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Related Experiment Videos

Physical interaction between proliferating cell nuclear antigen and replication factor C from Pyrococcus furiosus.

Shigeki Matsumiya1, Sonoko Ishino, Yoshizumi Ishino

  • 1Department of Structural Biology, Biomolecular Engineering Research Institute, 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|September 26, 2002
PubMed
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The crystal structure of archaeal PCNA (Proliferating Cell Nuclear Antigen) reveals a conserved ring-shaped structure. Its interaction with the PIP-box peptide is similar to human proteins, suggesting a conserved mechanism for DNA replication regulation.

Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Proliferating cell nuclear antigen (PCNA) is a key DNA polymerase processivity factor in eukaryotes.
  • PCNA interacts with numerous proteins involved in genetic information processing.
  • The toroidal, ring-shaped structure of PCNA is conserved across Eukarya and Archaea.

Purpose of the Study:

  • Determine the crystal structure of PCNA from the hyperthermophilic archaeon Pyrococcus furiosus (PfuPCNA).
  • Examine the interaction between PfuPCNA and its loading factor at the atomic level.
  • Elucidate the molecular interaction mechanism between PCNA and PCNA-binding proteins.

Main Methods:

  • Determined the crystal structure of PfuPCNA at 2.1 Å resolution.
  • Solved the crystal structure of the PfuPCNA complexed with an 11-residue peptide containing the PIP-box sequence of RFCL.

Related Experiment Videos

  • Investigated the inhibitory effect of the PIP-box peptide on PCNA-dependent primer extension.

    • Main Results:

    • The PfuPCNA structure revealed a conserved homotrimeric toroidal ring, similar to eukaryotic PCNA.
    • The crystal structure of the PfuPCNA-PIP-box peptide complex showed an interaction mode highly conserved with human PCNA.
    • PIP-box binding potentially influences the stability of the PfuPCNA ring structure through domain shifts.

    Conclusions:

    • The interaction mode between PCNA and PIP-box motifs is conserved between archaea and eukaryotes.
    • While the interaction mechanism is conserved, its functional significance may vary among different PCNA-interacting proteins.
    • PIP-box binding may enhance PCNA ring rigidity, optimizing its function in DNA replication.