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Lookup NU author(s): Dr Soren Nielsen, Professor Nikolay ZenkinORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2021 The Author(s). Phosphorylation of the RNA polymerase II C-terminal domain Y1S2P3T4S5P6S7 consensus sequence coordinates key events during transcription, and its deregulation leads to defects in transcription and RNA processing. Here, we report that the histone deacetylase activity of the fission yeast Hos2/Set3 complex plays an important role in suppressing cryptic initiation of antisense transcription when RNA polymerase II phosphorylation is dysregulated due to the loss of Ssu72 phosphatase. Interestingly, although single Hos2 and Set3 mutants have little effect, loss of Hos2 or Set3 combined with ssu72Δ results in a synergistic increase in antisense transcription globally and correlates with elevated sensitivity to genotoxic agents. We demonstrate a key role for the Ssu72/Hos2/Set3 mechanism in the suppression of cryptic antisense transcription at the 3′ end of convergent genes that are most susceptible to these defects, ensuring the fidelity of gene expression within dense genomes of simple eukaryotes.
Author(s): Heo D-H, Kuś K, Grzechnik P, Tan-Wong SM, Birot A, Kecman T, Nielsen S, Zenkin N, Vasiljeva L
Publication type: Article
Publication status: Published
Journal: Cell Reports
Year: 2021
Volume: 36
Issue: 10
Print publication date: 07/09/2021
Online publication date: 07/09/2021
Acceptance date: 13/08/2021
Date deposited: 07/02/2025
ISSN (electronic): 2211-1247
Publisher: Cell Press
URL: https://doi.org/10.1016/j.celrep.2021.109671
DOI: 10.1016/j.celrep.2021.109671
Data Access Statement: All raw sequencing data used in this study were deposited at GEO under accession numbers GEO: GSE144603 and GEO: GSE171307. They are publicly available as of the date of publication. Accession number is also listed in the Key resources table. This study did not generate any code. Any additional information required to reanalyse the data reported in this paper is available from the Lead Contact upon request.
PubMed id: 34496258
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