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Biological function of DNA methylation

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Abstract

Structural and functional properties of prokaryotic DNA methyltransferases are summarized. The different aspects of the role of DNA methylation which influences DNA-protein interaction in restriction and modification of DNA and in mismatch repair, DNA replication and gene expression are discussed.

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References

  • Adams R.L.P.: DNA methylation.Biochem. J. 265, 309–320 (1990).

    PubMed  CAS  Google Scholar 

  • Adams R.L.P., Burdon R.H.:Enzymes of Nucleic Acid Synthesis and Processing (S.T. Jacob, Ed.), Vol. 1, pp. 119–144. CRC Press, Boca Raton (FL) 1983.

    Google Scholar 

  • Adams R.L.P., Rinaldi A., McGarvey M., Bryans M., Ball K.: Eukaryotic DNA methyltransferase: tissue and species distribution.Gene 74, 125–128 (1988).

    Article  PubMed  CAS  Google Scholar 

  • Bale A., d’Alarcao M., Marinus M.G.: Characterization of DNA adenine methylation mutants ofEscherichia coli K-12.Mut. Res. 59, 165–175 (1979).

    Google Scholar 

  • Borek E., Srinivasan R.P.: The methylation of nucleic acids.Ann. Rev. Biochem. 35, 275–297 (1966).

    Article  CAS  Google Scholar 

  • Burckhardt J., Weisemann J., Hamilton D.L., Yuan R.: Complexes formed between the restriction endonucleaseEcoK and heteroduplex DNA.J. Mol. Biol. 153, 425–440 (1981).

    Article  PubMed  CAS  Google Scholar 

  • Bühler R., Yuan R.: Characterization of a restriction enzyme fromEscherichia coli K carrying a mutation on the modification subunit.J. Biol. Chem. 253, 6756–6760 (1978).

    PubMed  Google Scholar 

  • Cowan G.M., Gann A.A.F., Murray N.E.: Conservation of complex DNA recognition domains between families of restriction enzymes.Cell 56, 103–109 (1989).

    Article  PubMed  CAS  Google Scholar 

  • Hubáček J., Glover S.W.: Complementation analysis of temperature-sensitive host specificity mutations inEscherichia coli.J. Mol. Biol. 50, 111–127 (1970).

    Article  PubMed  Google Scholar 

  • Hubáček J., Zinkevich V.E., Weiserová M.: The location of temperature-sensitivetrans-dominant mutation and its effect on restriction and modification inEscherichia coli K12.J. Gen. Microbiol. 135, 3057–3065 (1989).

    PubMed  Google Scholar 

  • Jones M., Wagner R., Radman M.: Repair of a mismatch is influenced by the base composition of the surrounding nucleotide sequence.Genetics 115, 605–610 (1987).

    PubMed  CAS  Google Scholar 

  • Kan N.C., Lautenberger J.A., Edgell M.H., Hutchinson III,C.A.: The nucleotide sequence recognized by theEscherichia coli K12 restriction and modification enzymes.J. Mol. Biol. 130, 191–209 (1979).

    Article  PubMed  CAS  Google Scholar 

  • Kelleher J.E., Daniel A.S., Murray N.E.: Mutations that conferde novo activity upon a maintenance methyltransferase.J. Mol. Biol. 221, 431–440 (1991).

    Article  PubMed  CAS  Google Scholar 

  • Kleckner N.: Mechanism and regulation Tn10 and IS10 transposition, pp. 221–237 inRegulation of Gene Expression (I. Booth, C. Higgins, Eds). Symp. Soc. Gen. Microbiol, Cambridge University Press, Cambridge 1986.

    Google Scholar 

  • Kleckner N., Morisato D., Roberts D., Bender J.: Mechanism and regulation of Tn10 transposition.Cold Spring Harbor Symp. Quant. Biol. 49, 235–244 (1984).

    PubMed  CAS  Google Scholar 

  • Längle-Rouault F., Maenhaut-Michel G., Radman M.: GATC sequences, DNA nicks and the MutH function inEscherichia coli mismatch repair.EMBO J. 6, 1121–1127 (1987).

    PubMed  Google Scholar 

  • Lu A.-L., Welch K., Clark S., Su S.-S., Modrich P.: Repair of DNA base-pair mismatches in extracts ofEscherichia coli.Cold Spring Harbor Symp. Quant. Biol. 49, 589–596 (1984).

    PubMed  CAS  Google Scholar 

  • Lyons S.M., Schendel P.F.: Kinetics of methylation inEscherichia coli K12.J. Bacteriol. 159, 421–423 (1984).

