. Microbiol , vol.81 , pp. 391-403
    • Piekarowicz, A.1    Kauc, L.2    Glover, S.W.3
  • 17
    • 0016006298 scopus 로고
    • The influence of methionine deprivation on restriction properties of Haemophilus influenzae Rd and Ra strains
    • Piekarowicz, A. (1974) The influence of methionine deprivation on restriction properties of Haemophilus influenzae Rd and Ra strains. Acta Microbiol. Pol. A., 6, 71-74
    • (1974) Acta Microbiol. Pol. A. , vol.6 , pp. 71-74
    • Piekarowicz, A.1
  • 18
    • 84860487715 scopus 로고
    • The control of host-induced modification by phage P1
    • Glover, S.W., Schell, J., Symonds, N. and Stacey, K.A. (1963) The control of host-induced modification by phage P1. Genet. Res., 4, 480-482
    • (1963) Genet. Res , vol.4 , pp. 480-482
    • Glover, S.W.1    Schell, J.2    Symonds, N.3    Stacey, K.A.4
  • 19
    • 0014783509 scopus 로고
    • Clear plaque mutants of phage P1
    • Scott, J.R. (1970) Clear plaque mutants of phage P1. Virology, 41, 66-71
    • (1970) Virology , vol.41 , pp. 66-71
    • Scott, J.R.1
  • 20
    • 0015588599 scopus 로고
    • Modification-deficient mutants of bacteriophage P1 I Restriction by P1 cryptic lysogens
    • Rosner, J.L. (1973) Modification-deficient mutants of bacteriophage P1. I. Restriction by P1 cryptic lysogens. Virology, 52, 213-222
    • (1973) Virology , vol.52 , pp. 213-222
    • Rosner, J.L.1
  • 21
    • 0024670901 scopus 로고
    • Characterization of mutations of the bacteriophage P1 mod gene encoding the recognition subunit of the EcoP1 restriction and modification system
    • Rao, D.N., Eberle, H. and Bickle, T.A. (1989) Characterization of mutations of the bacteriophage P1 mod gene encoding the recognition subunit of the EcoP1 restriction and modification system. J. Bacteriol., 171, 2347-2352
    • (1989) J. Bacteriol , vol.171 , pp. 2347-2352
    • Rao, D.N.1    Eberle, H.2    Bickle, T.A.3
  • 22
    • 0014394062 scopus 로고
    • Prophage P1, and extrachromosomal replication unit
    • Ikeda, H. and Tomizawa, J. (1968) Prophage P1, and extrachromosomal replication unit. Cold Spring Harb. Symp. Quant. Biol., 33, 791-798
    • (1968) Cold Spring Harb. Symp. Quant. Biol , vol.33 , pp. 791-798
    • Ikeda, H.1    Tomizawa, J.2
  • 23
    • 0017413232 scopus 로고
    • Physical mapping of BglII, BamHI, EcoRI, HindIII and PstI restriction fragments of bacteriophage P1 DNA
    • Bächi, B. and Arber, W. (1977) Physical mapping of BglII, BamHI, EcoRI, HindIII and PstI restriction fragments of bacteriophage P1 DNA. Mol. Gen. Genet., 153, 311-324
    • (1977) Mol. Gen. Genet , vol.153 , pp. 311-324
    • Bächi, B.1    Arber, W.2
  • 24
    • 0018425317 scopus 로고
    • Isolation and characterization of cloned fragments of bacteriophage P1 DNA
    • Mural, R.J., Chesney, R.H., Vapnek, D., Kropf, M.M. and Scott, J.R. (1979) Isolation and characterization of cloned fragments of bacteriophage P1 DNA. Virology, 93, 387-397
    • (1979) Virology , vol.93 , pp. 387-397
    • Mural, R.J.1    Chesney, R.H.2    Vapnek, D.3    Kropf, M.M.4    Scott, J.R.5
  • 25
    • 0019132859 scopus 로고
    • Transposon mutagenesis of the gene encoding the bacteriophage P1 restriction endonuclease co-linearity of the gene and gene product
    • Heilmann, H., Burkardt, H.J., Pühler, A. and Reeve, J.N. (1980) Transposon mutagenesis of the gene encoding the bacteriophage P1 restriction endonuclease. Co-linearity of the gene and gene product. J. Mol. Biol., 144, 387-396
    • (1980) J. Mol. Biol , vol.144 , pp. 387-396
    • Heilmann, H.1    Burkardt, H.J.2    Pühler, A.3    Reeve, J.N.4
  • 29
    • 0024278335 scopus 로고
    • Type III DNA restriction and modification systems ecop1 and ecop15 nucleotide sequence of the ecop1 operon, the ecop15 mod gene and some ecop1 mod mutants
