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
. 1991 Jan 15;88(2):561–564. doi: 10.1073/pnas.88.2.561

X-ray scattering indicates that the leucine zipper is a coiled coil.

R Rasmussen 1, D Benvegnu 1, E K O'Shea 1, P S Kim 1, T Alber 1
PMCID: PMC50851  PMID: 1988953

Abstract

Dimerization of the bZIP class of eukaryotic transcriptional control proteins requires a sequence motif called the leucine zipper. We have grown two distinct crystal forms of a 33-amino acid peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4. This peptide is known to form a dimer of parallel helices in solution. X-ray scattering from both crystal forms shows reflections that are diagnostic of coiled coils. The most notable reflections occur at approximately 5.2 A resolution and correspond to the pitch of helices in coiled coils. There is no diffraction maximum near 5.4 A, the characteristic pitch of straight helices. Our results provide direct evidence that the leucine zipper of GCN4 is a coiled coil.

Full text

PDF
561

Images in this article

562Image
on p.562
562Image
on p.562
562Image
on p.562
563Image
on p.563
563Image
on p.563

Selected References

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

  1. Astbury W. T., Reed R., Spark L. C. An X-ray and electron microscope study of tropomyosin. Biochem J. 1948;43(2):282–287. doi: 10.1042/bj0430282. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. COHEN C., HOLMES K. C. X-ray diffraction evidence for alpha-helical coiled-coils in native muscle. J Mol Biol. 1963 May;6:423–432. doi: 10.1016/s0022-2836(63)80053-4. [DOI] [PubMed] [Google Scholar]
  3. CRICK F. H. C. Is alpha-keratin a coiled coil? Nature. 1952 Nov 22;170(4334):882–883. doi: 10.1038/170882b0. [DOI] [PubMed] [Google Scholar]
  4. Gentz R., Rauscher F. J., 3rd, Abate C., Curran T. Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains. Science. 1989 Mar 31;243(4899):1695–1699. doi: 10.1126/science.2494702. [DOI] [PubMed] [Google Scholar]
  5. HUXLEY H. E., PERUTZ M. F. Polypeptide chains in frog sartorius muscle. Nature. 1951 Jun 30;167(4261):1054–1054. doi: 10.1038/1671054a0. [DOI] [PubMed] [Google Scholar]
  6. Hope I. A., Struhl K. Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast. Cell. 1986 Sep 12;46(6):885–894. doi: 10.1016/0092-8674(86)90070-x. [DOI] [PubMed] [Google Scholar]
  7. Johnson P. F., McKnight S. L. Eukaryotic transcriptional regulatory proteins. Annu Rev Biochem. 1989;58:799–839. doi: 10.1146/annurev.bi.58.070189.004055. [DOI] [PubMed] [Google Scholar]
  8. Kouzarides T., Ziff E. The role of the leucine zipper in the fos-jun interaction. Nature. 1988 Dec 15;336(6200):646–651. doi: 10.1038/336646a0. [DOI] [PubMed] [Google Scholar]
  9. Landschulz W. H., Johnson P. F., McKnight S. L. The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite. Science. 1989 Mar 31;243(4899):1681–1688. doi: 10.1126/science.2494700. [DOI] [PubMed] [Google Scholar]
  10. Landschulz W. H., Johnson P. F., McKnight S. L. The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins. Science. 1988 Jun 24;240(4860):1759–1764. doi: 10.1126/science.3289117. [DOI] [PubMed] [Google Scholar]
  11. McLachlan A. D. The double helix coiled coil structure of murein lipoprotein from Escherichia coli. J Mol Biol. 1978 Jun 5;121(4):493–506. doi: 10.1016/0022-2836(78)90396-0. [DOI] [PubMed] [Google Scholar]
  12. Mitchell P. J., Tjian R. Transcriptional regulation in mammalian cells by sequence-specific DNA binding proteins. Science. 1989 Jul 28;245(4916):371–378. doi: 10.1126/science.2667136. [DOI] [PubMed] [Google Scholar]
  13. O'Shea E. K., Rutkowski R., Kim P. S. Evidence that the leucine zipper is a coiled coil. Science. 1989 Jan 27;243(4890):538–542. doi: 10.1126/science.2911757. [DOI] [PubMed] [Google Scholar]
  14. O'Shea E. K., Rutkowski R., Stafford W. F., 3rd, Kim P. S. Preferential heterodimer formation by isolated leucine zippers from fos and jun. Science. 1989 Aug 11;245(4918):646–648. doi: 10.1126/science.2503872. [DOI] [PubMed] [Google Scholar]
  15. Oas T. G., McIntosh L. P., O'Shea E. K., Dahlquist F. W., Kim P. S. Secondary structure of a leucine zipper determined by nuclear magnetic resonance spectroscopy. Biochemistry. 1990 Mar 27;29(12):2891–2894. doi: 10.1021/bi00464a001. [DOI] [PubMed] [Google Scholar]
  16. PAULING L., COREY R. B. Compound helical configurations of polypeptide chains: structure of proteins of the alpha-keratin type. Nature. 1953 Jan 10;171(4341):59–61. doi: 10.1038/171059a0. [DOI] [PubMed] [Google Scholar]
  17. Ransone L. J., Visvader J., Sassone-Corsi P., Verma I. M. Fos-Jun interaction: mutational analysis of the leucine zipper domain of both proteins. Genes Dev. 1989 Jun;3(6):770–781. doi: 10.1101/gad.3.6.770. [DOI] [PubMed] [Google Scholar]
  18. Schuermann M., Neuberg M., Hunter J. B., Jenuwein T., Ryseck R. P., Bravo R., Müller R. The leucine repeat motif in Fos protein mediates complex formation with Jun/AP-1 and is required for transformation. Cell. 1989 Feb 10;56(3):507–516. doi: 10.1016/0092-8674(89)90253-5. [DOI] [PubMed] [Google Scholar]
  19. Turner R., Tjian R. Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cFos-cJun heterodimers. Science. 1989 Mar 31;243(4899):1689–1694. doi: 10.1126/science.2494701. [DOI] [PubMed] [Google Scholar]
  20. Vinson C. R., Sigler P. B., McKnight S. L. Scissors-grip model for DNA recognition by a family of leucine zipper proteins. Science. 1989 Nov 17;246(4932):911–916. doi: 10.1126/science.2683088. [DOI] [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