Bacterial fumarase and L-malic acid are evolutionary ancient components of the DNA damage response

• Main Authors: Singer, E, Silas, Y.B.H, Ben-Yehuda, S, Pines, O
• Other Authors: MICROBIOLOGY AND IMMUNOLOGY
• Format: Article
• Published: 2020
• Subjects: fumarate hydratase; malic acid; bacterial DNA; bacterial protein; malic acid derivative; protein binding; RecN protein, Bacteria; restriction endonuclease; Article; Bacillus subtilis; bacterial growth; bacterial strain; citric acid cycle; colony forming unit; DNA damage response; enzyme activity; fluorescence microscopy; gene mutation; gene sequence; mass fragmentography; nonhuman; reverse transcription polymerase chain reaction; Saccharomyces cerevisiae; Western blotting; DNA damage; enzymology; genetic complementation; genetics; metabolism; Bacterial Proteins; DNA Damage; DNA Restriction Enzymes; DNA, Bacterial; Fumarate Hydratase; Genetic Complementation Test; Malates; Protein Binding
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/175194
• Institution: National University of Singapore

10.7554/eLife.30927