메뉴 건너뛰기




Volumn 286, Issue 2, 1999, Pages 389-401

Mechanism-based inhibition of C5-cytosine DNA methyltransferases by 2-H pyrimidinone

Author keywords

DNA methyltransferase; Inhibitor; Methylation; Nucleotide analogue; Pyrimidinone

Indexed keywords

CYSTEINE; DNA METHYLTRANSFERASE; DOUBLE STRANDED DNA; GUANINE; N ETHYLMALEIMIDE; PYRIMIDINONE DERIVATIVE; SERINE; THREONINE; TYROSINE;

EID: 0033582720     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2491     Document Type: Article
Times cited : (67)

References (57)
  • 3
    • 0026575027 scopus 로고
    • The decomposition of 1-(β- D -ribofuranosyl)-1,2-dihydropyrimidin-2-one (Zebularine) in alkali: Mechanism and products
    • Barchi J. J., Musser S., Marquez V. E. The decomposition of 1-(β- D -ribofuranosyl)-1,2-dihydropyrimidin-2-one (Zebularine) in alkali: mechanism and products. J. Org. Chem. 57:1992;536-541.
    • (1992) J. Org. Chem. , vol.57 , pp. 536-541
    • Barchi, J.J.1    Musser, S.2    Marquez, V.E.3
  • 4
    • 0142052452 scopus 로고
    • Sulfonic and phosphonic acids formed by bisulfite and phosphite adduct formation with pyrimidinones
    • Benneche T., Strande P., Undheim K. Sulfonic and phosphonic acids formed by bisulfite and phosphite adduct formation with pyrimidinones. Acta Chem. Scand. sect. B. 41:1987;448-454.
    • (1987) Acta Chem. Scand. Sect. B , vol.41 , pp. 448-454
    • Benneche, T.1    Strande, P.2    Undheim, K.3
  • 7
    • 0029036377 scopus 로고
    • The catalytic mechanism and structure of thymidylate synthase
    • Carreras C. W., Santi D. V. The catalytic mechanism and structure of thymidylate synthase. Annu. Rev. Biochem. 64:1995;721-762.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 721-762
    • Carreras, C.W.1    Santi, D.V.2
  • 8
    • 0023708084 scopus 로고
    • -cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing
    • -cloning vectors. I. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing. Gene. 68:1988;139-149.
    • (1988) Gene , vol.68 , pp. 139-149
    • Chambers, S.P.1    Prior, S.E.2    Barstow, D.A.3    Minton, N.P.4
  • 9
    • 0026316928 scopus 로고
    • Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase
    • Chen L., MacMillan A. M., Chang W., Ezaz-Nikpay K., Lane W. S., Verdine G. L. Direct identification of the active-site nucleophile in a DNA (cytosine-5)-methyltransferase. Biochemistry. 30:1991;11018-11025.
    • (1991) Biochemistry , vol.30 , pp. 11018-11025
    • Chen, L.1    MacMillan, A.M.2    Chang, W.3    Ezaz-Nikpay, K.4    Lane, W.S.5    Verdine, G.L.6
  • 10
    • 0001726386 scopus 로고
    • Mutational separation of DNA binding from catalysis in a DNA cytosine methyltransferase
    • Chen L., MacMillan A. M., Verdine G. L. Mutational separation of DNA binding from catalysis in a DNA cytosine methyltransferase. J. Am. Chem. Soc. 115:1993;5318-5319.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 5318-5319
    • Chen, L.1    MacMillan, A.M.2    Verdine, G.L.3
  • 11
    • 0030585418 scopus 로고    scopus 로고
    • Finding a basis for flipping bases
    • Cheng X., Blumenthal R. M. Finding a basis for flipping bases. Structure. 4:1996;639-645.
    • (1996) Structure , vol.4 , pp. 639-645
    • Cheng, X.1    Blumenthal, R.M.2
  • 12
    • 0027338134 scopus 로고
    • Crystal structure of the HhaI DNA methyltransferase complexed with S -adenosyl- L -methionine
    • Cheng X., Kumar S., Posfai J., Pflugrath J. W., Roberts R. J. Crystal structure of the HhaI DNA methyltransferase complexed with S -adenosyl- L -methionine. Cell. 74:1993;299-307.
    • (1993) Cell , vol.74 , pp. 299-307
    • Cheng, X.1    Kumar, S.2    Posfai, J.3    Pflugrath, J.W.4    Roberts, R.J.5
  • 13
    • 0024378102 scopus 로고
    • Synthesis and properties of oligonucleotides containing 4-thiothymidine, 5-methyl-2-pyrimidinone-1-β- D (2′-deoxyriboside) and 2-thiothymidine
    • Connolly B. A., Newman P. C. Synthesis and properties of oligonucleotides containing 4-thiothymidine, 5-methyl-2-pyrimidinone-1-β- D (2′-deoxyriboside) and 2-thiothymidine. Nucl. Acids Res. 17:1989;4957-4974.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 4957-4974
    • Connolly, B.A.1    Newman, P.C.2
  • 14
    • 0021827694 scopus 로고
    • Synthesis and biological activities of 2-pyrimidinone nucleosides. 2. 5-Halo-2-pyrimidinone 2′-deoxyribonucleosides
    • Efange S. M., Alessi E. M., Shih H. C., Cheng Y-C., Bardos T. J. Synthesis and biological activities of 2-pyrimidinone nucleosides. 2. 5-Halo-2-pyrimidinone 2′-deoxyribonucleosides. J. Med. Chem. 28:1985;904-910.
    • (1985) J. Med. Chem. , vol.28 , pp. 904-910
    • Efange, S.M.1    Alessi, E.M.2    Shih, H.C.3    Cheng, Y.-C.4    Bardos, T.J.5
  • 15
    • 0027207804 scopus 로고
    • Effects of co-factor and deoxycytidine substituted oligonucleotides upon sequence-specific interactions between Msp I DNA methyltransferase and DNA
    • Ford K., Taylor C., Connolly B., Hornby D. P. Effects of co-factor and deoxycytidine substituted oligonucleotides upon sequence-specific interactions between Msp I DNA methyltransferase and DNA. J. Mol. Biol. 230:1993;779-786.
    • (1993) J. Mol. Biol. , vol.230 , pp. 779-786
    • Ford, K.1    Taylor, C.2    Connolly, B.3    Hornby, D.P.4
  • 16
    • 0021830501 scopus 로고
    • The irreversible binding of azacytosine-containing DNA fragments to bacterial DNA (cytosine-5)methyltransferases
    • Friedman S. The irreversible binding of azacytosine-containing DNA fragments to bacterial DNA (cytosine-5)methyltransferases. J. Biol. Chem. 260:1985;5698-5705.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5698-5705
    • Friedman, S.1
  • 17
    • 0028920604 scopus 로고
    • The mechanism of inhibition of DNA (cytosine-5-)-methyltransferases by 5-azacytosine is likely to involve methyl transfer to the inhibitor
    • Gabbara S., Bhagwat A. The mechanism of inhibition of DNA (cytosine-5-)-methyltransferases by 5-azacytosine is likely to involve methyl transfer to the inhibitor. Biochem. J. 307:1995;87-92.
    • (1995) Biochem. J. , vol.307 , pp. 87-92
    • Gabbara, S.1    Bhagwat, A.2
  • 18
    • 0029035664 scopus 로고
    • Cytosine methyltransferase from Escherichia coli in which active site cysteine is replaced with serine is partially active
    • Gabbara S., Sheluho D., Bhagwat A. Cytosine methyltransferase from Escherichia coli in which active site cysteine is replaced with serine is partially active. Biochemistry. 34:1995;8914-8923.
    • (1995) Biochemistry , vol.34 , pp. 8914-8923
    • Gabbara, S.1    Sheluho, D.2    Bhagwat, A.3
  • 19
  • 20
    • 0024602182 scopus 로고
    • The synthesis of 2-pyrimidinone nucleosides and their incorporation into oligodeoxynucleotides
    • Gildea B., McLaughlin L. W. The synthesis of 2-pyrimidinone nucleosides and their incorporation into oligodeoxynucleotides. Nucl. Acids Res. 17:1989;2261-2281.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 2261-2281
    • Gildea, B.1    McLaughlin, L.W.2
  • 21
    • 0021906585 scopus 로고
    • Preparation of analogues of cytosine and 2-pyrimidinone nucleosides and their effect on bacterial (Escherichia coli A19) cytidine aminohydrolyase
    • Holý A., Ludziša A., Votruba I., Šedivá K., Pischel H. Preparation of analogues of cytosine and 2-pyrimidinone nucleosides and their effect on bacterial (Escherichia coli A19) cytidine aminohydrolyase. Collect. Czech. Chem. Commun. 50:1985;393-417.
