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oai:repisalud.isciii.es:20.500.12105/100022024-11-29T15:08:48Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597

00925njm 22002777a 4500 dc De Biasio, Alfredo author de Opakua, Alain Ibáñez author Mortuza, Gulnahar B author Molina, Rafael author Cordeiro, Tiago N author Castillo, Francisco author Villate, Maider author Merino, Nekane author Delgado, Sandra author Gil-Cartón, David author Luque, Irene author Diercks, Tammo author Bernadó, Pau author Montoya, Guillermo author Blanco, Francisco J author 2015-03-12 The intrinsically disordered protein p15(PAF) regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15(PAF)-PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15(PAF) tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15(PAF) also contacts the inside of, and passes through, the PCNA ring. The disordered p15(PAF) termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15(PAF) 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 p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding. Nat Commun. 2015 ;6:6439 10.1038/ncomms7439 2041-1723 2041-1723 Nature communications 25762514 http://hdl.handle.net/20.500.12105/10002 Structure of p15(PAF)-PCNA complex and implications for clamp sliding during DNA replication and repair