Cryo-EM structure of human Pol κ bound to DNA and mono-ubiquitylated PCNA

• Published in: Nature communications Vol. 12; no. 1; pp. 6095 - 14
• Main Authors: Lancey, Claudia, Tehseen, Muhammad, Bakshi, Souvika, Percival, Matthew, Takahashi, Masateru, Sobhy, Mohamed A., Raducanu, Vlad S., Blair, Kerry, Muskett, Frederick W., Ragan, Timothy J., Crehuet, Ramon, Hamdan, Samir M., De Biasio, Alfredo
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 19.10.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 631/45/147; 631/535/1258/1259; 82/83; Damage; Deoxyribonucleic acid; DNA; DNA biosynthesis; DNA damage; DNA polymerase; DNA structure; DNA-directed DNA polymerase; Docks; Domains; Humanities and Social Sciences; multidisciplinary; Nucleotides; Proliferating cell nuclear antigen; Replication; Replication forks; Science; Science (multidisciplinary); Stalling; Ubiquitin; Zinc finger proteins

Y-family DNA polymerase κ (Pol κ) can replicate damaged DNA templates to rescue stalled replication forks. Access of Pol κ to DNA damage sites is facilitated by its interaction with the processivity clamp PCNA and is regulated by PCNA mono-ubiquitylation. Here, we present cryo-EM reconstructions of...