ATAD5-BAZ1B interaction modulates PCNA ubiquitination during DNA repair

Yeongjae Kim, Na Young Ha, Mi-Sun Kang, Eunjin Ryu, Geunil Yi, Juyeong Yoo, Nalae Kang, Byung-Gyu Kim, Kyungjae Myung and Sukhyun Kang ()
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Yeongjae Kim: Institute for Basic Science
Na Young Ha: Institute for Basic Science
Mi-Sun Kang: Institute for Basic Science
Eunjin Ryu: Institute for Basic Science
Geunil Yi: Institute for Basic Science
Juyeong Yoo: Institute for Basic Science
Nalae Kang: Institute for Basic Science
Byung-Gyu Kim: Institute for Basic Science
Kyungjae Myung: Institute for Basic Science
Sukhyun Kang: Institute for Basic Science

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract Mono-ubiquitinated PCNA (mono-Ub-PCNA) is generated when replication forks encounter obstacles, enabling the bypass of DNA lesions. After resolving stalled forks, Ub-PCNA must be de-ubiquitinated to resume high-fidelity DNA synthesis. ATAD5, in cooperation with the UAF1-USP1 complex, is responsible for this de-ubiquitination. However, the precise regulation of timely Ub-PCNA de-ubiquitination remains unclear. Our research reveals that BAZ1B, a regulatory subunit of the BAZ1B-SMARCA5 chromatin-remodeling complex (also known as the WICH complex), plays a crucial role in fine-tuning the de-ubiquitination process of Ub-PCNA. The BAZ1B binding region of ATAD5 encompasses the UAF1-binding domain of ATAD5. Disruption of the ATAD5-BAZ1B interaction results in premature de-ubiquitination of Ub-PCNA following treatment with hydrogen peroxide. Cells with impaired BAZ1B binding to ATAD5 display increased sensitivity to oxidative stress compared to wild-type cells. These findings suggest that BAZ1B prevents premature Ub-PCNA de-ubiquitination, thereby safeguarding genome integrity.

Date: 2024
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DOI: 10.1038/s41467-024-55005-3

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