Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Mar;76(3):1089–1093. doi: 10.1073/pnas.76.3.1089

Enzymatic insertion of purine bases into depurinated DNA in vitro.

Z Livneh, D Elad, J Sperling
PMCID: PMC383194  PMID: 375225

Abstract

An enzymatic activity that inserts purines into depurinated DNA was found in a soluble enzyme extract of Escherichia coli. This activity brings about the insertion of adenine and guanine into the appropriate apurinic sites in double-stranded DNA by using the corresponding deoxyribonucleoside triphosphates as the purine donors. Magnesium ions are required for this activity, it is inhibited by caffeine, and it does not act on depurinated single-stranded DNA. The insertion activity described here may represent a step in a repair mechanism, "base-insertion repair," whereby apurinic sites (which may occur in double-stranded DNA either due to the removal of damaged purines with specific glycosylases or by spontaneous depurination) are directly filled with the correct missing purine base.

Full text

PDF
1091

Images in this article

1090Image
on p.1090

Selected References

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

  1. Bose K., Karran P., Strauss B. Repair of depurinated DNA in vitro by enzymes purified from human lymphoblasts. Proc Natl Acad Sci U S A. 1978 Feb;75(2):794–798. doi: 10.1073/pnas.75.2.794. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Brutlag D., Kornberg A. Enzymatic synthesis of deoxyribonucleic acid. 36. A proofreading function for the 3' leads to 5' exonuclease activity in deoxyribonucleic acid polymerases. J Biol Chem. 1972 Jan 10;247(1):241–248. [PubMed] [Google Scholar]
  3. Espejo R. T., Canelo E. S., Sinsheimer R. L. DNA of bacteriophage PM2: a closed circular double-stranded molecule. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1164–1168. doi: 10.1073/pnas.63.4.1164. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Hinnen R., Schäfer R., Franklin R. M. Structure and synthesis of a lipid-containing bacteriophage. Preparation of virus and localization of the structural proteins. Eur J Biochem. 1974 Dec 16;50(1):1–14. doi: 10.1111/j.1432-1033.1974.tb03867.x. [DOI] [PubMed] [Google Scholar]
  5. Kirtikar D. M., Goldthwait D. A. The enzymatic release of O6-methylguanine and 3-methyladenine from DNA reacted with the carcinogen N-methyl-N-nitrosourea. Proc Natl Acad Sci U S A. 1974 May;71(5):2022–2026. doi: 10.1073/pnas.71.5.2022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Knippers R., Razin A., Davis R., Sinsheimer R. L. The process of infection with Bacteriophage phi-X174. XXIX. In vivo studies on the synthesis of the single-stranded DNA of progeny phi-X174 bacteriophage. J Mol Biol. 1969 Oct 28;45(2):237–263. doi: 10.1016/0022-2836(69)90103-x. [DOI] [PubMed] [Google Scholar]
  7. Kuebler J. P., Goldthwait D. A. An endonuclease from calf liver specific for apurinic sites in DNA. Biochemistry. 1977 Apr 5;16(7):1370–1377. doi: 10.1021/bi00626a021. [DOI] [PubMed] [Google Scholar]
  8. LAWLEY P. D., BROOKES P. FURTHER STUDIES ON THE ALKYLATION OF NUCLEIC ACIDS AND THEIR CONSTITUENT NUCLEOTIDES. Biochem J. 1963 Oct;89:127–138. doi: 10.1042/bj0890127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Laval J. Two enzymes are required from strand incision in repair of alkylated DNA. Nature. 1977 Oct 27;269(5631):829–832. doi: 10.1038/269829a0. [DOI] [PubMed] [Google Scholar]
  11. Lindahl T., Nyberg B. Rate of depurination of native deoxyribonucleic acid. Biochemistry. 1972 Sep 12;11(19):3610–3618. doi: 10.1021/bi00769a018. [DOI] [PubMed] [Google Scholar]
  12. Linsley W. S., Penhoet E. E., Linn S. Human endonuclease specific for apurinic/apyrimidinic sites in DNA. Partial purification and characterization of multiple forms from placenta. J Biol Chem. 1977 Feb 25;252(4):1235–1242. [PubMed] [Google Scholar]
  13. Ljungquist S. A new endonuclease from Escherichia coli acting at apurinic sites in DNA. J Biol Chem. 1977 May 10;252(9):2808–2814. [PubMed] [Google Scholar]
  14. Ljungquist S., Lindahl T. A mammalian endonuclease specific for apurinic sites in double-stranded deoxyribonucleic acid. I. Purification and general properties. J Biol Chem. 1974 Mar 10;249(5):1530–1535. [PubMed] [Google Scholar]
  15. Razin A., Sedat J. W., Sinsheimer R. L. Structure of the DNA of bacteriophage phiX174. VII. Methylation. J Mol Biol. 1970 Oct 28;53(2):251–259. doi: 10.1016/0022-2836(70)90298-6. [DOI] [PubMed] [Google Scholar]
  16. Riazuddin S., Lindahl T. Properties of 3-methyladenine-DNA glycosylase from Escherichia coli. Biochemistry. 1978 May 30;17(11):2110–2118. doi: 10.1021/bi00604a014. [DOI] [PubMed] [Google Scholar]
  17. Strauss B., Hill T. The intermediate in the degradation of DNA alkylated with a monofunctional alkylating agent. Biochim Biophys Acta. 1970 Jul 16;213(1):14–25. doi: 10.1016/0005-2787(70)90003-1. [DOI] [PubMed] [Google Scholar]
  18. Teebor G. W., Duker N. J. Human endonuclease activity for DNA apurinic sites. Nature. 1975 Dec 11;258(5535):544–547. doi: 10.1038/258544a0. [DOI] [PubMed] [Google Scholar]
  19. Timson J. Caffeine. Mutat Res. 1977;47(1):1–52. doi: 10.1016/0165-1110(77)90016-1. [DOI] [PubMed] [Google Scholar]
  20. Verly W. G., Gossard F., Crine P. In vitro repair of apurinic sites in DNA. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2273–2275. doi: 10.1073/pnas.71.6.2273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Verly W. G., Rassart E. Purification of Escherichia coli endonuclease specific for apurinic sites in DNA. J Biol Chem. 1975 Oct 25;250(20):8214–8219. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES