메뉴 건너뛰기




Volumn 223, Issue 1-2, 1998, Pages 293-302

Two intertwined methylation activities of the MmeI restriction- modification class-IIS system from Methylophilus methylotrophus

Author keywords

Endonucleases; Enzyme purification; Methylation; Methyltransferases; S adenosyl L methionine; Sinefungin

Indexed keywords

6 N METHYLADENINE; BACTERIAL DNA; CALCIUM ION; COBALT; DIVALENT CATION; MAGNESIUM ION; RESTRICTION ENDONUCLEASE; S ADENOSYLMETHIONINE; SINEFUNGIN; ZINC ION;

EID: 0032570040     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00450-8     Document Type: Conference Paper
Times cited : (18)

References (36)
  • 1
    • 0001246049 scopus 로고
    • Derivations and genotypes of some mutant derivatives of Escherichia coli K-12
    • In: Neidhardt, F.C. et al., (Eds.), American Society for Microbiology, Washington, DC, pp.
    • Bachmann, B.J., 1987. Derivations and genotypes of some mutant derivatives of Escherichia coli K-12. In: Neidhardt, F.C. et al., (Eds.), Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology. American Society for Microbiology, Washington, DC, pp. 1190-1219.
    • (1987) Escherichia Coli and Salmonella Typhimurium, Cellular and Molecular Biology , pp. 1190-1219
    • Bachmann, B.J.1
  • 3
    • 0025031980 scopus 로고
    • The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli
    • Bergerat A., Guschlbauer W. The double role of methyl donor and allosteric effector of S-adenosyl-methionine for Dam methylase of E. coli. Nucleic Acids Res. 18:1990;4369-4375.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4369-4375
    • Bergerat, A.1    Guschlbauer, W.2
  • 5
    • 0025982162 scopus 로고
    • Cloning and characterization of the MboII restriction-modification system
    • Bocklage H., Heeger K., Müller-Hill B. Cloning and characterization of the MboII restriction-modification system. Nucleic Acids Res. 19:1991;1007-1013.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1007-1013
    • Bocklage, H.1    Heeger, K.2    Müller-Hill, B.3
  • 7
    • 0018407483 scopus 로고
    • Sinefungin, a potent inhibitor of S-adenosylmethionine: Protein O-methyltransferase
    • Borchardt R.T., Eiden L.E., Wu B., Rutledge C.O. Sinefungin, a potent inhibitor of S-adenosylmethionine: protein O-methyltransferase. Biochem. Biophys. Res. Commun. 89:1979;919-924.
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 919-924
    • Borchardt, R.T.1    Eiden, L.E.2    Wu, B.3    Rutledge, C.O.4
  • 8
    • 0023046881 scopus 로고
    • Isolation and computer-aided characterization of MmeI, a type II restriction endonuclease from Methylophilus methylotrophus
    • Boyd A.C., Charles I.G., Keyte J.W., Brammar W.J. Isolation and computer-aided characterization of MmeI, a type II restriction endonuclease from Methylophilus methylotrophus. Nucleic Acids Res. 14:1986;5255-5274.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 5255-5274
    • Boyd, A.C.1    Charles, I.G.2    Keyte, J.W.3    Brammar, W.J.4
  • 9
    • 0026647626 scopus 로고
    • Sequence-specific DNA binding by the MspI DNA methyltransferase
    • Dubey A.K., Roberts R.J. Sequence-specific DNA binding by the MspI DNA methyltransferase. Nucleic Acids Res. 20:1992;3167-3173.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3167-3173
    • Dubey, A.K.1    Roberts, R.J.2
  • 10
    • 0022589997 scopus 로고
    • Binding of the EcoRII methylase to azacytosine-containing DNA
    • Friedman S. Binding of the EcoRII methylase to azacytosine-containing DNA. Nucleic Acids Res. 14:1986;4543-4556.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4543-4556
    • Friedman, S.1
  • 11
    • 0018124538 scopus 로고
    • Inhibition of methyltransferases by some new analogs of S-adenosylhomocysteine
