메뉴 건너뛰기




Volumn 69, Issue 5, 2003, Pages 2638-2650

Genetic organization and molecular analysis of the EcoVIII restriction-modification system of Escherichia coli E1585-68 and its comparison with isospecific homologs

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; ESCHERICHIA COLI; GENES; GENETIC ENGINEERING;

EID: 0037545613     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.69.5.2638-2650.2003     Document Type: Article
Times cited : (12)

References (90)
  • 1
    • 0021929046 scopus 로고
    • Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
    • Alatossava, T., H. Jutte, A. Kuhn, and E. Kellenberger. 1985. Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187. J. Bacteriol. 162:413-419.
    • (1985) J. Bacteriol. , vol.162 , pp. 413-419
    • Alatossava, T.1    Jutte, H.2    Kuhn, A.3    Kellenberger, E.4
  • 3
    • 0023904810 scopus 로고
    • Overproduction, purification and crystallization of TaqI restriction endonuclease
    • Barany, F. 1988. Overproduction, purification and crystallization of TaqI restriction endonuclease. Gene 65:167-177.
    • (1988) Gene , vol.65 , pp. 167-177
    • Barany, F.1
  • 4
    • 0026588648 scopus 로고
    • Cloning and sequencing of genes encoding the TthHB8I restriction and modification enzymes: Comparison with the isoschizomeric TaqI enzymes
    • Barany, F., M. Danzitz, J. Zebala, and A. Mayer. 1992. Cloning and sequencing of genes encoding the TthHB8I restriction and modification enzymes: comparison with the isoschizomeric TaqI enzymes. Gene 112:3-12.
    • (1992) Gene , vol.112 , pp. 3-12
    • Barany, F.1    Danzitz, M.2    Zebala, J.3    Mayer, A.4
  • 7
    • 0029995002 scopus 로고    scopus 로고
    • Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 Å resolution
    • Bozic, D., S. Grazulis, V. Siksnys, and R. Huber. 1996. Crystal structure of Citrobacter freundii restriction endonuclease Cfr10I at 2.15 Å resolution. J. Mol. Biol. 255:176-186.
    • (1996) J. Mol. Biol. , vol.255 , pp. 176-186
    • Bozic, D.1    Grazulis, S.2    Siksnys, V.3    Huber, R.4
  • 8
    • 0018848403 scopus 로고
    • A general method for defining restriction enzyme cleavage and recognition sites
    • Brown, N. L., and M. Smith. 1980. A general method for defining restriction enzyme cleavage and recognition sites. Methods Enzymol. 65:391-404.
    • (1980) Methods Enzymol. , vol.65 , pp. 391-404
    • Brown, N.L.1    Smith, M.2
  • 9
    • 0033933471 scopus 로고    scopus 로고
    • Phylogeny of the restriction endonuclease-like superfamily inferred from comparison of protein structure
    • Bujnicki, J. M. 2000. Phylogeny of the restriction endonuclease-like superfamily inferred from comparison of protein structure. J. Mol. Evol. 50:39-44.
    • (2000) J. Mol. Evol. , vol.50 , pp. 39-44
    • Bujnicki, J.M.1
  • 10
    • 0035750103 scopus 로고    scopus 로고
    • Understanding the evolution of restriction-modification systems: Clues from sequence and structure comparisons
    • Bujnicki, J. M. 2001. Understanding the evolution of restriction-modification systems: clues from sequence and structure comparisons. Acta Biochim. Pol. 48:935-967.
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 935-967
    • Bujnicki, J.M.1
  • 11
    • 0033571544 scopus 로고    scopus 로고
    • Molecular evolution of DNA(cytosine-N4) methyltransferases: Evidence for their potyphyletic origin
    • Bujnicki, J. M., and M. Radlinska. 1999. Molecular evolution of DNA(cytosine-N4) methyltransferases: evidence for their potyphyletic origin. Nucleic Acids Res. 22:4501-4509.
