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Originally published as Genetics Published Articles Ahead of Print on December 15, 2008.
Genetics, Vol. 181, 461-472, February 2009, Copyright © 2009
doi:10.1534/genetics.108.098897
Genetic and Genomewide Analysis of Simultaneous Mutations in Acetylated and Methylated Lysine Residues in Histone H3 in Saccharomyces cerevisiae
Yi Jin*,
Amy M. Rodriguez
and
John J. Wyrick*,,
,1
* Molecular Plant Sciences, School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, Washington 99164-4660
1 Corresponding author: Washington State University, School of Molecular Biosciences, Fulmer 675, Pullman, WA 99164-4660.
E-mail: jwyrick{at}wsu.edu
Acetylated and methylated lysine residues in histone H3 play important roles in regulating yeast gene expression and other cellular processes. Previous studies have suggested that histone H3 acetylated and methylated lysine residues may functionally interact through interdependent pathways to regulate gene transcription. A common genetic test for functional interdependence is to characterize the phenotype of a double mutant. Using this strategy, we tested the genetic interaction between histone H3 mutant alleles that simultaneously eliminate acetylated or methylated lysine residues. Our results indicate that mutation of histone H3 acetylated lysine residues alleviates growth phenotypes exhibited by the H3 methylated lysine mutant. In contrast, histone H3 acetylated and methylated lysine mutants display largely independent effects on yeast gene expression. Intriguingly, these expression changes are preferentially associated with chromosomal regions in which histone H3 lysine residues are hypoacetylated and hypomethylated. Finally, we show that the acetylated and methylated lysine mutants have strikingly different effects on the binding of Sir4 to yeast telomeres, suggesting that histone H3 acetylated lysine residues regulate yeast silencing through a mechanism independent of SIR binding.
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Genetics 2009 181: NP.
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