    • Fuller R.W., Nagarajan R. Inhibition of methyltransferases by some new analogs of S-adenosylhomocysteine. Biochem. Pharmacol. 27:1978;1981-1983.
    • (1978) Biochem. Pharmacol. , vol.27 , pp. 1981-1983
    • Fuller, R.W.1    Nagarajan, R.2
  • 12
    • 0016807734 scopus 로고
    • The role of S-adenosylmethionine in the cleavage of deoxyribonucleic acid by the restriction endonuclease from Escherichia coli K
    • Hadi S.M., Bickle T.A., Yuan R. The role of S-adenosylmethionine in the cleavage of deoxyribonucleic acid by the restriction endonuclease from Escherichia coli K. J. Biol. Chem. 250:1975;4159-4163.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4159-4163
    • Hadi, S.M.1    Bickle, T.A.2    Yuan, R.3
  • 13
    • 0023724367 scopus 로고
    • Activity of DNA modification and restriction enzymes in KGB, a potassium glutamate buffer
    • Hanish J., McClelland M. Activity of DNA modification and restriction enzymes in KGB, a potassium glutamate buffer. Gene Anal. Techn. 5:1988;105-107.
    • (1988) Gene Anal. Techn. , vol.5 , pp. 105-107
    • Hanish, J.1    McClelland, M.2
  • 14
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gel and the mechanism of silver staining
    • Heukeshoven J., Dernick R. Simplified method for silver staining of proteins in polyacrylamide gel and the mechanism of silver staining. Electrophoresis. 6:1985;103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 15
    • 0026613987 scopus 로고
    • Purification and properties of the Eco57I restriction and methylase-prototypes of a new class (type IV)
    • Janulaitis A., Petrušytė M., Maneliene Z., Klimasauskas S., Butkus V. Purification and properties of the Eco57I restriction and methylase-prototypes of a new class (type IV). Nucleic Acids Res. 20:1992;6043-6049.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6043-6049
    • Janulaitis, A.1    Petrušyte, M.2    Maneliene, Z.3    Klimasauskas, S.4    Butkus, V.5
  • 16
    • 0026468485 scopus 로고
    • Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes
    • Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V. Cloning and sequence analysis of the genes coding for Eco57I type IV restriction-modification enzymes. Nucleic Acids Res. 20:1992;6051-6056.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 6051-6056
    • Janulaitis, A.1    Vaisvila, R.2    Timinskas, A.3    Klimasauskas, S.4    Butkus, V.5
  • 18
    • 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., Aiken C.R., O'Connor C.D., Gumport R.I. 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. 17:1989;10403-10425.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10403-10425
    • Kaszubska, W.1    Aiken, C.R.2    O'Connor, C.D.3    Gumport, R.I.4
  • 19
    • 0026698903 scopus 로고
    • Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli
    • Kaszubska W., Webb H.K., Gumport R.I. Purification and characterization of the M.RsrI DNA methyltransferase from Escherichia coli. Gene. 118:1992;5-11.
    • (1992) Gene , vol.118 , pp. 5-11
    • Kaszubska, W.1    Webb, H.K.2    Gumport, R.I.3
  • 20
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0024440974 scopus 로고
    • Nucleotide sequence of the FokI restriction-modification system: Separate strand-specificity domains in the methyltransferase
    • Looney M.C., Moran L.S., Jack W.E., Feehery G.R., Benner J.S., Slatko B.E., Wilson G.G. Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase. Gene. 80:1989;193-208.
    • (1989) Gene , vol.80 , pp. 193-208
    • Looney, M.C.1    Moran, L.S.2    Jack, W.E.3    Feehery, G.R.4    Benner, J.S.5    Slatko, B.E.6    Wilson, G.G.7
  • 23
    • 0027117638 scopus 로고
    • Bce83I, a restriction endonuclease from Bacillus cereus 83 which recognizes novel nonpalindromic sequence 5′-CTTGAG-3′ and is stimulated by S-adenosylmethionine
