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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
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
reverse transcription polymerase chain reaction
Saccharomyces cerevisiae
Western blotting
DNA damage
genetic complementation
Bacillus subtilis
Bacterial Proteins
DNA Damage
DNA Restriction Enzymes
DNA, Bacterial
Fumarate Hydratase
Genetic Complementation Test
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.
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
ISSN: 2050084X
DOI: 10.7554/eLife.30927
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