| Autor: |
Martin BJE; Department of Biochemistry and Molecular Biology, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada., Brind'Amour J; Department of Medical Genetics, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada., Kuzmin A; Department of Biochemistry and Molecular Biology, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada., Jensen KN; Department of Medical Genetics, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada., Liu ZC; Department of Biochemistry and Molecular Biology, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada., Lorincz M; Department of Medical Genetics, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada., Howe LJ; Department of Biochemistry and Molecular Biology, Life Sciences Institute, Molecular Epigenetics Group, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC, V6T 1Z3, Canada. ljhowe@mail.ubc.ca. |
| Abstrakt: |
Histone acetylation is a ubiquitous hallmark of transcription, but whether the link between histone acetylation and transcription is causal or consequential has not been addressed. Using immunoblot and chromatin immunoprecipitation-sequencing in S. cerevisiae, here we show that the majority of histone acetylation is dependent on transcription. This dependency is partially explained by the requirement of RNA polymerase II (RNAPII) for the interaction of H4 histone acetyltransferases (HATs) with gene bodies. Our data also confirms the targeting of HATs by transcription activators, but interestingly, promoter-bound HATs are unable to acetylate histones in the absence of transcription. Indeed, HAT occupancy alone poorly predicts histone acetylation genome-wide, suggesting that HAT activity is regulated post-recruitment. Consistent with this, we show that histone acetylation increases at nucleosomes predicted to stall RNAPII, supporting the hypothesis that this modification is dependent on nucleosome disruption during transcription. Collectively, these data show that histone acetylation is a consequence of RNAPII promoting both the recruitment and activity of histone acetyltransferases. |
