Regulation of PCNA cycling on replicating DNA by RFC and RFC-like complexes

Mi-Sun Kang, Eunjin Ryu, Seung-Won Lee, Jieun Park, Na Young Ha, Jae Sun Ra, Yeong Jae Kim, Jinwoo Kim, Mohamed Abdel-Rahman, Su Hyung Park, Kyoo-young Lee, Hajin Kim (), Sukhyun Kang () and Kyungjae Myung ()
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Mi-Sun Kang: Center for Genomic Integrity, Institute for Basic Science
Eunjin Ryu: Center for Genomic Integrity, Institute for Basic Science
Seung-Won Lee: School of Life Sciences, Ulsan National Institute of Science and Technology
Jieun Park: Center for Genomic Integrity, Institute for Basic Science
Na Young Ha: Center for Genomic Integrity, Institute for Basic Science
Jae Sun Ra: Center for Genomic Integrity, Institute for Basic Science
Yeong Jae Kim: Center for Genomic Integrity, Institute for Basic Science
Jinwoo Kim: Center for Genomic Integrity, Institute for Basic Science
Mohamed Abdel-Rahman: Ohio State University Comprehensive Cancer Center
Su Hyung Park: Center for Genomic Integrity, Institute for Basic Science
Kyoo-young Lee: Center for Genomic Integrity, Institute for Basic Science
Hajin Kim: Center for Genomic Integrity, Institute for Basic Science
Sukhyun Kang: Center for Genomic Integrity, Institute for Basic Science
Kyungjae Myung: Center for Genomic Integrity, Institute for Basic Science

Nature Communications, 2019, vol. 10, issue 1, 1-16

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-10376-w

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