Recognition of DNA Sequences by Restriction Endonucleases

  • Guenter Maass
Part of the NATO ASI Series book series (volume 137)


Type II restriction endonucleases recognize DNA sequences 4 or 6 basepairs long with very high specificity in a vast excess of non-specific DNA binding sites. They cleave the DNA within or in the immediate vicinity of the recognition sequence. Because of the immense importance of these enzymes in analysis, preparation and in vitro recombination of DNA many investigations have been carried out to understand the structural and mechanistic features underlying their mode of recognition1. Among approximately 500 type II restriction endonucleases described, EcoRI is the so far best studied enzyme. EcoRI is a dimeric protein with two identical sub-units, the aminoacid sequence of which is known2,3.


Recognition Sequence Cleavage Rate Major Groove Linear Diffusion Canonical Sequence 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Modrich, P., CRC Crit. Rev. Biochem. 13, 287 (1982).PubMedCrossRefGoogle Scholar
  2. 2.
    Newman, A. K., Rubin, R. A., Kine, S. H., and Modrich, P., J. Biol. Chem. 256, 2131 (1981).PubMedGoogle Scholar
  3. 3.
    Greene, P. J., Gupta, M., Boyer, H. W., Brown, W. E., and Rosenberg, J. M., J. Biol. Chem 256, 2143 (1981).PubMedGoogle Scholar
  4. 4.
    Frederick, C., Grable, J., Melia, M., Samudzi, C., Jen-Jacobsen, L., Wang, B. C., Greene, P., Boyer, H. W., and Rosenberg, J. M., Nature 309, 327 (1984).PubMedCrossRefGoogle Scholar
  5. 5.
    Rosenberg, J. M., Proceedings of the 14th Aharon-Katzir-Conference, Bielefeld 1985.Google Scholar
  6. 6.
    Halford, S. E., Biochem. Soc. Transactions 8, 399 (1980).Google Scholar
  7. 7.
    Berg, O. G., Winter, R. B., and von Hippel, P. H., Biochemistry 20, 6926 (1981).CrossRefGoogle Scholar
  8. 8.
    Winter, R. B., Berg, O. G., and von Hippel, P. H., Biochemistry 20, 6961 (1981).PubMedCrossRefGoogle Scholar
  9. 9.
    Jen-Jacobsen, L., Lesser, D., and Kurpiewski, M., Cell 45, 619 (1986).CrossRefGoogle Scholar
  10. 10.
    Woodhead, J. L., and Malcolm, A. D. B., Nucl. Acids Res., 8, 389 (1980).PubMedCrossRefGoogle Scholar
  11. 11.
    Goppelt, M., Pingoud, A., Maass, G., Mayer, H., Koester, H., and Frank, R., Eur. J. Biochem 104, 101 (1980).PubMedCrossRefGoogle Scholar
  12. 12.
    Modrich, P., and Zabel, D., J. Biol. Chem., 251, 5866 (1976).PubMedGoogle Scholar
  13. 13.
    Halford, S. E., and Johnsen, N. P., Biochem. J., 191, 593 (1980).PubMedGoogle Scholar
  14. 14.
    Langowski, J., Pingoud, A., Goppelt, M., and Maass, G., Nucl. Acids Res. 8, 4727 (1980).PubMedCrossRefGoogle Scholar
  15. 15.
    Clore, G. M., Gronenborn, A. M., and Davies, R. W., J. Mol. Biol. 155, 447 (1982).PubMedCrossRefGoogle Scholar
  16. 16.
    Pingoud, A., Alves, J. Urbanke, C., and Zabeau, M., to be published.Google Scholar
  17. 17.
    Goodman, H. M., Greene, P. J., Garfin, D. E., and Boyer, H. W., in Vogel, H. J. (Ed.): “Nucleic Acid-Protein Recognition”, Academic Press, New York, pp 239–259 (1977).CrossRefGoogle Scholar
  18. 18.
