The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

EAF3  -  Eaf3p

Saccharomyces cerevisiae S288c

Synonyms: Chromatin modification-related protein EAF3, ESA1-associated factor 3, YP9367.03C, YPR023C
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on EAF3

  • Chromatin immunoprecipitation and biochemical experiments indicate that the chromodomain of Eaf3 recruits Rpd3C(S) to nucleosomes methylated by Set2 on histone H3 lysine 36, leading to deacetylation of transcribed regions [1].
  • Set2 functioned upstream of Rpd3S and the Eaf3 methyl-histone binding chromodomain was important for recruitment of Rpd3S and for deacetylation within the STE11 ORF [2].
  • Rco1 and Eaf3 were subunits specific to Rpd3S [2].
  • Eaf3, a component of the NuA4 histone acetylase and Rpd3 histone deacetylase complexes, is important for the global pattern of histone acetylation in Saccharomyces cerevisiae [3].
  • Lastly, Eaf3 inhibits internal initiation within mRNA coding regions in a manner similar to FACT and Spt6 [3].
 

Biological context of EAF3

  • However, the Eaf3 chromodomain and H3-K36 methylation do not significantly affect acetylation at promoters, suggesting that Eaf3 has a distinct function, presumably in the NuA4 complex [3].
  • Preferential deacetylation of coding regions requires the Eaf3 chromodomain and H3-K36 methylation by Set2 [3].
  • Specifically, the loss of Eaf3 causes increases in H3 and H4 acetylation at coding sequences and decreases at promoters, such that histone acetylation levels become evenly distributed across the genome [4].
  • Eaf3 does not affect the overall level of H4 acetylation, the recruitment of the NuA4 catalytic subunit Esa1 to target promoters, or the level of transcription of the genes analyzed for histone acetylation [4].

References

  1. Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a repressive Rpd3 complex. Keogh, M.C., Kurdistani, S.K., Morris, S.A., Ahn, S.H., Podolny, V., Collins, S.R., Schuldiner, M., Chin, K., Punna, T., Thompson, N.J., Boone, C., Emili, A., Weissman, J.S., Hughes, T.R., Strahl, B.D., Grunstein, M., Greenblatt, J.F., Buratowski, S., Krogan, N.J. Cell (2005) [Pubmed]
  2. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Carrozza, M.J., Li, B., Florens, L., Suganuma, T., Swanson, S.K., Lee, K.K., Shia, W.J., Anderson, S., Yates, J., Washburn, M.P., Workman, J.L. Cell (2005) [Pubmed]
  3. Eaf3 chromodomain interaction with methylated H3-K36 links histone deacetylation to Pol II elongation. Joshi, A.A., Struhl, K. Mol. Cell (2005) [Pubmed]
  4. Eaf3 regulates the global pattern of histone acetylation in Saccharomyces cerevisiae. Reid, J.L., Moqtaderi, Z., Struhl, K. Mol. Cell. Biol. (2004) [Pubmed]
 
WikiGenes - Universities