Structure of p15PAF–PCNA complex and implications for clamp sliding during DNA replication and repair

Alfredo De Biasio (), Alain Ibáñez de Opakua, Gulnahar B. Mortuza, Rafael Molina, Tiago N. Cordeiro, Francisco Castillo, Maider Villate, Nekane Merino, Sandra Delgado, David Gil-Cartón, Irene Luque, Tammo Diercks, Pau Bernadó, Guillermo Montoya and Francisco J. Blanco ()
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Alfredo De Biasio: Structural Biology Unit, CIC bioGUNE
Alain Ibáñez de Opakua: Structural Biology Unit, CIC bioGUNE
Gulnahar B. Mortuza: Structural Biology and Biocomputing Programme, Centro Nacional de Investigaciones Oncológicas
Rafael Molina: Structural Biology and Biocomputing Programme, Centro Nacional de Investigaciones Oncológicas
Tiago N. Cordeiro: Centre de Biochimie Structurale, INSERM U1054, CNRS UMR 5048, Université Montpellier 1 and 2
Francisco Castillo: Universidad de Granada, Fuentenueva s/n
Maider Villate: Structural Biology Unit, CIC bioGUNE
Nekane Merino: Structural Biology Unit, CIC bioGUNE
Sandra Delgado: Structural Biology Unit, CIC bioGUNE
David Gil-Cartón: Structural Biology Unit, CIC bioGUNE
Irene Luque: Universidad de Granada, Fuentenueva s/n
Tammo Diercks: Structural Biology Unit, CIC bioGUNE
Pau Bernadó: Centre de Biochimie Structurale, INSERM U1054, CNRS UMR 5048, Université Montpellier 1 and 2
Guillermo Montoya: Structural Biology and Biocomputing Programme, Centro Nacional de Investigaciones Oncológicas
Francisco J. Blanco: Structural Biology Unit, CIC bioGUNE

Nature Communications, 2015, vol. 6, issue 1, 1-12

Abstract: Abstract The intrinsically disordered protein p15PAF regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15PAF–PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15PAF tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15PAF also contacts the inside of, and passes through, the PCNA ring. The disordered p15PAF termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15PAF binds DNA mainly through its histone-like N-terminal tail, while PCNA does not, and a model of the ternary complex with DNA inside the PCNA ring is consistent with electron micrographs. We propose that p15PAF acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.

Date: 2015
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DOI: 10.1038/ncomms7439

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