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Related Experiment Videos

Ssn6-Tup1 interacts with class I histone deacetylases required for repression.

A D Watson1, D G Edmondson, J R Bone

  • 1Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030, USA.

Genes & Development
|November 9, 2000
PubMed
Summary

The Ssn6-Tup1 corepressor complex in yeast interacts with histones. Histone hyperacetylation disrupts Ssn6-Tup1 function, suggesting active recruitment of histone deacetylases.

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Area of Science:

  • Molecular Biology
  • Yeast Genetics
  • Epigenetics

Background:

  • The Ssn6-Tup1 complex is a key transcriptional corepressor in yeast.
  • Tup1 directly interacts with histones H3 and H4, and this interaction is crucial for repression.
  • Histone acetylation status is known to influence transcriptional regulation.

Purpose of the Study:

  • To investigate the role of histone acetylation in Ssn6-Tup1-mediated gene repression.
  • To determine if histone deacetylase (HDAC) activity is required for Ssn6-Tup1 function.
  • To explore the physical interaction between Ssn6-Tup1 and HDACs.

Main Methods:

  • Utilizing yeast genetics to create combined mutations in histone deacetylase genes (RPD3, HOS1, HOS2).
  • Assessing Ssn6-Tup1-mediated repression in mutant strains.

Related Experiment Videos

  • Performing in vitro binding assays to study Tup1-histone interactions.
  • Investigating physical interactions between Ssn6-Tup1 components and HDACs.

    • Main Results:

    • Combined mutations in RPD3, HOS1, and HOS2 led to histone hyperacetylation and abolished Ssn6-Tup1 repression.
    • This specific combination of mutations caused simultaneous hyperacetylation of both H3 and H4.
    • Two class I HDACs were found to physically interact with the Ssn6-Tup1 complex.

    Conclusions:

    • Histone hyperacetylation disrupts Ssn6-Tup1-mediated repression in yeast.
    • Ssn6-Tup1 likely recruits histone deacetylase activity to deacetylate nucleosomes and facilitate Tup1-histone interactions.
    • This provides a mechanism for how corepressor function is modulated by epigenetic modifications.