    • Hümbelin, M., Suri, B., Rao, D.N., Hornby, D.P., Eberle, H., Pripfl, T., Kenel, S. and Bickle, T.A. (1988) Type III DNA restriction and modification systems EcoP1 and EcoP15. Nucleotide sequence of the EcoP1 operon, the EcoP15 mod gene and some EcoP1 mod mutants. J. Mol. Biol., 200, 23-29
    • (1988) J. Mol. Biol , vol.200 , pp. 23-29
    • Hümbelin, M.1    Suri, B.2    Rao, D.N.3    Hornby, D.P.4    Eberle, H.5    Pripfl, T.6    Kenel, S.7    Bickle, T.A.8
  • 30
    • 0021111764 scopus 로고
    • DNA restriction-modification enzymes of phage p1 and plasmid p15b subunit functions and structural homologies
    • Hadi, S.M., Bächi, 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    Bächi, B.2    Iida, S.3    Bickle, T.A.4
  • 31
    • 0003088269 scopus 로고
    • Strain-specific modification and restriction of DNA in bacteria
    • Arber, W., Yuan, R. and Bickle, T.A. (1975) Strain-specific modification and restriction of DNA in bacteria. FEBS Proc. Symp., 9, 3-22
    • (1975) FEBS Proc. Symp , vol.9 , pp. 3-22
    • Arber, W.1    Yuan, R.2    Bickle, T.A.3
  • 32
    • 0001399793 scopus 로고
    • Bacteriophage P1
    • In: Calendar, R. (ed 1 Plenum Publishing Corporation, New York, NY
    • Yarmolinsky, M.B. and Sternberg, N. (1988) Bacteriophage P1. In: Calendar, R. (ed.), The Bacteriophages, Vol. 1. Plenum Publishing Corporation, New York, NY, pp. 291-438
    • (1988) Bacteriophages , pp. 291-438
    • Yarmolinsky, M.B.1    Sternberg, N.2
  • 33
    • 0026066060 scopus 로고
    • Transcriptional analysis of the restriction and modification genes of bacteriophage P1
    • Sharrocks, A.D. and Hornby, D.P. (1991) Transcriptional analysis of the restriction and modification genes of bacteriophage P1. Mol. Microbiol., 5, 685-694
    • (1991) Mol. Microbiol , vol.5 , pp. 685-694
    • Sharrocks, A.D.1    Hornby, D.P.2
  • 34
    • 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
  • 35
    • 0014277562 scopus 로고
    • Host specificity of DNA produced by escherichia coli, x in vitro restriction of phage fd replicative form
    • Linn, S. and Arber, W. (1968) Host specificity of DNA produced by Escherichia coli, X. In vitro restriction of phage fd replicative form. Proc. Natl Acad. Sci. USA, 59, 1300-1306
    • (1968) Proc. Natl Acad. Sci. USA , vol.59 , pp. 1300-1306
    • Linn, S.1    Arber, W.2
  • 37
    • 0015313287 scopus 로고
    • The deoxyribonucleic acid modification 1enzyme of bacteriophage P1
    • Brockes, J.P., Brown, P.R. and Murray, K. (1972) The deoxyribonucleic acid modification 1enzyme of bacteriophage P1. Biochem. J., 127, 1-10
    • (1972) Biochem. J. , vol.127 , pp. 1-10
    • Brockes, J.P.1    Brown, P.R.2    Murray, K.3
  • 38
    • 0015793428 scopus 로고
    • The deoxyribonucleic acid-modification enzyme of bacteriophage p1 subunit structure
    • Brockes, J.P. (1973) The deoxyribonucleic acid-modification enzyme of bacteriophage P1. Subunit structure. Biochem. J., 133, 629-633
    • (1973) Biochem. J. , vol.133 , pp. 629-633
    • Brockes, J.P.1
  • 39
    • 0021697631 scopus 로고
    • Preferential cleavage by restriction endonuclease HinfIII
    • Piekarowicz, A. (1984) Preferential cleavage by restriction endonuclease HinfIII. Acta Biochim. Pol., 31, 453-464
    • (1984) Acta Biochim. Pol , vol.31 , pp. 453-464
    • Piekarowicz, A.1
  • 40
    • 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
  • 41
    • 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
  • 42
    • 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
  • 43
    • 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., Möncke-Buchner, E., Schutkowski, M., Krüger, 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    Möncke-Buchner, E.5    Schutkowski, M.6    Krüger, D.H.7    Reuter, M.8
  • 44
    • 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
  • 45