    • (1999) Nucleic Acids Res. , vol.22 , pp. 4501-4509
    • Bujnicki, J.M.1    Radlinska, M.2
  • 12
    • 0018956590 scopus 로고
    • Analysis of gene control signals by DNA fusion and cloning in Escherichia coli
    • Casadaban, M. J., and S. N. Cohen. 1980. Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J. Mol. Biol. 138:179-207.
    • (1980) J. Mol. Biol. , vol.138 , pp. 179-207
    • Casadaban, M.J.1    Cohen, S.N.2
  • 13
    • 0023816268 scopus 로고
    • Cloning and sequencing the HinfI restriction and modification genes
    • Chandrasegaran, S., K. D. Lunnen, H. O. Smith, and G. G. Wilson. 1988. Cloning and sequencing the HinfI restriction and modification genes. Gene 70:387-392.
    • (1988) Gene , vol.70 , pp. 387-392
    • Chandrasegaran, S.1    Lunnen, K.D.2    Smith, H.O.3    Wilson, G.G.4
  • 14
    • 0037628090 scopus 로고
    • Amino acid sequence homologies among twenty-five restriction endonucleases and methylases
    • R. H. Sarma and M. H. Sarma (ed.). Adenine Press, New York, N.Y.
    • Chandrasegaran, S., and H. O. Smith. 1988. Amino acid sequence homologies among twenty-five restriction endonucleases and methylases, p. 149-156. In R. H. Sarma and M. H. Sarma (ed.), Structure & expression, vol. 1. From proteins to ribosomes. Adenine Press, New York, N.Y.
    • (1988) Structure & Expression, Vol. 1. From Proteins to Ribosomes , vol.1 , pp. 149-156
    • Chandrasegaran, S.1    Smith, H.O.2
  • 15
    • 0017741879 scopus 로고
    • In vivo site specific genetic recombination promoted by the EcoRI restriction endonuclease
    • Chang, S., and S. N. Cohen. 1977. In vivo site specific genetic recombination promoted by the EcoRI restriction endonuclease. Proc. Natl. Acad. Sci. USA 74:4811-4815.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4811-4815
    • Chang, S.1    Cohen, S.N.2
  • 16
    • 0025348395 scopus 로고
    • Suppression of the negative effect of minor arginine codons on gene expression: Preferential usage of minor codons within the first 25 codons of the Escherichia coli genes
    • Chen, G. F. T., and M. Inouye. 1990. Suppression of the negative effect of minor arginine codons on gene expression: preferential usage of minor codons within the first 25 codons of the Escherichia coli genes. Nucleic Acids Res. 18:1465-1473.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1465-1473
    • Chen, G.F.T.1    Inouye, M.2
  • 17
    • 0028584414 scopus 로고
    • Determination of the optimal aligned spacing between the Shine-Dalgarno sequence and the translation initiation codon of Escherichia coli mRNAs
    • Chen, H., M. Bjerknes, R. Kumar, and E. Jay. 1994. Determination of the optimal aligned spacing between the Shine-Dalgarno sequence and the translation initiation codon of Escherichia coli mRNAs. Nucleic Acids Res. 22:4953-4957.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4953-4957
    • Chen, H.1    Bjerknes, M.2    Kumar, R.3    Jay, E.4
  • 18
  • 20
    • 0035868627 scopus 로고    scopus 로고
    • Isolation and characterization of type IIS restriction endonuclease from Neisseria cuniculi ATCC 14668
    • Furmanek, B., K. Gromek, M. Sektas, and T. Kaczorowski. 2001. Isolation and characterization of type IIS restriction endonuclease from Neisseria cuniculi ATCC 14668. FEMS Microbiol. Lett. 196:171-176.
    • (2001) FEMS Microbiol. Lett. , vol.196 , pp. 171-176
    • Furmanek, B.1    Gromek, K.2    Sektas, M.3    Kaczorowski, T.4
  • 21
    • 0036076817 scopus 로고    scopus 로고
    • Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases
    • Fuxreiter, M., and I. Simon. 2002. Protein stability indicates divergent evolution of PD-(D/E)XK type II restriction endonucleases. Protein Sci. 11:1978-1983.
