Skip to main content
SpringerLink
Log in

Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein

  • Letter
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

THE cold-shock response in both Escherichia coli and Bacillus subtilis is induced by an abrupt downshift in growth temperature. It leads to the increased production of the major cold-shock proteins, CS7.4 and CspB, respectively1–3. CS7.4 is a transcriptional activator of two genes4,5. CS7.4 and CspB share 43 per cent sequence identity with the nucleic acid-binding domain of the eukaryotic gene-regulatory Y-box factors6. This cold-shock domain is conserved from bacteria to man7 and contains the RNA-binding RNP1 sequence motif8. As a prototype of the cold-shock domain, the structure of CspB has been determined here from two crystal forms. In both, CspB is present as an antiparallel five-stranded β-barrel. Three consecutive β-strands, the central one containing the RNP1 motif, create a surface rich in aromatic and basic residues that are presumably involved in nucleic acid binding. Preferential binding of CspB to single-stranded DNA is observed in gel retardation experiments.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Jones, P. G., VanBogelen, R. A. & Neidhardt, F. C. J. Bact. 169, 2092–2095 (1987).

    Article  CAS  Google Scholar 

  2. Goldstein, J., Pollitt, N. S. & Inouye, M. Proc. natn. Acad. Sci. U.S.A. 87, 283–287 (1990).

    Article  ADS  CAS  Google Scholar 

  3. Willimsky, G., Bang, H., Fischer, G. & Marahiel, M. A. J. Bact. 174, 6326–6335 (1992).

    Article  CAS  Google Scholar 

  4. La Teana, A. et al. Proc. natn. Acad. Sci. U.SA. 88, 10907–10911 (1991).

    Article  ADS  CAS  Google Scholar 

  5. Jones, P. G., Krah, R., Tafuri, S. A. & Wolffe, A. P., J. Bact. 174, 5798–5802 (1992).

    Article  CAS  Google Scholar 

  6. Wistow, G. Nature 344, 823–824 (1990).

    Article  ADS  CAS  Google Scholar 

  7. Wolffe, A. P., Tafuri, S., Ranjan, M. & Familari, M. New Biol. 4, 290–298 (1992).

    CAS  PubMed  Google Scholar 

  8. Landsman, D. Nucleic Acids Res. 20, 2861–2864 (1992).

    Article  CAS  Google Scholar 

  9. Richardson, J. S. Adv. Protein Chem. 34, 167–339 (1981).

    Article  CAS  Google Scholar 

  10. Schnuchel, A. et al. Nature (this issue).

  11. Nagai, K., Oubridge, C., Jessen, T. H., Li, J. & Evans, P. R. Nature 348, 515–520 (1990).

    Article  ADS  CAS  Google Scholar 

  12. Crawford, D. R. & Richter, J. D. Development 101, 741–749 (1987).

    CAS  PubMed  Google Scholar 

  13. Murray, M. T., Krohne, G. & Franke, W. W. J. Cell Blol. 112, 1–11 (1991).

    Article  CAS  Google Scholar 

  14. Murzin, A. G. EMBO J. 12, 861–867 (1993).

    Article  CAS  Google Scholar 

  15. Hynes, T. R. & Fox, R. O. Proteins: Struct. Funct. Genet. 10, 92–105 (1991).

    Article  CAS  Google Scholar 

  16. Brayer, G. D. & McPherson, A. J. molec. Biol. 169, 565–596 (1983).

    Article  CAS  Google Scholar 

  17. Folkers, P. J. M. et al. Eur. J. Biochem. 202, 349–360 (1991).

    Article  CAS  Google Scholar 

  18. Merrill, B. M., Stone, K. L., Cobianchi, F., Wilson, S. H. & Williams, K. R. J. biol. Chem. 263, 3307–3313 (1988).

    CAS  PubMed  Google Scholar 

  19. Brennan, C. A. & Platt, T. J. biol. Chem. 266, 17296–17305 (1991).

    CAS  PubMed  Google Scholar 

  20. Schindelin, H., Herrler, M., Willimsky, G., Marahiel, M. A. & Heinemann, U. Proteins Struct. Funct. Genet. 14, 120–124 (1992).

    Article  CAS  Google Scholar 

  21. CCP4 (The SERC Collaborative Computing Project No. 4, SERC Daresbury Laboratory. Warrington, UK, 1979).

  22. Sheidrick, G. M. in Crystallographic Computing (eds Sheldrick, G. M., Krüger, C. & Goddard, R.) 175–189 (Oxford Univ. Press. Oxford, UK, 1985).

    Google Scholar 

  23. Wang, B. C. Meth. Enzym. 115, 90–112 (1985).

    Article  CAS  Google Scholar 

  24. Jones, T. A. J. appl. Crystallogr. 11, 268–272 (1978).

    Article  CAS  Google Scholar 

  25. Brünger, A. T., Kuriyan, J. & Karplus, M. Science 235, 458–460 (1987).

    Article  ADS  Google Scholar 

  26. Read, R. Acta crystallogr. A42, 140–149 (1986).

    Article  Google Scholar 

  27. Kraulis, J. P. J. appl. Crystallogr. 24, 946–950 (1991).

    Article  Google Scholar 

  28. Kabsch, W. & Sander, C. Biopolymers 22, 2577–2637 (1983).

    Article  CAS  Google Scholar 

  29. Fried, M. & Crothers, D. M. Nucleic Acids Res. 9, 6505–6525 (1981).

    Article  CAS  Google Scholar 

  30. Merril, C. R., Goldman, D., Sedman, S. A. & Ebert, M. H. Science 211, 1437–1438 (1980).

    Article  ADS  Google Scholar 

Download references

Author information

Author notes

  1. Mohamed A. Marahiel: Biochemie/FB Chemie, Philipps-Universität Marburg, Hans-Meerwein Strasse, D-35043 Marburg, Germany

Authors and Affiliations

  1. Institut für Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195, Berlin, Germany

    Hermann Schindelin, Mohamed A. Marahiel & Udo Heinemann

Authors
  1. Hermann Schindelin
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Mohamed A. Marahiel
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Udo Heinemann
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Schindelin, H., Marahiel, M. & Heinemann, U. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 364, 164–168 (1993). https://doi.org/10.1038/364164a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/364164a0

  • Springer Nature Limited

This article is cited by

Search

Navigation