    • 0017579598 scopus 로고
    • Purification and properties of the P15 specific restriction endonuclease from Escherichia coli
    • Reiser, J. and Yuan, R. (1977) Purification and properties of the P15 specific restriction endonuclease from Escherichia coli. J. Biol. Chem., 252, 451-456
    • (1977) J. Biol. Chem , vol.252 , pp. 451-456
    • Reiser, J.1    Yuan, R.2
  • 46
    • 0019203695 scopus 로고
    • Role of ATP in the cleavage mechanism of the EcoP15 restriction endonuclease
    • Yuan, R., Hamilton, D.L., Hadi, S.M. and Bickle, T.A. (1980) Role of ATP in the cleavage mechanism of the EcoP15 restriction endonuclease. J. Mol. Biol., 144, 501-419
    • (1980) J. Mol. Biol , vol.144 , pp. 501-419
    • Yuan, R.1    Hamilton, D.L.2    Hadi, S.M.3    Bickle, T.A.4
  • 47
    • 0017830222 scopus 로고
    • Steps in the reaction mechanism of the Escherichia coli plasmid P15-specific restriction endonuclease
    • Yuan, R. and Reiser, J. (1978) Steps in the reaction mechanism of the Escherichia coli plasmid P15-specific restriction endonuclease. J. Mol. Biol., 122, 433-445
    • (1978) J. Mol. Biol , vol.122 , pp. 433-445
    • Yuan, R.1    Reiser, J.2
  • 48
    • 84891810021 scopus 로고
    • The role of Sadenosyl- L-methionine in the cleavage of deoxyribonucleic acid by the restriction endonuclease
    • Hadi, S.M., Bickle, T.A. and Yuan, R. (1975) The role of Sadenosyl- L-methionine in the cleavage of deoxyribonucleic acid by the restriction endonuclease. J. Mol. Biol., 134, 655-666
    • (1975) J. Mol. Biol , vol.134 , pp. 655-666
    • Hadi, S.M.1    Bickle, T.A.2    Yuan, R.3
  • 49
    • 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., Krüger, 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. , Issue.14 , pp. 2958-2966
    • Meisel, A.1    Mackeldanz, P.2    Bickle, T.A.3    Krüger, D.H.4    Schroeder, C.5
  • 50
    • 0016299917 scopus 로고
    • Nucleotide sequences at the sites of action of the deoxyribonucleic acid modification enzyme of bacteriophage P1
    • Brockes, J.P., Brown, P.R. and Murray, K. (1974) Nucleotide sequences at the sites of action of the deoxyribonucleic acid modification enzyme of bacteriophage P1. J. Mol. Biol., 88, 437-443
    • (1974) J. Mol. Biol , vol.88 , pp. 437-443
    • Brockes, J.P.1    Brown, P.R.2    Murray, K.3
  • 51
    • 0018214882 scopus 로고
    • Sequence specificity of the P1 modification methylase (M.EcoP1) and the DNA methylase (M.Ecodam) controlled by the Escherichia coli dam gene
    • Hattman, S., Brooks, J.E. and Masurekar, M. (1978) Sequence specificity of the P1 modification methylase (M.EcoP1) and the DNA methylase (M.Ecodam) controlled by the Escherichia coli dam gene. J. Mol. Biol., 126, 367-380
    • (1978) J. Mol. Biol , vol.126 , pp. 367-380
    • Hattman, S.1    Brooks, J.E.2    Masurekar, M.3
  • 52
    • 0018800362 scopus 로고
    • Methylation and cleavage sequences of the EcoP1 restriction-modification enzyme
    • Bächi, 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
    • Bächi, B.1    Reiser, J.2    Pirrotta, V.3
  • 53
    • 0025767319 scopus 로고
    • M EcoP15 methylates the second adenine in its recognition sequence
    • Meisel, A., Krüger, 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    Krüger, D.H.2    Bickle, T.A.3
  • 54
    • 0019944002 scopus 로고
    • HineI is an isoschizomer of HinfIII restriction endonuclease
    • Piekarowicz, A. (1982) HineI is an isoschizomer of HinfIII restriction endonuclease. J. Mol. Biol., 157, 373-381
    • (1982) J. Mol. Biol , vol.157 , pp. 373-381
    • Piekarowicz, A.1
  • 55
    • 0019880373 scopus 로고
    • The DNA sequence recognised by the HinfIII restriction endonuclease
    • Piekarowicz, A., Bickle, T.A., Shepherd, J.C. and Ineichen, K. (1981) The DNA sequence recognised by the HinfIII restriction endonuclease. J. Mol .Biol., 146, 167-172
