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PCNA Structure and Interactions with Partner Proteins

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Molecular Life Sciences

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Synopsis

Proliferating cell nuclear antigen (PCNA) consists of three identical monomers that topologically encircle double-stranded DNA. PCNA stimulates the processivity of DNA polymerase δ and, to a less extent, the intrinsically highly processive DNA polymerase ε. It also functions as a platform that recruits and coordinates the activities of a large number of DNA processing proteins. Emerging structural and biochemical studies suggest that the nature of PCNA-partner proteins interactions is complex. A hydrophobic groove at the front side of PCNA serves as a primary docking site for the consensus PIP box motifs present in many PCNA-binding partners. Sequences that immediately flank the PIP box motif or regions that are distant from it could also interact with the hydrophobic groove and other regions of PCNA. Posttranslational modifications on the backside of PCNA could add another dimension to its interaction with partner proteins. An encounter of PCNA with different DNA structures...

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Author information

Authors and Affiliations

  1. Division of Biological and Environmental Sciences and Engineering, Laboratory of DNA Replication and Recombination, King Abdullah University of Science and Technology (KAUST), 23955-6900, Thuwal, Saudi Arabia

    Muse Oke, Manal S. Zaher & Samir M. Hamdan

Authors
  1. Muse Oke
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  2. Manal S. Zaher
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  3. Samir M. Hamdan
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Corresponding author

Correspondence to Samir M. Hamdan .

Editor information

Editors and Affiliations

  1. Texas A&M University, College Station, TX, USA

    Robert D. Wells

  2. Penn State College of Medicine, Hershey, PA, USA

    Judith S. Bond

  3. University of California, Berkeley, CA, USA

    Judith Klinman

  4. University of Texas Health Science Center, San Antonio, TX, USA

    Bettie Sue Siler Masters

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Oke, M., Zaher, M.S., Hamdan, S.M. (2018). PCNA Structure and Interactions with Partner Proteins. In: Wells, R.D., Bond, J.S., Klinman, J., Masters, B.S.S. (eds) Molecular Life Sciences. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-1531-2_138

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