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Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.


ABSTRACT: 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.

SUBMITTER: Heo DH 

PROVIDER: S-EPMC8441049 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature

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Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.

Heo Dong-Hyuk DH   Kuś Krzysztof K   Grzechnik Pawel P   Tan-Wong Sue Mei SM   Birot Adrien A   Kecman Tea T   Nielsen Soren S   Zenkin Nikolay N   Vasiljeva Lidia L  

Cell reports 20210901 10


Phosphorylation of the RNA polymerase II C-terminal domain Y<sub>1</sub>S<sub>2</sub>P<sub>3</sub>T<sub>4</sub>S<sub>5</sub>P<sub>6</sub>S<sub>7</sub> 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 phosphory  ...[more]

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