    PubMed  CAS  Google Scholar 

  • Marinus M.G.: Methylation of DNA, pp. 697–702 inEscherichia coli and Salmonella typhimurium Cellular and Molecular Biology (F.C. Neihardt, Ed. in Chief), Vol. I. American Society for Microbiology, Washington (DC) 1987.

    Google Scholar 

  • Meselson M., Yuan R.: DNA restriction enzyme fromEscherichia coli.Nature 217, 1111–1114 (1968).

    Article  Google Scholar 

  • Messer W., Bellekes U., Lother H.: Effect ofdam-methylation on the activity of the replication origin,oriC.EMBO J. 4, 1319–1326 (1985).

    Google Scholar 

  • Modrich P.: Methyl-directed DNA mismatch correction.J. Biol. Chem. 264, 6597–6600 (1989).

    PubMed  CAS  Google Scholar 

  • Oka A., Sugimoto K., Takanami M., Hirota Y.: Replication origin ofEscherichia coli K-12 chromosome: the size and structure of the minimum DNA segment carrying the information for autonomous replication.Mol. Gen. Genet. 178, 9–20 (1980).

    Article  PubMed  CAS  Google Scholar 

  • Peterson K.R., Wertman K.F., Mount D.W., Marinus M.G.: Viability ofEscherichia coli K-12 DNA adenine methylase (dam) mutants requires increased expression of specific genes in the SOS regulon.Mol. Gen. Genet. 201, 14–19 (1985).

    Article  PubMed  CAS  Google Scholar 

  • Pösfai J., Bhagwat A.S., Posfai G., Roberts R.J.: Predictive motifs derived from cytosine methyltransferases.Nucl. Acid. Res. 17, 2421–2435 (1989).

    Article  Google Scholar 

  • Price C., Lingner J., Bickle T.A.: Basis for changes in DNA recognition by theEcoR124 andEcoR124/3 type I DNA restriction and modification enzymes.J. Mol. Biol. 205, 115–125 (1989).

    Article  PubMed  CAS  Google Scholar 

  • Smith D.W., Garland A.M., Herman G., Enns R.E., Baker T.A., Zyskind J.W.: Importance of state of methylation oforiC GATC sites in initiation of DNA replication inEscherichia coli.EMBO J. 4, 1327–1332 (1985).

    Google Scholar 

  • Sternberg N.: Evidence that adenine methylation influences DNA—protein interactions inEscherichia coli.J. Bacteriol. 164, 490–493 (1985).

    PubMed  CAS  Google Scholar 

  • Su S.-S., Modrich P.:Escherichia coli mutS-encoded protein binds to mismatched DNA base pairs.Proc. Nat. Acad. Sci. USA 83, 5057–5061 (1986).

    Article  PubMed  CAS  Google Scholar 

  • Subbaramaiah K., Charles H., Simms S.A.: Probing the role of cysteine residues in theCheR methyltransferase.J. Biol. Chem. 266, 19023–19027 (1991).

    PubMed  CAS  Google Scholar 

  • Vovis G.F., Horiuchi K., Hartman W., Zinder N.D.: Restriction endonuclease B and f1 heteroduplex DNA.Nature New Biol. 246, 13–16 (1973).

    PubMed  CAS  Google Scholar 

  • Wilson G.G.: Type II restriction-modification systems.Trends Genet. 4, 314–318 (1988).

    Article  PubMed  CAS  Google Scholar 

  • Wilson G.G.: Organization of restriction modification systems.Nucl. Acid. Res. 19, 2539–2566 (1991).

    Article  CAS  Google Scholar 

  • Yuan R.: Structure and mechanism of multifunctional restriction endonucleases.Ann. Rev. Biochem. 50, 285–315 (1981).

    Article  PubMed  CAS  Google Scholar 

  • Zinkevich V.E., Weiserová M., Kryukov V.M., Hubáček J.: A mutation that converts serine340 of the HsdSK polypeptide to phenylalanine and its effects on restriction and modification inEscherichia coli K-12.Gene 90, 125–128 (1990).

    Article  PubMed  CAS  Google Scholar 

  • Zinkevich V.E., Heslop P., Glover S.W., Weiserová M., Hubáček J., Firman K.: A mutation that identifies a protein: protein interaction domain in the specificity polypeptide of the type I restriction endonuclease R·EcoK.J. Mol. Biol., in press (1992).

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  1. Institute of Microbiology, Czechoslovak Academy of Sciences, 142 20, Prague 4

    J. Hubáček

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Hubáček, J. Biological function of DNA methylation. Folia Microbiol 37, 323–329 (1992). https://doi.org/10.1007/BF02815658

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