4
Views
11
CrossRef citations to date
0
Altmetric
Transcriptional Regulation

Highly Conserved Residues in the bZIP Domain of Yeast GCN4 Are Not Essential for DNA Binding

&
Pages 4918-4926 | Received 21 May 1991, Accepted 11 Jul 1991, Published online: 31 Mar 2023

References

  • Agre, P., P. F. Johnson, and S. L. McKnight. 1989. Cognate DNA binding specificity retained after leucine zipper exchange between GCN4 and C/EBP. Science 246:922-926.
  • Arndt, K., and G. Fink. 1986. GCN4 protein, a positive transcription factor in yeast, binds general control promoters at all 5′ TGACTC 3′ sequences. Proc. Natl. Acad. Sci. USA 83:8516-8520.
  • Brunelle, A., and R. F. Schleif. 1987. Missing contact probing of DNA-protein interactions. Proc. Natl. Acad. Sci. USA 84:6673-6676.
  • Collart, M., and K. Struhl. Unpublished data.
  • Dubendorff, J. W., P. L. deHaseth, M. S. Rosendahl, and M. H. Caruthers. 1987. DNA functional groups required for formation of open complexes between E. coli RNA polymerase and the λ PR promoter. J. Biol. Chem. 262:892-898.
  • Gentz, R., F. I. Rauscher, C. Abate, and T. Curran. 1989. Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains. Science 243:1695-1699.
  • Hill, D. E., I. A. Hope, J. P. Macke, and K. Struhl. 1986. Saturation mutagenesis of the yeast HIS3 regulatory site: requirements for transcriptional induction and for binding by GCN4 activator protein. Science 234:451-457.
  • Himmelfarb, H. J., J. Pearlberg, D. H. Last, and M. Ptashne. 1990. GAL11P: a yeast mutation that potentiates the effect of weak GAL4-derived activators. Cell 63:1299-1309.
  • Hinnebusch, A. G. 1984. Evidence for translational regulation of the activator of general amino acid control in yeast. Proc. Natl. Acad. Sci. USA 81:6442-6446.
  • Hope, I. A., and K. Struhl. 1985. GCN4 protein, synthesized in vitro, binds to HIS3 regulatory sequences: implications for the general control of amino acid biosynthetic genes in yeast. Cell 43:177-188.
  • Hope, I. A., and K. Struhl. 1986. Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast. Cell 46:885-894.
  • Hope, I. A., and K. Struhl. 1987. GCN4, a eukaryotic transcriptional activator protein, binds as a dimer to target DNA. EMBO J. 6:2781-2784.
  • Jordan, S. R., and C. O. Pabo. 1988. Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions. Science 242:893-899.
  • Kouzarides, T., and E. Ziff. 1988. The role of the leucine zipper in the fos-jun interaction. Nature (London) 336:646-651.
  • Kouzarides, T., and E. Ziff. 1989. Leucine zippers of fos, jun, and GCN4 dictate dimerization specificity and thereby control DNA binding. Nature (London) 340:568-571.
  • Landschulz, W. H., P. F. Johnson, and S. L. McKnight. 1989. The DNA binding domain of the rat liver nuclear protein C/EBP is bipartite. Science 243:1681-1688.
  • Nishizawa, M., Y. Suzuki, Y. Nogi, K. Matsumoto, and T. Fukasawa. 1990. Yeast GAL11 protein mediates the transcriptional activation signal of two different transacting factors, GAL4 and general regulatory factor 1/repressor/activator site binding protein 1/translation upstream factor. Proc. Natl. Acad. Sci. USA 87:5373-5377.
  • Oliphant, A. R., C. J. Brandi, and K. Struhl. 1989. Defining sequence specificity of DNA-binding proteins by selecting binding sites from random-sequence oligonucleotides: analysis of the yeast GCN4 protein. Mol. Cell. Biol. 9:2944-2949.
  • Oliphant, A. R., A. L. Nussbaum, and K. Struhl. 1986. Cloning of random-sequence oligodeoxynucleotides. Gene 44:177-183.
  • O’Neil, K. T., R. H. Hoess, and W. F. DeGrado. 1990. Design of DNA-binding peptides based on the leucine zipper motif. Science 249:774-778.
  • O’Shea, E. K., R. Rutkowski, and P. S. Kim. 1989. Evidence that the leucine zipper is a coiled coil. Science 243:538-542.
  • Pu, W. T., and K. Struhl. 1991. The leucine zipper symmetrically positions the adjacent basic regions for specific binding to DNA. Proc. Natl. Acad. Sci. USA 88:6901-6905.
  • Reidhaar-Olson, J. F., and R. T. Sauer. 1988. Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences. Science 241:53-57.
  • Richardson, J. S., and D. C. Richardson. 1988. Amino acid preferences for specific locations at ends of a helices. Science 240:1648-1652.
  • Risse, G., K. Jooss, M. Neuberg, H.-J. Bruller, and R. Muller. 1989. Asymmetrical recognition of the palindromic AP1 binding site (TRE) by Fos protein complexes. EMBO J. 8:3825-3832.
  • Sellers, J. W., and K. Struhl. 1989. Changing fos oncoprotein to a DNA-binding protein with GCN4 dimerization specificity by swapping "leucine zippers". Nature (London) 341:74-76.
  • Sellers, J. W., A. C. Vincent, and K. Struhl. 1990. Mutations that define the optimal half-site for binding yeast GCN4 activator protein and identify an ATF/CREB-like repressor that recognizes similar DNA sites. Mol. Cell. Biol. 10:5077-5086.
  • Struhl, K. 1987. The DNA-binding domains of the jun oncoprotein and the yeast GCN4 transcriptional activator are functionally homologous. Cell 50:841-846.
  • Takeda, Y., A. Sarai, and V. M. Rivera. 1989. Analysis of sequence-specific interactions between Cro repressor and operator DNA by systematic base substitution experiments. Proc. Natl. Acad. Sci. USA 86:439-443.
  • Talanian, R. V., C. J. McKnight, and P. S. Kim. 1990. Sequence-specific DNA binding by a short peptide dimer. Science 249:769-771.
  • Turner, R., and R. Tjian. 1989. Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cFos-cJun heterodimers. Science 243:1689-1694.
  • Tzamarias, D., W. T. Pu, and K. Struhl. Submitted for publication.
  • Vinson, C. R., P. B. Sigler, and S. L. McKnight. 1989. Scissorsgrip model for DNA recognition by a family of leucine zipper proteins. Science 246:911-916.
  • Weiss, M. A., T. Ellenberger, C. R. Wobbe, J. P. Lee, S. C. Harrison, and K. Struhl. 1990. Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA. Nature (London) 347:575-578.
  • Wharton, R. P., and M. Ptashne. 1987. A new-specificity mutant of 434 repressor that defines an amino acid-base pair contact. Nature (London) 326:888-891.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.