    • (2002) Protein Sci. , vol.11 , pp. 1978-1983
    • Fuxreiter, M.1    Simon, I.2
  • 23
    • 0028907431 scopus 로고
    • Consecutive low-usage leucine codons block translation only when near the 5′ end of a message in Escherichia coli
    • Goldman, E., A. H. Rosenberg, G. Zubay, and F. W. Studier. 1995. Consecutive low-usage leucine codons block translation only when near the 5′ end of a message in Escherichia coli. J. Mol. Biol. 245:467-473.
    • (1995) J. Mol. Biol. , vol.245 , pp. 467-473
    • Goldman, E.1    Rosenberg, A.H.2    Zubay, G.3    Studier, F.W.4
  • 24
    • 0030612472 scopus 로고    scopus 로고
    • Structure of PvuII DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
    • Gong, W., M. O'Gara, R. M. Blumenthal, and X. Cheng. 1997. Structure of PvuII DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment. Nucleic Acids Res. 25:2702-2715.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2702-2715
    • Gong, W.1    O'Gara, M.2    Blumenthal, R.M.3    Cheng, X.4
  • 25
    • 0023724367 scopus 로고
    • Activity of DNA modification and restriction enzymes in KGB, a potassium glutamate buffer
    • Hanish, J., and M. McClelland, 1988. Activity of DNA modification and restriction enzymes in KGB, a potassium glutamate buffer. Gene Anal. Techn. 5:105-107.
    • (1988) Gene Anal. Techn. , vol.5 , pp. 105-107
    • Hanish, J.1    McClelland, M.2
  • 26
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 27
    • 0033514996 scopus 로고    scopus 로고
    • Evolutionary relationships among diverse bacteriophages and prophages: All the world's a phage
    • Hendrix, R. W., M. C. M. Smith, R. N. Burns, M. E. Ford, and G. F. Hatfull. 1999. Evolutionary relationships among diverse bacteriophages and prophages: all the world's a phage. Proc. Natl. Acad. Sci. USA 96:2192-2197.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2192-2197
    • Hendrix, R.W.1    Smith, M.C.M.2    Burns, R.N.3    Ford, M.E.4    Hatfull, G.F.5
  • 28
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven, J., and R. Dernick. 1985. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 6:103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 29
    • 0025738784 scopus 로고
    • In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage
    • Hill, C., L. A. Miller, and T. R. Klaenhammer. 1991. In vivo genetic exchange of a functional domain from a type II A methylase between lactococcal plasmid pTR2030 and a virulent bacteriophage. J. Bacteriol. 173:4363-4370.
    • (1991) J. Bacteriol. , vol.173 , pp. 4363-4370
    • Hill, C.1    Miller, L.A.2    Klaenhammer, T.R.3
  • 30
    • 0032506110 scopus 로고    scopus 로고
    • Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases
    • Horton, N. C., K. J. Newberry, and J. J. Perona. 1998. Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases. Proc. Natl. Acad. Sci. USA 95:13489-13494.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13489-13494
    • Horton, N.C.1    Newberry, K.J.2    Perona, J.J.3
  • 31
    • 0029940857 scopus 로고    scopus 로고
    • Horizontal gene transfer contributes to the wide distribution and evolution of type II restriction-modification systems
    • Jeltsch, A., and A. Pingoud. 1996. Horizontal gene transfer contributes to the wide distribution and evolution of type II restriction-modification systems. J. Mol. Evol. 42:91-96.
    • (1996) J. Mol. Evol. , vol.42 , pp. 91-96
    • Jeltsch, A.1    Pingoud, A.2
  • 32
    • 0024450479 scopus 로고
    • Purification and characterization of the FokI restriction endonuclease
    • Kaczorowski, T., P. Skowron, and A. J. Podhajska. 1989. Purification and characterization of the FokI restriction endonuclease. Gene 80:209-216.
