p15PAF binding to PCNA modulates the DNA sliding surface

• Published in: Nucleic acids research Vol. 46; no. 18; pp. 9816 - 9828
• Main Authors: De March, Matteo, Barrera-Vilarmau, Susana, Crespan, Emmanuele, Mentegari, Elisa, Merino, Nekane, Gonzalez-Magaña, Amaia, Romano-Moreno, Miguel, Maga, Giovanni, Crehuet, Ramon, Onesti, Silvia, Blanco, Francisco J, De Biasio, Alfredo
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 12.10.2018
• Subjects: Carrier Proteins - chemistry; Carrier Proteins - genetics; Crystallography, X-Ray; DNA - chemistry; DNA - genetics; DNA Polymerase III - chemistry; DNA Polymerase III - genetics; DNA Replication - genetics; DNA-Directed DNA Polymerase - chemistry; DNA-Directed DNA Polymerase - genetics; Escherichia coli - genetics; Holoenzymes - chemistry; Holoenzymes - genetics; Humans; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - genetics; Magnetic Resonance Spectroscopy; Multiprotein Complexes - chemistry; Multiprotein Complexes - genetics; Proliferating Cell Nuclear Antigen - chemistry; Proliferating Cell Nuclear Antigen - genetics; Structural Biology

Abstract p15PAF is an oncogenic intrinsically disordered protein that regulates DNA replication and lesion bypass by interacting with the human sliding clamp PCNA. In the absence of DNA, p15PAF traverses the PCNA ring via an extended PIP-box that contacts the sliding surface. Here, we probed the ato...