FACT Assists Base Excision Repair by Boosting the Remodeling Activity of RSC

• Main Authors: Charles Richard J.L., Shukla M.S., Menoni H., Ouararhni K., Lone I.N., Roulland Y., Papin C., Ben Simon E., Kundu T., Hamiche A., Angelov D., Dimitrov S.
• Other Authors: CANCER SCIENCE INSTITUTE OF SINGAPORE
• Format: Article
• Published: Public Library of Science 2020
• Subjects: nucleoplasmin; uracil DNA glycosidase; chromatin; DNA binding protein; high mobility group protein; histone; nonhistone protein; nucleosome; RSC complex, S cerevisiae; Saccharomyces cerevisiae protein; SSRP1 protein, human; SWI-SNF-B chromatin-remodeling complex; transcription elongation factor; transcription factor; uracil; antibody affinity; Article; centrifugation; chromatin assembly and disassembly; controlled study; dissociation; DNA histone interaction; DNA repair; excision repair; human; human cell; hydrolysis; immunoprecipitation; in vivo study; mass spectrometry; molecular docking; molecular dynamics; oxidative stress; protein analysis; protein domain; protein footprinting; protein function; protein protein interaction; protein purification; Western blotting; animal; biosynthesis; DNA damage; genetic transcription; genetics; HeLa cell line; metabolism; Saccharomyces cerevisiae; Xenopus laevis; Animals; Chromatin; Chromatin Assembly and Disassembly; Chromosomal Proteins, Non-Histone; DNA Damage; DNA Repair; DNA-Binding Proteins; HeLa Cells; High Mobility Group Proteins; Histones; Humans; Nucleosomes; Oxidative Stress; Saccharomyces cerevisiae Proteins; Transcription Factors; Transcription, Genetic; Transcriptional Elongation Factors; Uracil
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/165384
• Institution: National University of Singapore

10.1371/journal.pgen.1006221