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Myung, Kyungjae
Center for Genomic Integrity
Research Interests
  • DNA Replication, DNA Repair, DNA Recombination, DNA Damage Response, cancer, aging

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PCNA Unloading Is Negatively Regulated by BET Proteins

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Title
PCNA Unloading Is Negatively Regulated by BET Proteins
Author
Kang, Mi-SunKim, JinwooRyu, EunjinHa, Na YoungHwang, SunyoungKim, Byung-GyuRa, Jae SunKim, Yeong JaeHwang, Jung MeMyung, KyungjaeKang, Sukhyun
Issue Date
2019-12
Publisher
Cell Press
Citation
CELL REPORTS, v.29, no.13, pp.4632 - 4645.e5
Abstract
Proliferating cell nuclear antigen (PCNA) is a DNA clamp essential for DNA replication. During DNA synthesis, PCNA is continuously loaded onto and unloaded from DNA. PCNA recruits various proteins to nascent DNA to facilitate chromosome duplication. Therefore, timely PCNA unloading is crucial for high-fidelity DNA replication. The ATAD5-RFC-like complex (ATAD5-RLC) unloads PCNA from replicated DNA. It is unclear how ATAD5-RLC activity is regulated to prevent premature PCNA unloading. Here, we find that BRD4, an acetyl-histone-binding chromatin reader, inhibits the PCNA-unloading activity of ATAD5-RLC. The BRD4 ET domain interacts with a region upstream of the ATAD5 PCNA-unloading domain. BRD4-ATAD5 binds to acetyl-histones in nascent chromatin. BRD4 release from chromatin correlates with PCNA unloading. Disruption of the interaction between BRD4 and acetyl-histones or between BRD4 and ATAD5 reduces the PCNA amount on chromatin. In contrast, the overexpression of BRD4 increases the amount of chromatin-bound PCNA. Thus, acetyl-histone-bound BRD4 fine-tunes PCNA unloading from nascent DNA.
URI
https://scholarworks.unist.ac.kr/handle/201301/30642
URL
https://www.sciencedirect.com/science/article/pii/S2211124719316377?via%3Dihub
DOI
10.1016/j.celrep.2019.11.114
ISSN
2211-1247
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