Display options
Share it on

Microbiologyopen. 2012 Jun;1(2):105-14. doi: 10.1002/mbo3.8.

Zinc-responsive coactivator recruitment by the yeast Zap1 transcription factor.

MicrobiologyOpen

Avery G Frey, David J Eide

Affiliations

  1. Department of Nutritional Sciences, University of Wisconsin-Madison Madison, Wisconsin.

PMID: 22950018 PMCID: PMC3426420 DOI: 10.1002/mbo3.8

Abstract

The zinc-responsive Zap1 transcription factor of Saccharomyces cerevisiae controls many genes involved in zinc homeostasis. Zap1 has two activation domains, AD1 and AD2, which are independently regulated by zinc. While AD1 can fully activate most Zap1 target genes, AD2 is active only on a subset of those genes. One hypothesis explaining this promoter specificity was that AD1 and AD2 recruit different coactivators. To address this question, we carried out a genetic screen to identify coactivator complexes that are required for Zap1-mediated activation. SWI/SNF, SAGA, and Mediator complexes were implicated as playing major roles in Zap1 activation. Consistent with this conclusion, we found that these three complexes are recruited to Zap1 target promoters in a zinc-responsive and Zap1-dependent manner. Coactivator recruitment was highly interdependent such that mutations disrupting SAGA impaired recruitment of SWI/SNF and vice versa. Optimal Mediator recruitment was dependent on both SAGA and SWI/SNF. A comparison of the coactivators recruited by AD1 and AD2 found no obvious differences suggesting that recruitment of different coactivators is not likely the mechanism of AD specificity. Rather, our results suggest that AD2 recruits coactivators less effectively than AD1 and is therefore only functional on some promoters.

Keywords: Coactivators; Zap1 transcription; homeostasis; regulation; yeast; zinc

References

  1. J Biol Chem. 2009 Jul 10;284(28):18565-9 - PubMed
  2. Cell. 1993 May 21;73(4):747-60 - PubMed
  3. Yeast. 2009 Apr;26(4):205-20 - PubMed
  4. Mol Cell Biol. 2003 Apr;23(8):2800-20 - PubMed
  5. Curr Opin Genet Dev. 2003 Apr;13(2):136-42 - PubMed
  6. PLoS One. 2011;6(7):e22535 - PubMed
  7. Mol Cell Biol. 1997 Sep;17(9):5044-52 - PubMed
  8. Mol Cell. 2004 Feb 27;13(4):573-85 - PubMed
  9. Mol Cell. 2002 Aug;10(2):227-36 - PubMed
  10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5812-7 - PubMed
  11. Biochim Biophys Acta. 2010 Aug;1799(8):533-8 - PubMed
  12. Proc Natl Acad Sci U S A. 2000 Jul 5;97(14):7957-62 - PubMed
  13. J Mol Biol. 2006 Apr 7;357(4):1167-83 - PubMed
  14. Methods Enzymol. 1983;101:181-91 - PubMed
  15. Genes Dev. 1992 Jan;6(1):93-104 - PubMed
  16. Microbiol Mol Biol Rev. 2000 Jun;64(2):435-59 - PubMed
  17. Mol Cell. 2003 May;11(5):1301-9 - PubMed
  18. BMC Genomics. 2008 Aug 01;9:370 - PubMed
  19. Biochemistry. 2003 Feb 4;42(4):1053-61 - PubMed
  20. Biotechniques. 2000 Dec;29(6):1226-31 - PubMed
  21. EMBO J. 2003 Oct 1;22(19):5137-46 - PubMed
  22. J Biol Chem. 1998 Oct 30;273(44):28617-24 - PubMed
  23. EMBO J. 2000 Jul 17;19(14):3704-13 - PubMed
  24. Gene. 1986;45(3):299-310 - PubMed
  25. C R Biol. 2005 Sep;328(9):773-82 - PubMed
  26. J Biol Chem. 2011 Feb 25;286(8):6844-54 - PubMed
  27. EMBO J. 2004 Oct 13;23(20):4040-50 - PubMed
  28. Biochim Biophys Acta. 2010 May-Jun;1799(5-6):379-88 - PubMed
  29. Mol Microbiol. 2005 Aug;57(3):834-46 - PubMed
  30. Biochim Biophys Acta. 2011 Feb;1809(2):97-108 - PubMed
  31. Gene. 2003 Aug 14;313:1-16 - PubMed

Publication Types

Grant support