    • (1985) Collect. Czech. Chem. Commun. , vol.50 , pp. 393-417
    • Holý, A.1    Ludziša, A.2    Votruba, I.3    Šedivá, K.4    Pischel, H.5
  • 24
    • 0025062410 scopus 로고
    • Mild acid hydrolysis of 2-pyrimidinone containing DNA fragments generates apurinic/apyrimidinic sites
    • Iocono J. A., Gildea B., McLaughlin L. W. Mild acid hydrolysis of 2-pyrimidinone containing DNA fragments generates apurinic/apyrimidinic sites. Tetrahedron Letters. 31:1990;175-178.
    • (1990) Tetrahedron Letters , vol.31 , pp. 175-178
    • Iocono, J.A.1    Gildea, B.2    McLaughlin, L.W.3
  • 25
    • 0028990179 scopus 로고
    • M. Hha I binds tightly to substrates containing mismatches at the target base
    • Klimašauskas S., Roberts R. J. M. Hha I binds tightly to substrates containing mismatches at the target base. Nucl. Acids Res. 23:1995;1388-1395.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1388-1395
    • Klimašauskas, S.1    Roberts, R.J.2
  • 26
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimašauskas S., Kumar S., Roberts R. J., Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell. 76:1994;357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimašauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 27
    • 0025740912 scopus 로고
    • Improved site-directed mutagenesis method using PCR
    • Kuipers O. P., Boot H. J., de Vos W. M. Improved site-directed mutagenesis method using PCR. Nucl. Acids Res. 19:1991;4558.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 4558
    • Kuipers, O.P.1    Boot, H.J.2    De Vos, W.M.3
  • 28
    • 0030789978 scopus 로고    scopus 로고
    • DNA containing 4′-thio-2′-deoxycytidine inhibits methylation by Hha I methyltransferase
    • Kumar S., Horton J. R., Jones G. D., Walker R. T., Roberts R. J., Cheng X. DNA containing 4′-thio-2′-deoxycytidine inhibits methylation by Hha I methyltransferase. Nucl. Acids Res. 25:1997;2773-2783.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 2773-2783
    • Kumar, S.1    Horton, J.R.2    Jones, G.D.3    Walker, R.T.4    Roberts, R.J.5    Cheng, X.6
  • 29
    • 0029049872 scopus 로고
    • Methylation of slipped duplexes, snapbacks and cruciforms by human DNA(cytosine-5)methyltransferase
    • Laayoun A., Smith S. S. Methylation of slipped duplexes, snapbacks and cruciforms by human DNA(cytosine-5)methyltransferase. Nucl. Acids Res. 23:1995;1584-1589.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1584-1589
    • Laayoun, A.1    Smith, S.S.2
  • 30
    • 0028173199 scopus 로고
    • The response of M. Hpa II to heteroduplexes
    • Laayoun A., Baker D. J., Riley J., Smith S. S. The response of M. Hpa II to heteroduplexes. Gene. 150:1994;195-196.
    • (1994) Gene , vol.150 , pp. 195-196
    • Laayoun, A.1    Baker, D.J.2    Riley, J.3    Smith, S.S.4
  • 31
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt O., Grunert H.-P., Hahn U. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene. 96:1990;125-128.
    • (1990) Gene , vol.96 , pp. 125-128
    • Landt, O.1    Grunert, H.-P.2    Hahn, U.3
  • 32
    • 0024588529 scopus 로고
    • Cloning and characterization of the genes encoding the Msp I restriction-modification system
    • Lin P. M., Lee C. H., Roberts R. J. Cloning and characterization of the genes encoding the Msp I restriction-modification system. Nucl. Acids Res. 17:1989;3001-3011.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 3001-3011
    • Lin, P.M.1    Lee, C.H.2    Roberts, R.J.3
  • 34
    • 0027318633 scopus 로고
    • The DNA-binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center
    • Mi S., Roberts R. J. The DNA-binding affinity of HhaI methylase is increased by a single amino acid substitution in the catalytic center. Nucl. Acids Res. 21:1993;2459-2464.
