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Transcriptional elongation control of hypoxic response

Shimaa Soliman, Marta Iwanaszko, Bin Zheng, Sarah Gold, Benjamin Charles Howard, Madhurima Das, Ram Prosad Chakrabarty, Navdeep S. Chandel, Ali Shilatifard

2024Proceedings of the National Academy of Sciences11 citationsDOIOpen Access PDF

Abstract

The release of paused RNA polymerase II (RNAPII) from promoter-proximal regions is tightly controlled to ensure proper regulation of gene expression. The elongation factor PTEF-b is known to release paused RNAPII via phosphorylation of the RNAPII C-terminal domain by its cyclin-dependent kinase component, CDK9. However, the signal and stress-specific roles of the various RNAPII-associated macromolecular complexes containing PTEF-b/CDK9 are not yet clear. Here, we identify and characterize the CDK9 complex required for transcriptional response to hypoxia. Contrary to previous reports, our data indicate that a CDK9 complex containing BRD4 but not AFF1/4 is essential for this hypoxic stress response. We demonstrate that BRD4 bromodomains (BET) are dispensable for the release of paused RNAPII at hypoxia-activated genes and that BET inhibition by JQ1 is insufficient to impair hypoxic gene response. Mechanistically, we demonstrate that the C-terminal region of BRD4 is required for Polymerase-Associated Factor-1 Complex (PAF1C) recruitment to establish an elongation-competent RNAPII complex at hypoxia-responsive genes. PAF1C disruption using a small-molecule inhibitor (iPAF1C) impairs hypoxia-induced, BRD4-mediated RNAPII release. Together, our results provide insight into potentially targetable mechanisms that control the hypoxia-responsive transcriptional elongation.

Topics & Concepts

BRD4RNA polymerase IIBromodomainCell biologyTranscription (linguistics)Elongation factorChemistryCyclin-dependent kinase 9GenePhosphorylationBiologyMolecular biologyGene expressionRNAProtein kinase APromoterBiochemistryAcetylationMitogen-activated protein kinase kinaseRibosomeLinguisticsPhilosophyProtein Degradation and InhibitorsUbiquitin and proteasome pathwaysCancer, Hypoxia, and Metabolism
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