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https://doi.org/10.7554/eLife.30927
Title: | Bacterial fumarase and L-malic acid are evolutionary ancient components of the DNA damage response | Authors: | Singer, E Silas, Y.B.H Ben-Yehuda, S Pines, O |
Keywords: | fumarate hydratase malic acid bacterial DNA bacterial protein fumarate hydratase malic acid 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 Bacillus subtilis Bacterial Proteins DNA Damage DNA Restriction Enzymes DNA, Bacterial Fumarate Hydratase Genetic Complementation Test Malates Protein Binding Saccharomyces cerevisiae |
Issue Date: | 2017 | Citation: | Singer, E, Silas, Y.B.H, Ben-Yehuda, S, Pines, O (2017). Bacterial fumarase and L-malic acid are evolutionary ancient components of the DNA damage response. eLife 6 : e30927. ScholarBank@NUS Repository. https://doi.org/10.7554/eLife.30927 | Abstract: | Fumarase is distributed between two compartments of the eukaryotic cell. The enzyme catalyses the reversible conversion of fumaric to L-malic acid in mitochondria as part of the tricarboxylic acid (TCA) cycle, and in the cytosol/nucleus as part of the DNA damage response (DDR). Here, we show that fumarase of the model prokaryote Bacillus subtilis (Fum-bc) is induced upon DNA damage, co-localized with the bacterial DNA and is required for the DDR. Fum-bc can substitute for both eukaryotic functions in yeast. Furthermore, we found that the fumarasedependent intracellular signaling of the B. subtilis DDR is achieved via production of L-malic acid, which affects the translation of RecN, the first protein recruited to DNA damage sites. This study provides a different evolutionary scenario in which the dual function of the ancient prokaryotic fumarase, led to its subsequent distribution into different cellular compartments in eukaryotes. © Singer et al. | Source Title: | eLife | URI: | https://scholarbank.nus.edu.sg/handle/10635/175194 | ISSN: | 2050084X | DOI: | 10.7554/eLife.30927 |
Appears in Collections: | Elements Staff Publications |
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