Skip to main content
PMC home page
Biochemical Journal logoLink to Biochemical Journal
. 1988 Oct 15;255(2):699–703.

A DNA-modification methylase from Bacillus stearothermophilus V.

R Barra 1, M Chiong 1, E González 1, C Vásquez 1
PMCID: PMC1135282  PMID: 3202841

Abstract

A type II modification methylase (M BstVI) was partially purified from the thermophilic bacterium Bacillus stearothermophilus V. The methylase catalyses the transfer of methyl groups from S-adenosyl-L-methionine to unmodified double-stranded DNA. The product of methylation was identified by paper chromatography as N6-methyladenine. Since M BstVI protects DNA against cleavage by BstVI and XhoI restriction endonucleases, it follows that it methylates the adenine residue in the sequence 5'-C-T-C-G-A-G-3'.

Full text

PDF
699

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ARBER W., DUSSOIX D. Host specificity of DNA produced by Escherichia coli. I. Host controlled modification of bacteriophage lambda. J Mol Biol. 1962 Jul;5:18–36. doi: 10.1016/s0022-2836(62)80058-8. [DOI] [PubMed] [Google Scholar]
  2. Boyer H. W. DNA restriction and modification mechanisms in bacteria. Annu Rev Microbiol. 1971;25:153–176. doi: 10.1146/annurev.mi.25.100171.001101. [DOI] [PubMed] [Google Scholar]
  3. Brooks J. E., Roberts R. J. Modification profiles of bacterial genomes. Nucleic Acids Res. 1982 Feb 11;10(3):913–934. doi: 10.1093/nar/10.3.913. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Butkus V. V., Klimasauskas S. J., Janulaitis A. A. Analysis of products of DNA modification by methylases: a procedure for the determination of 5- and N4-methylcytosines in DNA. Anal Biochem. 1985 Jul;148(1):194–198. doi: 10.1016/0003-2697(85)90645-1. [DOI] [PubMed] [Google Scholar]
  5. Butkus V., Klimasauskas S., Kersulyte D., Vaitkevicius D., Lebionka A., Janulaitis A. Investigation of restriction-modification enzymes from M. varians RFL19 with a new type of specificity toward modification of substrate. Nucleic Acids Res. 1985 Aug 26;13(16):5727–5746. doi: 10.1093/nar/13.16.5727. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dugaiczyk A., Hedgpeth J., Boyer H. W., Goodman H. M. Physical identity of the SV40 deoxyribonucleic acid sequence recognized by the Eco RI restriction endonuclease and modification methylase. Biochemistry. 1974 Jan 29;13(3):503–512. doi: 10.1021/bi00700a016. [DOI] [PubMed] [Google Scholar]
  7. Gingeras T. R., Brooks J. E. Cloned restriction/modification system from Pseudomonas aeruginosa. Proc Natl Acad Sci U S A. 1983 Jan;80(2):402–406. doi: 10.1073/pnas.80.2.402. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Janulaitis A., Klimasauskas S., Petrusyte M., Butkus V. Cytosine modification in DNA by BcnI methylase yields N4-methylcytosine. FEBS Lett. 1983 Sep 5;161(1):131–134. doi: 10.1016/0014-5793(83)80745-5. [DOI] [PubMed] [Google Scholar]
  9. Kessler C., Höltke H. J. Specificity of restriction endonucleases and methylases--a review. Gene. 1986;47(1):1–153. doi: 10.1016/0378-1119(86)90245-3. [DOI] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Levy W. P., Welker N. E. Deoxyribonucleic acid modification methylase from Bacillus stearothermophilus. Biochemistry. 1981 Mar 3;20(5):1120–1127. doi: 10.1021/bi00508a012. [DOI] [PubMed] [Google Scholar]
  12. MARSHAK A., VOGEL H. J. Microdetermination of purines and pyrimidines in biological materials. J Biol Chem. 1951 Apr;189(2):597–605. [PubMed] [Google Scholar]
  13. McClelland M., Kessler L. G., Bittner M. Site-specific cleavage of DNA at 8- and 10-base-pair sequences. Proc Natl Acad Sci U S A. 1984 Feb;81(4):983–987. doi: 10.1073/pnas.81.4.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. McClelland M., Nelson M., Cantor C. R. Purification of Mbo II methylase (GAAGmA) from Moraxella bovis: site specific cleavage of DNA at nine and ten base pair sequences. Nucleic Acids Res. 1985 Oct 25;13(20):7171–7182. doi: 10.1093/nar/13.20.7171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. McClelland M., Nelson M. The effect of site specific methylation on restriction endonuclease digestion. Nucleic Acids Res. 1985;13 (Suppl):r201–r207. doi: 10.1093/nar/13.suppl.r201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. McClelland M. Purification and characterization of two new modification methylases: MClaI from Caryophanon latum L and MTaqI from Thermus aquaticus YTI. Nucleic Acids Res. 1981 Dec 21;9(24):6795–6804. doi: 10.1093/nar/9.24.6795. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. McClelland M. The effect of site specific methylation on restriction endonuclease cleavage (update). Nucleic Acids Res. 1983 Jan 11;11(1):r169–r173. doi: 10.1093/nar/11.1.235-c. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Meselson M., Yuan R., Heywood J. Restriction and modification of DNA. Annu Rev Biochem. 1972;41:447–466. doi: 10.1146/annurev.bi.41.070172.002311. [DOI] [PubMed] [Google Scholar]
  19. Nelson M., Christ C., Schildkraut I. Alteration of apparent restriction endonuclease recognition specificities by DNA methylases. Nucleic Acids Res. 1984 Jul 11;12(13):5165–5173. doi: 10.1093/nar/12.13.5165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Roberts R. J. Restriction and modification enzymes and their recognition sequences. Nucleic Acids Res. 1985;13 (Suppl):r165–r200. doi: 10.1093/nar/13.suppl.r165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sato S., Nakazawa K., Shinomiya T. A DNA methylase from Thermus thermophilus HB8. J Biochem. 1980 Sep;88(3):737–747. doi: 10.1093/oxfordjournals.jbchem.a133026. [DOI] [PubMed] [Google Scholar]
  22. Vásquez C. Isolation and partial characterization of BstVI, a thermostable isoschizomer of XhoI. Biochem Int. 1985 Apr;10(4):655–662. [PubMed] [Google Scholar]
  23. Yuan R. Structure and mechanism of multifunctional restriction endonucleases. Annu Rev Biochem. 1981;50:285–319. doi: 10.1146/annurev.bi.50.070181.001441. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES