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

Author

Listed:
  • Mi-Sun Kang

    (Center for Genomic Integrity, Institute for Basic Science)

  • Eunjin Ryu

    (Center for Genomic Integrity, Institute for Basic Science
    School of Life Sciences, Ulsan National Institute of Science and Technology)

  • 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
    School of Life Sciences, Ulsan National Institute of Science and Technology)

  • Jinwoo Kim

    (Center for Genomic Integrity, Institute for Basic Science
    School of Life Sciences, Ulsan National Institute of Science and Technology)

  • 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
    School of Life Sciences, Ulsan National Institute of Science and Technology)

  • Sukhyun Kang

    (Center for Genomic Integrity, Institute for Basic Science)

  • Kyungjae Myung

    (Center for Genomic Integrity, Institute for Basic Science
    School of Life Sciences, Ulsan National Institute of Science and Technology)

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.

Suggested Citation

  • 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 & Kyung, 2019. "Regulation of PCNA cycling on replicating DNA by RFC and RFC-like complexes," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10376-w
    DOI: 10.1038/s41467-019-10376-w
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    Cited by:

    1. Javier Zamarreño & Sofía Muñoz & Esmeralda Alonso-Rodríguez & Macarena Alcalá & Sergio Rodríguez & Rodrigo Bermejo & María P. Sacristán & Avelino Bueno, 2024. "Timely lagging strand maturation relies on Ubp10 deubiquitylase-mediated PCNA dissociation from replicating chromatin," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Tanay Thakar & Ashna Dhoonmoon & Joshua Straka & Emily M. Schleicher & Claudia M. Nicolae & George-Lucian Moldovan, 2022. "Lagging strand gap suppression connects BRCA-mediated fork protection to nucleosome assembly through PCNA-dependent CAF-1 recycling," Nature Communications, Nature, vol. 13(1), pages 1-19, December.

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