    • (1993) Nucl. Acids Res. , vol.21 , pp. 2459-2464
    • Mi, S.1    Roberts, R.J.2
  • 35
    • 0023426552 scopus 로고
    • Cloning of two type II methylase genes that recognise asymmetric nucleotide sequences. Fok I and Hga I
    • Nwankwo D., Wilson G. Cloning of two type II methylase genes that recognise asymmetric nucleotide sequences. Fok I and Hga I. Mol. Gen. Genet. 209:1987;570-574.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 570-574
    • Nwankwo, D.1    Wilson, G.2
  • 36
    • 0024604147 scopus 로고
    • Predictive motifs derived from cytosine methyltransferases
    • Posfai J., Bhagwat A. S., Posfai G., Roberts R. J. Predictive motifs derived from cytosine methyltransferases. Nucl. Acids Res. 17:1989;2421-2435.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 2421-2435
    • Posfai, J.1    Bhagwat, A.S.2    Posfai, G.3    Roberts, R.J.4
  • 37
    • 0029257354 scopus 로고
    • Distinct CG and CNG DNA methyltransferases in Pisum sativum
    • Pradhan S., Adams R. L. P. Distinct CG and CNG DNA methyltransferases in Pisum sativum. Plant J. 7:1995;471-481.
    • (1995) Plant J. , vol.7 , pp. 471-481
    • Pradhan, S.1    Adams, R.L.P.2
  • 38
    • 0029068629 scopus 로고
    • The crystal structure of HaeIII methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinisch K. M., Chen L., Verdine G. L., Lipscomb W. N. The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing. Cell. 82:1995;143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinisch, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 39
    • 0001373226 scopus 로고
    • Reactions with N -ethylmaleimide and p -mercuribenzoate
    • Riordan J. F., Vallee B. L. Reactions with N -ethylmaleimide and p -mercuribenzoate. Methods Enzymol. 25:1972;449-456.
    • (1972) Methods Enzymol. , vol.25 , pp. 449-456
    • Riordan, J.F.1    Vallee, B.L.2
  • 40
    • 0344246128 scopus 로고
    • Regioselectivity in the reductive formation of dihydro-5-halo-2(1H)-pyrimidinones
    • Rise F., Undheim K. Regioselectivity in the reductive formation of dihydro-5-halo-2(1H)-pyrimidinones. Acta Chem. Scand. sect. B. 39:1985;195-201.
    • (1985) Acta Chem. Scand. Sect. B , vol.39 , pp. 195-201
    • Rise, F.1    Undheim, K.2
  • 41
    • 0024668449 scopus 로고
    • Sodium 2-mercaptoethanesulfonate in reversible adduct formation and water solubilization
    • Rise F., Undheim K. Sodium 2-mercaptoethanesulfonate in reversible adduct formation and water solubilization. Acta Chem. Scand. 43:1989;489-492.
    • (1989) Acta Chem. Scand. , vol.43 , pp. 489-492
    • Rise, F.1    Undheim, K.2
  • 42
    • 0344246127 scopus 로고
    • Structure investigations on products from the reaction of organocopper, organolithium and organomeganesium reagents with 2(1H)-pyrimidinones
    • Rise F., Romming C., Undheim K. Structure investigations on products from the reaction of organocopper, organolithium and organomeganesium reagents with 2(1H)-pyrimidinones. Acta Chem. Scand. sect. B. 39:1985;459-468.
    • (1985) Acta Chem. Scand. Sect. B , vol.39 , pp. 459-468
    • Rise, F.1    Romming, C.2    Undheim, K.3
  • 43
    • 38249029402 scopus 로고
    • Ethynyltriisopropoxytitanium reactions with pyrimidinones
    • Rise F., Grace D., Undheim K. Ethynyltriisopropoxytitanium reactions with pyrimidinones. J. Organomet. Chem. 338:1988;341-346.
    • (1988) J. Organomet. Chem. , vol.338 , pp. 341-346
    • Rise, F.1    Grace, D.2    Undheim, K.3
  • 45
    • 0000418476 scopus 로고
    • Covalent bond formation between a DNA cytosine methyltransferase and DNA containing 5-azacytosine
    • Santi D. V., Norment A., Garrett C. E. Covalent bond formation between a DNA cytosine methyltransferase and DNA containing 5-azacytosine. Proc. Natl. Acad. Sci. USA. 81:1984;6993-6997.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6993-6997
    • Santi, D.V.1    Norment, A.2    Garrett, C.E.3
  • 46
    • 0019367665 scopus 로고
    • Synthesis and antiviral activity of 1-(2-deoxy-β- D -ribofuranosyl)-5-(methylmercapto)-2-pyrimidinone
    • Schroeder A. C., Bardos T. H., Cheng Y.-C. Synthesis and antiviral activity of 1-(2-deoxy-β- D -ribofuranosyl)-5-(methylmercapto)-2-pyrimidinone. J. Med. Chem. 24:1981;109-112.