    • (1989) Gene , vol.80 , pp. 209-216
    • Kaczorowski, T.1    Skowron, P.2    Podhajska, A.J.3
  • 33
    • 0030125189 scopus 로고    scopus 로고
    • Rapid removal of unincorporated label and proteins from DNA sequencing reactions
    • Kaczorowski, T., and M. Sektas. 1996. Rapid removal of unincorporated label and proteins from DNA sequencing reactions. Mol. Biotechnol. 5:177-181.
    • (1996) Mol. Biotechnol. , vol.5 , pp. 177-181
    • Kaczorowski, T.1    Sektas, M.2
  • 34
    • 0027196087 scopus 로고
    • An improvement in electrophoretic transfer of DNA from a gel to DEAE-cellulose membrane
    • Kaczorowski, T., M. Sektas, and B. Furmanek. 1993. An improvement in electrophoretic transfer of DNA from a gel to DEAE-cellulose membrane. BioTechniques 14:900.
    • (1993) BioTechniques , vol.14 , pp. 900
    • Kaczorowski, T.1    Sektas, M.2    Furmanek, B.3
  • 35
    • 0033382901 scopus 로고    scopus 로고
    • The FokI methyltransferase from Flavobacterium okeanokoites: Purification and characterization of the enzyme and its truncated derivatives
    • Kaczorowski, T., M. Sektas, P. Skowron, and A. J. Podhajska. 1999. The FokI methyltransferase from Flavobacterium okeanokoites: purification and characterization of the enzyme and its truncated derivatives. Mol. Biotechnol. 13:1-15.
    • (1999) Mol. Biotechnol. , vol.13 , pp. 1-15
    • Kaczorowski, T.1    Sektas, M.2    Skowron, P.3    Podhajska, A.J.4
  • 36
    • 0032569967 scopus 로고    scopus 로고
    • Genomic DNA sequencing by SPEL-6 primer walking using hexamer ligation
    • Kaczorowski, T., and W. Szybalski. 1998. Genomic DNA sequencing by SPEL-6 primer walking using hexamer ligation. Gene 223:83-91.
    • (1998) Gene , vol.223 , pp. 83-91
    • Kaczorowski, T.1    Szybalski, W.2
  • 37
    • 0031720281 scopus 로고    scopus 로고
    • Codon usages in different gene classes of the Escherichia coli genome
    • Karlin, S., J. Mrazek, and A. M. Campbell. 1998. Codon usages in different gene classes of the Escherichia coli genome. Mol. Microbiol. 29:1341-1355.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1341-1355
    • Karlin, S.1    Mrazek, J.2    Campbell, A.M.3
  • 38
    • 0024811702 scopus 로고
    • Purification, cloning and sequence analysis of RsrI DNA methyltransferase: Lack of homology between two enzymes, RsrI and EcoRI, that methylate the same nucleotide in identical recognition sequences
    • Kaszubska, W., C. Aiken, C. D. O'Connor, and R. I. Gumport. 1989. Purification, cloning and sequence analysis of RsrI DNA methyltransferase: lack of homology between two enzymes, RsrI and EcoRI, that methylate the same nucleotide in identical recognition sequences. Nucleic Acids Res. 17:10403-10425.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10403-10425
    • Kaszubska, W.1    Aiken, C.2    O'Connor, C.D.3    Gumport, R.I.4
  • 40
    • 0024456703 scopus 로고
    • Overproduction and crystallization of FokI restriction endonuclease
    • Kita, K., H. Kotani, N. Hiraoka, T. Nakamura, and K. Yonaha. 1989. Overproduction and crystallization of FokI restriction endonuclease. Nucleic Acids Res. 17:8741-8753.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8741-8753
    • Kita, K.1    Kotani, H.2    Hiraoka, N.3    Nakamura, T.4    Yonaha, K.5
  • 42
    • 0344898766 scopus 로고
    • Evidence for use of rare codons in the dnaG gene and other regulatory genes of Escherichia coli
    • Konigsberg, W., and N. G. Godson. 1983. Evidence for use of rare codons in the dnaG gene and other regulatory genes of Escherichia coli. Proc. Natl. Acad. Sci. USA 80:687-691.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 687-691
    • Konigsberg, W.1    Godson, N.G.2
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0031596401 scopus 로고    scopus 로고
    • Sequence comparison of the EcoHK31I and EaeI restriction-modification systems suggests an intergenic transfer of genetic material
    • Lee, K. F., P. C. Shaw, S. J. Picone, G. G. Wilson, and K. D. Lunnen. 1998. Sequence comparison of the EcoHK31I and EaeI restriction-modification systems suggests an intergenic transfer of genetic material. Biol. Chem. 379:437-441.