    • Matvienko N.N., Kramarov M.V., Ivanov L.Yu., Matvienko N. Bce83I, a restriction endonuclease from Bacillus cereus 83 which recognizes novel nonpalindromic sequence 5′-CTTGAG-3′ and is stimulated by S-adenosylmethionine. Nucleic Acids Res. 20:1992;1803.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1803
    • Matvienko, N.N.1    Kramarov, M.V.2    Ivanov, L.yu.3    Matvienko, N.4
  • 25
    • 0027453423 scopus 로고
    • DNA recognition by the EcoK methyltransferase. The influence of DNA methylation and the cofactor S-adenosyl-L-metionine
    • Powell L.M., Dryden D.T., Willcock D.F., Pain R.H., Murray N.E. DNA recognition by the EcoK methyltransferase. The influence of DNA methylation and the cofactor S-adenosyl-L-metionine. J. Mol. Biol. 234:1993;60-71.
    • (1993) J. Mol. Biol. , vol.234 , pp. 60-71
    • Powell, L.M.1    Dryden, D.T.2    Willcock, D.F.3    Pain, R.H.4    Murray, N.E.5
  • 26
    • 0028955417 scopus 로고
    • S-adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase
    • Powell L.M., Murray N.E. S-adenosyl methionine alters the DNA contacts of the EcoKI methyltransferase. Nucleic Acids Res. 23:1995;967-974.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 967-974
    • Powell, L.M.1    Murray, N.E.2
  • 27
    • 0017899194 scopus 로고
    • Sinefungin, a potent inhibitor of virion mRNA (guanine-7-)-methyltransferase, mRNA(nucleoside-2′-)-methyltransferase, and viral multiplication
    • Pugh C.S.G., Borchardt R.T., Stone H.O. Sinefungin, a potent inhibitor of virion mRNA (guanine-7-)-methyltransferase, mRNA(nucleoside-2′-)-methyltransferase, and viral multiplication. J. Biol. Chem. 253:1978;4075-4077.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4075-4077
    • Pugh, C.S.G.1    Borchardt, R.T.2    Stone, H.O.3
  • 28
    • 0002598414 scopus 로고
    • Type II restriction endonucleases
    • In: Linn, S.M., Lloyd, R.S., Roberts, R.J. (Eds.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp.
    • Roberts, R.J., Halford, S.E., 1993. Type II restriction endonucleases. In: Linn, S.M., Lloyd, R.S., Roberts, R.J. (Eds.), Nucleases. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 35-87.
    • (1993) Nucleases , pp. 35-87
    • Roberts, R.J.1    Halford, S.E.2
  • 32
    • 0024322164 scopus 로고
    • Discrimination between the DNA sequences by the EcoRV restriction endonuclease
    • Taylor J.D., Halford S.E. Discrimination between the DNA sequences by the EcoRV restriction endonuclease. Biochemistry. 28:1989;6198-6207.
    • (1989) Biochemistry , vol.28 , pp. 6198-6207
    • Taylor, J.D.1    Halford, S.E.2
  • 33
    • 0025889005 scopus 로고
    • EcoRV restriction endonuclease binds all DNA sequences with equal affinity
    • Taylor J.D., Badcoe I.G., Clarke A.R., Halford S.E. EcoRV restriction endonuclease binds all DNA sequences with equal affinity. Biochemistry. 30:1991;8743-8753.
    • (1991) Biochemistry , vol.30 , pp. 8743-8753
    • Taylor, J.D.1    Badcoe, I.G.2    Clarke, A.R.3    Halford, S.E.4
  • 34
    • 0029066981 scopus 로고
    • MmeI, a class-IIS restriction endonuclease: Purification and characterization
    • Tucholski J., Skowron P.M., Podhajska A.J. MmeI, a class-IIS restriction endonuclease: purification and characterization. Gene. 157:1995;87-92.
    • (1995) Gene , vol.157 , pp. 87-92
    • Tucholski, J.1    Skowron, P.M.2    Podhajska, A.J.3
  • 36
    • 0026722915 scopus 로고
    • Characterization of steady state, single-turnover, and binding kinetics of the TaqI restriction endonuclease
    • Zebala J.A., Choi J., Barany F.J. Characterization of steady state, single-turnover, and binding kinetics of the TaqI restriction endonuclease. J. Biol. Chem. 267:1992;8097-8105.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8097-8105
    • Zebala, J.A.1    Choi, J.2    Barany, F.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.