2023
DOI: 10.1016/j.jbc.2023.104773
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Interaction with single-stranded DNA-binding protein modulates Escherichia coli RadD DNA repair activities

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Cited by 5 publications
(2 citation statements)
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“…The helicase domain of IEE is similar to that of E. coli RadD (Figure S4). RadD binds to fork-structured DNA (Romero et al, 2020) and exhibits ATPase activity facilitated by SSB (Garcia et al, 2023). A mutation in motif I abolishes the ATPase activity of RadD and decreases its DNA-binding capacity in the presence of ATP (Chen et al, 2016).…”
Section: Strand Displacement Activity Of Iee and Its Helicase Domainmentioning
confidence: 99%
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“…The helicase domain of IEE is similar to that of E. coli RadD (Figure S4). RadD binds to fork-structured DNA (Romero et al, 2020) and exhibits ATPase activity facilitated by SSB (Garcia et al, 2023). A mutation in motif I abolishes the ATPase activity of RadD and decreases its DNA-binding capacity in the presence of ATP (Chen et al, 2016).…”
Section: Strand Displacement Activity Of Iee and Its Helicase Domainmentioning
confidence: 99%
“…Each motif is drawn based on Chaar et al (2017) and Chen et al (2015). RecA‐like domains 1 (RD1) and RD2 are highlighted light blue and light green, respectively, which was inferred from data of RadD (Garcia et al, 2023). Dots at the bottom of the aligned sequences show residues acting either as incoming nucleotide ligands (black) or a water molecule ligand (red).…”
mentioning
confidence: 94%