A novel feature of DNA recognition: A mutant Gcn4p bZip peptide with dual DNA binding specificities dependent of half-site spacing

Journal of Molecular Biology

Volumn 286, Issue 4, 1999, Pages 983-987

  Suckow, Manfred ^a   Kisters Woike, Brigitte ^b   Hollenberg, Cornelis P ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

bZip domain; Change of specificity; Gcn4p; Palindromes; Pseudo palindromes

Indexed keywords

CYTOSINE; DNA; DNA BINDING PROTEIN; GUANINE; TRANSCRIPTION FACTOR AP 1;

AMINO TERMINAL SEQUENCE; ARTICLE; BASE PAIRING; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DNA BINDING;

EID: 0033525463     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2537     Document Type: Article

References (15)

1. Ellenberger T. E., Brandl C. J., Struhl K., Harrison S. C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: crystal structure of the protein-DNA complex. Cell. 71:1992;1223-1237.
2. Hinnebusch A. Evidence for translational regulation of the activator of general amino acid control in yeast. Proc. Natl Acad. Sci. USA. 81:1984;6442-6446.
3. Keller W., König P., Richmond T. J. Crystal structure of a bZIP/DNA complex at 2.2 Å: determinants of DNA specific recognition. J. Mol. Biol. 254:1995;657-667.
4. König P., Richmond T. J. The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J. Mol. Biol. 233:1993;139-154.
5. Lewis M., Chang G., Horton N. C., Kercher M. A., Pace H. C., Schumacher M. A., Brennan R. G., Lu P. Crystal structure of the Escherichia coli lactose operon repressor and its complexes with DNA and inducer. Science. 271:1996;1247-1254.
6. Luisi B. F., Otwinowski Z., Freedman L. P., Yamamoto K. R., Sigler P. B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature. 352:1991;497-505.
7. Pabo C. O., Sauer R. T. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61:1992;1053-1095.
8. 6binuclear cluster. Proc. Natl Acad. Sci. USA. 87:1990;2077-2081.
9. Schumacher M. A., Choi K. Y., Zalkin H., Brennan R. G. Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by α-helices. Science. 266:1994;763-770.
10. Sellers J. W., Vincent A. C., Struhl K. 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. 10:1990;5077-5086.
11. Simons A., Tils D., von Wilcken-Bergmann B., Müller-Hill B. Possible ideal lac operator: Escherichia coli lac operator-like sequences from eukaryotic genomes lack the central G·C pair. Proc. Natl Acad. Sci. USA. 81:1984;1624-1628.
12. Suckow M., Hollenberg C. P. The activation specificities of wild-type and mutant Gcn4p in vivo can be different from the DNA-binding specificities of the corresponding bZip peptides in vitro. J. Mol. Biol. 276:1998;887-902.
13. Suckow M., von Wilcken-Bergmann B., Müller-Hill B. Identification of three residues in the basic regions of the bZIP proteins GCN4, C/EBP and TAF-1 that are involved in specific DNA-binding. EMBO J. 12:1993a;1193-1200.
14. Suckow M., von Wilcken-Bergmann B., Müller-Hill B. The DNA-binding specificity of the basic region of the yeast transcriptional activator GCN4 can be changed by substitution of a single amino acid. Nucl. Acids. Res. 21:1993b;2081-2086.
15. Suckow M., Schwamborn K., Kisters-Woike B., von Wilcken-Bergmann B., Müller-Hill B. Replacement of invariant bZip residues within the basic region of the yeast transcriptional activator GCN4 can change its DNA-binding specificity. Nucl. Acids. Res. 22:1994;4395-4404.