    • (1998) Biol. Chem. , vol.379 , pp. 437-441
    • Lee, K.F.1    Shaw, P.C.2    Picone, S.J.3    Wilson, G.G.4    Lunnen, K.D.5
  • 45
    • 0025248655 scopus 로고
    • Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication
    • Liberek, K., J. Osipiuk, M. Zylicz, D. Ang, J. Skórko, and C. Georgopoulos. 1990. Physical interactions between bacteriophage and Escherichia coli proteins required for initiation of lambda DNA replication. J. Biol. Chem. 265:3022-3029.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3022-3029
    • Liberek, K.1    Osipiuk, J.2    Zylicz, M.3    Ang, D.4    Skórko, J.5    Georgopoulos, C.6
  • 46
    • 0027230594 scopus 로고
    • Compilation of E. coli mRNA promoter sequences
    • Lisser, S., and H. Margalit. 1993. Compilation of E. coli mRNA promoter sequences. Nucleic Acids Res. 21:1507-1516.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 1507-1516
    • Lisser, S.1    Margalit, H.2
  • 47
    • 0028273930 scopus 로고
    • Cloning and analysis of translational control for genes encoding the Cfr9I restriction-modification system
    • Lubys, A., S. Menkevièius, A. Timinskas, V. Butkus, and A. Janulaitis. 1994. Cloning and analysis of translational control for genes encoding the Cfr9I restriction-modification system. Gene 141:85-89.
    • (1994) Gene , vol.141 , pp. 85-89
    • Lubys, A.1    Menkevièius, S.2    Timinskas, A.3    Butkus, V.4    Janulaitis, A.5
  • 48
    • 0014429667 scopus 로고
    • Magnesium and the growth of Escherichia coli
    • Lusk, J. E., J. P. Williams, and E. P. Kennedy. 1968. Magnesium and the growth of Escherichia coli. J. Biol. Chem. 243:2618-2624.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2618-2624
    • Lusk, J.E.1    Williams, J.P.2    Kennedy, E.P.3
  • 49
    • 0031596404 scopus 로고    scopus 로고
    • Characterization of LlaCI, a new restriction-modification system from Lactococcus lactis subsp. cremoris W15
    • Madsen, A., and J. Josephsen. 1998. Characterization of LlaCI, a new restriction-modification system from Lactococcus lactis subsp. cremoris W15. Biol. Chem. 379:443-449.
    • (1998) Biol. Chem. , vol.379 , pp. 443-449
    • Madsen, A.1    Josephsen, J.2
  • 50
    • 0028841409 scopus 로고
    • Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes
    • Malone, T., R. M. Blumenthal, and X. Cheng. 1995. Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes. J. Mol. Biol. 253:618-632.