    • (1981) J. Med. Chem. , vol.24 , pp. 109-112
    • Schroeder, A.C.1    Bardos, T.H.2    Cheng, Y.-C.3
  • 47
    • 0027849713 scopus 로고
    • Purification of glutathione S -transferase fusion proteins
    • Smith D. B. Purification of glutathione S -transferase fusion proteins. Methods Mol. Cell. Biol. 4:1993;220-229.
    • (1993) Methods Mol. Cell. Biol. , vol.4 , pp. 220-229
    • Smith, D.B.1
  • 48
    • 0023258177 scopus 로고
    • Human DNA (cytosine-5)methyltransferase selectively methylates duplex DNA containing mispairs
    • Smith S. S., Hardy T. A., Baker D. J. Human DNA (cytosine-5)methyltransferase selectively methylates duplex DNA containing mispairs. Nucl. Acids Res. 15:1987;6899-6916.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 6899-6916
    • Smith, S.S.1    Hardy, T.A.2    Baker, D.J.3
  • 49
    • 0025737988 scopus 로고
    • The Hga I restriction-modification system contains two cytosine methylase genes responsible for modification of different DNA strands
    • Sugisaki H., Yamamoto K., Takanami M. The Hga I restriction-modification system contains two cytosine methylase genes responsible for modification of different DNA strands. J. Biol. Chem. 266:1991;13952-13957.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13952-13957
    • Sugisaki, H.1    Yamamoto, K.2    Takanami, M.3
  • 50
    • 0027285491 scopus 로고
    • Determination of the order of addition of substrates to Msp I DNA methyltransferase using a novel mechanism-based inhibitor
    • Taylor C., Ford K., Connolly B. A., Hornby D. P. Determination of the order of addition of substrates to Msp I DNA methyltransferase using a novel mechanism-based inhibitor. Biochem. J. 291:1993;493-504.
    • (1993) Biochem. J. , vol.291 , pp. 493-504
    • Taylor, C.1    Ford, K.2    Connolly, B.A.3    Hornby, D.P.4
  • 51
    • 0015890852 scopus 로고
    • The mechanism of inhibition of DNA synthesis in Escherichia coli by pyrimidin-2-one β- D ribofuranoside
    • Votruba I., Holý A., Wightman R. H. The mechanism of inhibition of DNA synthesis in Escherichia coli by pyrimidin-2-one β- D ribofuranoside. Biochim. Biophys. Acta. 324:1973;14-23.
    • (1973) Biochim. Biophys. Acta , vol.324 , pp. 14-23
    • Votruba, I.1    Holý, A.2    Wightman, R.H.3
  • 54
    • 0023176797 scopus 로고
    • Kinetic and catalytic mechanism of HhaI methyltransferase
    • Wu J. C., Santi D. V. Kinetic and catalytic mechanism of HhaI methyltransferase. J. Biol. Chem. 262:1987;4778-4786.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4778-4786
    • Wu, J.C.1    Santi, D.V.2
  • 55
    • 0026585662 scopus 로고
    • Substitutions of a cysteine conserved among DNA cytosine methylases result in a variety of phenotypes
    • Wyszynski M. W., Gabbara S., Bhagwat A. S. Substitutions of a cysteine conserved among DNA cytosine methylases result in a variety of phenotypes. Nucl. Acids Res. 20:1992;319-326.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 319-326
    • Wyszynski, M.W.1    Gabbara, S.2    Bhagwat, A.S.3
  • 57
    • 0029050606 scopus 로고
    • Hha I and Hpa II methyltransferases bind DNA mismatches, methylate uracil and block DNA repair
    • Yang A. S., Shen J.-C., Zingg J.-M., Mi S., Jones P. A. Hha I and Hpa II methyltransferases bind DNA mismatches, methylate uracil and block DNA repair. Nucl. Acids Res. 23:1995;1380-1387.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 1380-1387
    • Yang, A.S.1    Shen, J.-C.2    Zingg, J.-M.3    Mi, S.4    Jones, P.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.