    • (1981) J. Mol .Biol , vol.146 , pp. 167-172
    • Piekarowicz, A.1    Bickle, T.A.2    Shepherd, J.C.3    Ineichen, K.4
  • 56
    • 0015929640 scopus 로고
    • Studies of SV 40 DNA V Conversion of circular to linear SV 40 DNA by restriction endonuclease from Escherichia coli B
    • Adler, S.P. and Nathans, D. (1973) Studies of SV 40 DNA. V. Conversion of circular to linear SV 40 DNA by restriction endonuclease from Escherichia coli B. Biochim. Biophys. Acta, 299, 177-188
    • (1973) Biochim. Biophys. Acta , vol.299 , pp. 177-188
    • Adler, S.P.1    Nathans, D.2
  • 57
    • 0016311617 scopus 로고
    • Action of Escherichia coli P1 restriction endonuclease on simian virus 40 DNA
    • Risser, R., Hopkins, N., Davis, R.W., Delius, H. and Mulder, C. (1974) Action of Escherichia coli P1 restriction endonuclease on simian virus 40 DNA. J. Mol. Biol., 89, 517-544
    • (1974) J. Mol. Biol , vol.89 , pp. 517-544
    • Risser, R.1    Hopkins, N.2    Davis, R.W.3    Delius, H.4    Mulder, C.5
  • 58
    • 0019219860 scopus 로고
    • Cleavage and methylation of DNA by the resytriction endonuclease HinfIII isolated from Haemophilus influenzae Rf
    • Piekarowicz, A. and Brzezinski, R. (1980) Cleavage and methylation of DNA by the resytriction endonuclease HinfIII isolated from Haemophilus influenzae Rf. J. Mol. Biol., 144, 415-429
    • (1980) J. Mol. Biol , vol.144 , pp. 415-429
    • Piekarowicz, A.1    Brzezinski, R.2
  • 59
    • 0022410842 scopus 로고
    • DNA methylation of bacterial viruses T3 and T7 by different DNA methylases in Escherichia coli K12 cells
    • Krüger, D.H., Schroeder, C., Reuter, M., Bogdarina, I.G., Buryanov, Y.I. and Bickle, T.A. (1985) DNA methylation of bacterial viruses T3 and T7 by different DNA methylases in Escherichia coli K12 cells. Eur. J. Biochem., 150, 323-330
    • (1985) Eur. J. Biochem , vol.150 , pp. 323-330
    • Krüger, D.H.1    Schroeder, C.2    Reuter, M.3    Bogdarina, I.G.4    Buryanov, Y.I.5    Bickle, T.A.6
  • 60
    • 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
  • 61
    • 0035965141 scopus 로고    scopus 로고
    • DNA cleavage by type III restrictionmodification 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 restrictionmodification 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
  • 62
    • 63449097890 scopus 로고    scopus 로고
    • Functional characterization and modulation of the DNA cleavage efficiency of type III restriction endonuclease EcoP15I in its interaction with two sites in the DNA target
    • Möncke-Buchner, E., Rothenberg, M., Reich, S., Wagenführ, K., Matsumura, H., Terauchi, R., Krüger, D.H. and Reuter, M. (2009) Functional characterization and modulation of the DNA cleavage efficiency of type III restriction endonuclease EcoP15I in its interaction with two sites in the DNA target. J. Mol. Biol., 387, 1309-1319
    • (2009) J. Mol. Biol , vol.387 , pp. 1309-1319
    • Möncke-Buchner, E.1    Rothenberg, M.2    Reich, S.3    Wagenführ, K.4    Matsumura, H.5    Terauchi, R.6    Krüger, D.H.7    Reuter, M.8
  • 63
    • 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
  • 64
    • 77952722979 scopus 로고    scopus 로고
    • Type III restriction enzymes cleave DNA by long-range interaction between sites in both head-Tohead and tail-To-Tail inverted repeat
    • van Aelst, K., Töth, 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-Tohead 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    Töth, J.2    Ramanathan, S.P.3    Schwarz, F.W.4    Seidel, R.5    Szczelkun, M.D.6
  • 65
    • 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
  • 66
    • 0037388105 scopus 로고    scopus 로고
    • Functional cooperation between exonucleases and endonucleases-basis for the evolution of restriction enzymes
    • Raghavendra, N.K. and Rao, D.N. (2003) Functional cooperation between exonucleases and endonucleases-basis for the evolution of restriction enzymes. Nucleic Acids Res., 31, 1888-1896
    • (2003) Nucleic Acids Res , vol.31 , pp. 1888-1896
    • Raghavendra, N.K.1    Rao, D.N.2
  • 67
    • 79959383539 scopus 로고    scopus 로고
    • DNA translocation by type III restriction enzymes: A comparison of current models of their operation derived from ensemble and single-molecule measurements
    • Dryden, D.T., Edwardson, J.M. and Henderson, R.M. (2011) DNA translocation by type III restriction enzymes: A comparison of current models of their operation derived from ensemble and single-molecule measurements. Nucleic Acids Res., 39, 4525-4531
    • (2011) Nucleic Acids Res , vol.39 , pp. 4525-4531
    • Dryden, D.T.1    Edwardson, J.M.2    Henderson, R.M.3
  • 68
    • 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. (2011) Translocation, switching and gating: Potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases. Biochem. Soc. Trans., 39, 589-594
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 589-594
    • Szczelkun, M.D.1
  • 69
    • 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
  • 71
    • 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
  • 73
    • 84876346296 scopus 로고    scopus 로고
    • The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA
    • Schwarz, F.W., Töth, 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    Töth, J.2    Van Aelst, K.3    Cui, G.4    Clausing, S.5    Szczelkun, M.D.6    Seidel, R.7
  • 74
    • 0033559871 scopus 로고    scopus 로고
    • Characterization of a CACAG pentanucleotide repeat in Pasteurella haemolytica and its possible role in modulation of a novel type III restriction-modification system
    • Ryan, K.A. and Lo, R.Y. (1999) Characterization of a CACAG pentanucleotide repeat in Pasteurella haemolytica and its possible role in modulation of a novel type III restriction-modification system. Nucleic Acids Res., 27, 1505-1511
    • (1999) Nucleic Acids Res , vol.27 , pp. 1505-1511
    • Ryan, K.A.1    Lo, R.Y.2
  • 75
    • 0033972220 scopus 로고    scopus 로고
    • The length of a tetranucleotide repeat tract in Haemophilus influenzae determines the phase variation rate of a gene with homology to type III DNA methyltransferases
    • De Bolle, X., Bayliss, C.D., Field, D., van de Ven, T., Saunders, N.J., Hood, D.W. and Moxon, E.R. (2000) The length of a tetranucleotide repeat tract in Haemophilus influenzae determines the phase variation rate of a gene with homology to type III DNA methyltransferases. Mol. Microbiol., 35, 211-222
    • (2000) Mol. Microbiol , vol.35 , pp. 211-222
    • De Bolle, X.1    Bayliss, C.D.2    Field, D.3    Van De Ven, T.4    Saunders, N.J.5    Hood, D.W.6    Moxon, E.R.7
  • 78
    • 76949108806 scopus 로고    scopus 로고
    • The phasevarion: Phase variation of type III DNA methyltransferases controls coordinated switching in multiple genes
    • Srikhanta, Y.N., Fox, K.L. and Jennings, M.P. (2010) The phasevarion: Phase variation of type III DNA methyltransferases controls coordinated switching in multiple genes. Nat. Rev. Microbiol., 8, 196-206
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 196-206
    • Srikhanta, Y.N.1    Fox, K.L.2    Jennings, M.P.3
  • 80
    • 22744453077 scopus 로고    scopus 로고
    • Exogenous AdoMet and its analogue sinefungin differentially influence DNA cleavage by R.EcoP15I-usefulness in SAGE
    • Raghavendra, N.K. and Rao, D.N. (2005) Exogenous AdoMet and its analogue sinefungin differentially influence DNA cleavage by R.EcoP15I-usefulness in SAGE. Biochem. Biophys. Res. Commun., 334, 803-811
    • (2005) Biochem Biophys. Res. Commun , vol.334 , pp. 803-811
    • Raghavendra, N.K.1    Rao, D.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.