    • (1995) J. Mol. Biol. , vol.253 , pp. 618-632
    • Malone, T.1    Blumenthal, R.M.2    Cheng, X.3
  • 51
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: The S-adenosylmethionine-dependent methyltransferase fold
    • Martin, J. L., and F. M. McMillan. 2002. SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr. Opin. Struct. Biol. 12:783-793.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 52
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory. Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics, p. 352-355. Cold Spring Harbor Laboratory. Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.H.1
  • 53
    • 0021718053 scopus 로고
    • Isolation of restriction enzyme EcoVIII, an isoschizomer of HindIII, produced by Escherichia coli E1585-68
    • Mise, K., and K. Nakajima. 1984. Isolation of restriction enzyme EcoVIII, an isoschizomer of HindIII, produced by Escherichia coli E1585-68. Gene 30:79-85.
    • (1984) Gene , vol.30 , pp. 79-85
    • Mise, K.1    Nakajima, K.2
  • 54
    • 0034780998 scopus 로고    scopus 로고
    • Characterization of pEC156, a ColE1-type plasmid from Escherichia coli E1585-68 that carries genes of the EcoVIII restriction-modification system
    • Mruk, I., M. Sektas, and T. Kaczorowski. 2001. Characterization of pEC156, a ColE1-type plasmid from Escherichia coli E1585-68 that carries genes of the EcoVIII restriction-modification system. Plasmid 46:128-139.
    • (2001) Plasmid , vol.46 , pp. 128-139
    • Mruk, I.1    Sektas, M.2    Kaczorowski, T.3
  • 55
    • 0036226256 scopus 로고    scopus 로고
    • Mobility of a restriction-modification system revealed by its genetic contexts in three hosts
    • Naderer, M., J. R. Brust, D. Knowle, and R. M. Blumenthal. 2002. Mobility of a restriction-modification system revealed by its genetic contexts in three hosts. J. Bacteriol. 184:2411-2419.
    • (2002) J. Bacteriol. , vol.184 , pp. 2411-2419
    • Naderer, M.1    Brust, J.R.2    Knowle, D.3    Blumenthal, R.M.4
  • 57
    • 0035883723 scopus 로고    scopus 로고
    • Structure and function of type II restriction endonucleases
    • Pingoud, A., and A. Jeltsch. 2001. Structure and function of type II restriction endonucleases. Nucleic Acids Res. 29:3705-3727.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3705-3727
    • Pingoud, A.1    Jeltsch, A.2
  • 59
    • 0023727317 scopus 로고
    • A simple method for locating methylated bases in DNA, as applied to detect asymmetric methylation by M · FokI
    • Pósfai, G., and W. Szybalski. 1988. A simple method for locating methylated bases in DNA, as applied to detect asymmetric methylation by M · FokI. Gene 69:147-151.
    • (1988) Gene , vol.69 , pp. 147-151
    • Pósfai, G.1    Szybalski, W.2
  • 61
    • 0035175516 scopus 로고    scopus 로고
    • REBASE-restriction enzymes and methylases
    • Roberts, R. J., and D. Macelis. 2001. REBASE-restriction enzymes and methylases. Nucleic Acids Res. 29:268-269.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 268-269
    • Roberts, R.J.1    Macelis, D.2
  • 63
    • 0036606915 scopus 로고    scopus 로고
    • Base composition bias might result from competition for metabolic resources
    • Rocha, E. P. C., and A. Danchin. 2002. Base composition bias might result from competition for metabolic resources. Trends Genet. 18:291-294.
    • (2002) Trends Genet. , vol.18 , pp. 291-294
    • Rocha, E.P.C.1    Danchin, A.2
  • 64
    • 0027513392 scopus 로고
    • Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system
    • Rosenberg, A. H., E. Goldman, J. J. Dunn, F. W. Studier, and G. Zubay. 1993. Effects of consecutive AGG codons on translation in Escherichia coli, demonstrated with a versatile codon test system. J. Bacteriol. 175:716-722.
    • (1993) J. Bacteriol. , vol.175 , pp. 716-722
    • Rosenberg, A.H.1    Goldman, E.2    Dunn, J.J.3    Studier, F.W.4    Zubay, G.5
  • 65
    • 0015759308 scopus 로고
    • DNA methylases of Haemophilus influenzae Rd. I. Purification and properties
    • Roy, P. H., and H. O. Smith. 1973. DNA methylases of Haemophilus influenzae Rd. I. Purification and properties. J. Mol. Biol. 81:427-444.