    Rosenberg, J. M., and Greene, P. J., DNA 1, 117 (1982).PubMedCrossRefGoogle Scholar
  19. 19.
    Jen-Jacobsen, L., Kurpiewski, M., Lesser, D., Grable, J., Boyer, H. W., Rosenberg, J. M., and Greene, P. J., J. Biol. Chem. 258, 14638 (1983).Google Scholar
  20. 20.
    Alves, J., Pingoud, A., Haupt, W., Langowski, J., Peters, F., Maass, G., and Wolff, C., Eur. J. Biochem., 140, 83 (1984).PubMedCrossRefGoogle Scholar
  21. 21.
    Wolfes, H., Fliess, A., and Pingoud, A., Eur. J. Biochem., 150, 105 (1985).PubMedCrossRefGoogle Scholar
  22. 22.
    Richter, P.H., and Eigen, M., Biophys.Chem. 2, 255 (1974).PubMedCrossRefGoogle Scholar
  23. 23.
    Jack, W. E., Terry, B. J., and Modrich, P., Proc. Natl. Acad. Sci. USA, 79, 4010 (1982).PubMedCrossRefGoogle Scholar
  24. 24.
    Langowski, J., Alves, J., Pingoud, A., and Maass, G., Nucl. Acids Res. 11, 501 (1983).PubMedCrossRefGoogle Scholar
  25. 25.
    Terry, B. J., Jack, W. E., and Modrich, P., J. Biol. Chem. 260, 13130 (1985).PubMedGoogle Scholar
  26. 26.
    Ehbrecht, H. J., Pingoud, A., Urbanke, C., Maass, G., and Gualerzi, C., J. Biol. Chem. 260, 6160 (1985).PubMedGoogle Scholar
  27. 27.
    Kohring, G. W., Mayer, F., and Mayer, H., Europ. J. Cell Biology 37, 1 (1985).Google Scholar
  28. 28.
    von Hippel, P. H., and Berg, O.G., Proc. Natl. Acad. Sci. USA, 83, 1608 (1986).CrossRefGoogle Scholar
  29. 29.
    Modrich, P., and Roberts, R. J., in “Nucleases”, Linn, S. M., and Roberts, R. J., ed., 109, Cold Spring Harbor Laboratory, New York (1982).Google Scholar
  30. 30.
    Fersht, A. R., Leatherbarrow, R. J., and Wells, T. N. C., TIBS 11, 321 (1986).Google Scholar
  31. 31.
    Haupt, W., Ph. D. thesis, University of Hannover (1983).Google Scholar
  32. 32.
    Fliess, A., Wolfes, H., Rosenthahl, A., Schwellnus, K., Bloecker, H., Frank, R., and Pingoud, A., Nucl. Acids Res., 14, 3463 (1986).PubMedCrossRefGoogle Scholar
  33. 33.
    Brennan, C. A., von Cleve, M. D., and Gumport, R. I., J. Biol. Chem. 261, 7270 (1986).PubMedGoogle Scholar
  34. 34.
    Woodhead, J. L., and Malcolm, A. D. B., Eur, J. Biochem. 120, 125 (1981).CrossRefGoogle Scholar
  35. 35.
    Scholtissek, S., Pingoud, A., Maass, G., and Zabeau, M., J. Biol. Chem. 261, 2228 (1986).PubMedGoogle Scholar
  36. 36.
    Wolfes, H., Fliess, A., Winkler, F., and Pingoud, A., Eur. J. Biochem., in press (1986).Google Scholar
  37. 37.
    Matthews, B. W., Ohlendorf, D. H., Anderson, W. F., Fisher, R. G., and Takeda, Y., Cold Spring Harbor Symp. Quant. Biol. 47, 427 (1983).PubMedCrossRefGoogle Scholar
  38. 38.
    Cotton, F. A., Hazen, E. E.(Jr.), and Legg, M. J., Proc. Natl. Acad. Sci. USA, 76, 2551 (1979).PubMedCrossRefGoogle Scholar
  39. 39.
    Price, P. A., Stein, W. H., and Moore, S., J. Biol. Chem. 244, 924 (1969).PubMedGoogle Scholar
  40. 40.
    Suck, D., Oefner, C., and Kabsch, W., EMBO J., 3, 2423 (1984).PubMedGoogle Scholar
  41. 41.
    Halford, S. E., TIBS 8, 455 (1983).Google Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Guenter Maass
    • 1
  1. 1.Biophysikalische ChemieMed. Hochschule HannoverHannover 61Germany

Personalised recommendations