한빛사 논문
Mi-Sun Kang1,4, Eunjin Ryu1,2,4, Seung-Won Lee2,4, Jieun Park1, Na Young Ha1, Jae Sun Ra1, Yeong Jae Kim1,2, Jinwoo Kim1,2, Mohamed Abdel-Rahman3, Su Hyung Park1, Kyoo-young Lee1, Hajin Kim1,2,*, Sukhyun Kang1,* & Kyungjae Myung1,2,*
1 Center for Genomic Integrity, Institute for Basic Science, Ulsan 44919, Republic of Korea. 2 School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 44919, Republic of Korea. 3 Department of Ophthalmology, Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA. 4 These authors contributed equally: Mi-Sun Kang, Eunjin Ryu, Seung-Won Lee
*Correspondence to Hajin Kim or Sukhyun Kang or Kyungjae Myung
Abstract
Replication-Factor-C (RFC) and RFC-like complexes (RLCs) mediate chromatin engagement of the proliferating cell nuclear antigen (PCNA). It remains controversial how RFC and RLCs cooperate to regulate PCNA loading and unloading. Here, we show the distinct PCNA loading or unloading activity of each clamp loader. ATAD5-RLC possesses the potent PCNA unloading activity. ATPase motif and collar domain of ATAD5 are crucial for the unloading activity. DNA structures did not affect PCNA unloading activity of ATAD5-RLC. ATAD5-RLC could unload ubiquitinated PCNA. Through single molecule measurements, we reveal that ATAD5-RLC unloaded PCNA through one intermediate state before ATP hydrolysis. RFC loaded PCNA through two intermediate states on DNA, separated by ATP hydrolysis. Replication proteins such as Fen1 could inhibit the PCNA unloading activity of Elg1-RLC, a yeast homolog of ATAD5-RLC in vitro. Our findings provide molecular insights into how PCNA is released from chromatin to finalize DNA replication/repair.
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