    • (1973) J. Mol. Biol. , vol.81 , pp. 427-444
    • Roy, P.H.1    Smith, H.O.2
  • 69
    • 0021280391 scopus 로고
    • An enzyme that removes clathrin coats: Purification of an uncoating ATPase
    • Schlossman, D. M., S. L. Schmid, W. A. Brael, and J. E. Rothman. 1984. An enzyme that removes clathrin coats: purification of an uncoating ATPase. J. Cell Biol. 99:723-733.
    • (1984) J. Cell Biol. , vol.99 , pp. 723-733
    • Schlossman, D.M.1    Schmid, S.L.2    Brael, W.A.3    Rothman, J.E.4
  • 70
    • 0025088762 scopus 로고
    • Cloning, expression and characterization of the Sau3AI restriction and modification genes in Staphylococcus carnosus TM300
    • Seeber, S., C. Kessler, and F. Götz. 1990. Cloning, expression and characterization of the Sau3AI restriction and modification genes in Staphylococcus carnosus TM300. Gene 94:37-43.
    • (1990) Gene , vol.94 , pp. 37-43
    • Seeber, S.1    Kessler, C.2    Götz, F.3
  • 71
    • 0026564724 scopus 로고
    • Purification and properties of the MboII, a class-IIS restriction endonuclease
    • Sektas, M., T. Kaczorowski, and A. J. Podhajska. 1992. Purification and properties of the MboII, a class-IIS restriction endonuclease. Nucleic Acids Res. 20:433-438.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 433-438
    • Sektas, M.1    Kaczorowski, T.2    Podhajska, A.J.3
  • 72
    • 0023650543 scopus 로고
    • The codon adaptation index - A measure of directional synonymous codon usage bias, and its potential applications
    • Sharp, P. M., and W. H. Li. 1987. The codon adaptation index - a measure of directional synonymous codon usage bias, and its potential applications. Nucleic Acids Res. 15:1281-1295.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 1281-1295
    • Sharp, P.M.1    Li, W.H.2
  • 73
    • 0027411243 scopus 로고
    • Heteroduplex strand-specificity in restriction-stimulated recombination by the RecE pathway of Escherichia coli
    • Silberstein, Z., M. Shalit, and A. Cohen. 1993. Heteroduplex strand-specificity in restriction-stimulated recombination by the RecE pathway of Escherichia coli. Genetics 133:439-448.
    • (1993) Genetics , vol.133 , pp. 439-448
    • Silberstein, Z.1    Shalit, M.2    Cohen, A.3
  • 74
    • 0023255472 scopus 로고
    • Improved single and multicopy lac-based cloning vectors for protein and operon fusions
    • Simons, R. W., F. Houman, and N. Kleckner. 1987. Improved single and multicopy lac-based cloning vectors for protein and operon fusions. Gene 53:85-96.
    • (1987) Gene , vol.53 , pp. 85-96
    • Simons, R.W.1    Houman, F.2    Kleckner, N.3
  • 75
    • 0032486108 scopus 로고    scopus 로고
    • Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues
    • Skirgaila, R., S. Grazulis, D. Bozic, R. Huber, and V. Siksnys. 1998. Structure-based redesign of the catalytic/metal binding site of Cfr10I restriction endonuclease reveals importance of spatial rather than sequence conservation of active centre residues. J. Mol. Biol. 279:473-481.
    • (1998) J. Mol. Biol. , vol.279 , pp. 473-481
    • Skirgaila, R.1    Grazulis, S.2    Bozic, D.3    Huber, R.4    Siksnys, V.5
  • 76
    • 0014966125 scopus 로고
    • A restriction enzyme from Haemophilus influenzae. I. Purification and general properties
    • Smith, H. O., and K. W. Wilcox. 1970. A restriction enzyme from Haemophilus influenzae. I. Purification and general properties. J. Mol. Biol. 51:379-391.
    • (1970) J. Mol. Biol. , vol.51 , pp. 379-391
    • Smith, H.O.1    Wilcox, K.W.2
  • 77
    • 0000516715 scopus 로고
    • Translation of the sequence AGG-AGG yields 50% ribosomal frameshift
    • Spanjaard, R. A., and J. van Duin. 1988. Translation of the sequence AGG-AGG yields 50% ribosomal frameshift. Proc. Natl. Acad. Sci. USA 85:7967-7971.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7967-7971
    • Spanjaard, R.A.1    Van Duin, J.2
  • 78
    • 0020609129 scopus 로고
    • Activation of Chi, a recombinator, by the action of an endonuclease at a distant site
    • Stahl, M. M., I. Kobayashi, F. W. Stahl, and S. K. Huntington. 1983. Activation of Chi, a recombinator, by the action of an endonuclease at a distant site. Proc. Natl. Acad. Sci. USA 80:2310-2313.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2310-2313
    • Stahl, M.M.1    Kobayashi, I.2    Stahl, F.W.3    Huntington, S.K.4
  • 79
    • 0024851310 scopus 로고
    • Comparison of the nucleotide and amino acid sequences of the RsrI and EcoRI restriction endonucleases
    • Stephenson, F. H., B. T. Ballard, H. W. Boyer, J. M. Rosenberg, and P. J. Greene. 1989. Comparison of the nucleotide and amino acid sequences of the RsrI and EcoRI restriction endonucleases. Gene 85:1-13.
    • (1989) Gene , vol.85 , pp. 1-13
    • Stephenson, F.H.1    Ballard, B.T.2    Boyer, H.W.3    Rosenberg, J.M.4    Greene, P.J.5
  • 80
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 81
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 82
    • 0024509697 scopus 로고
    • Nucleotide sequence and genetic organization of the NgoPII restriction-modification system of Neisseria gonorrhoeae
    • Sullivan, K. M., and J. R. Saunders. 1989. Nucleotide sequence and genetic organization of the NgoPII restriction-modification system of Neisseria gonorrhoeae. Mol. Gen. Genet. 216:380-387.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 380-387
    • Sullivan, K.M.1    Saunders, J.R.2
  • 83
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 84
    • 0026087311 scopus 로고
    • A family of regulatory genes associated with type II restriction-modification systems
    • Tao, T., J. C. Bourne, and R. M. Blumenthal. 1991. A family of regulatory genes associated with type II restriction-modification systems. J. Bacteriol. 173:1367-1375.
    • (1991) J. Bacteriol. , vol.173 , pp. 1367-1375
    • Tao, T.1    Bourne, J.C.2    Blumenthal, R.M.3
  • 85
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 86
    • 0028172810 scopus 로고
    • Five-stranded β-sheet sandwiched with two α-helices: A structural link between restriction endonucleases EcoRI and EcoRV
    • Venclovas, C., A. Timinskas, and V. Siksnys. 1994. Five-stranded β-sheet sandwiched with two α-helices: a structural link between restriction endonucleases EcoRI and EcoRV. Proteins 20:279-282.
    • (1994) Proteins , vol.20 , pp. 279-282
    • Venclovas, C.1    Timinskas, A.2    Siksnys, V.3
  • 87
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K., and M. Osborn. 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244:4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 88
    • 0027023842 scopus 로고
    • Amino acid sequence arrangements of DNA methyltransferases
    • Wilson, G. G. 1992. Amino acid sequence arrangements of DNA methyltransferases. Methods Enzymol. 216:259-279.
    • (1992) Methods Enzymol. , vol.216 , pp. 259-279
    • Wilson, G.G.1
  • 89
    • 0002241426 scopus 로고
    • Structure and function of restriction endonucleases
    • Winkler, F. 1992. Structure and function of restriction endonucleases. Curr. Opin. Struct. Biol. 2:93-99.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 93-99
    • Winkler, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.