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To investigate the helicase activity of redox-dependent E. coli UvrD dimers compared to monomers.

BPS2026 – Cross-linked E. coli UvrD dimers are constitutively activated helicases and show increased ssDNA translocation processivity

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To investigate the helicase activity of redox-dependent E. coli UvrD dimers compared to monomers.
Used E. coli UvrD mutant (R421C) for dimer formation.
Assessed ssDNA translocation and DNA unwinding activities.
Employed ensemble (stopped-flow) and single molecule (LUMICKS C-Trap) methods.
Cross-linked UvrD dimers showed higher ssDNA translocation processivity than monomers.
UvrD dimers exhibited enhanced unwinding activity compared to un-crosslinked dimers.
Monomers displayed no detectable DNA unwinding.

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Experiments demonstrate increased ssDNA translocation and unwinding in redox-activated E. coli UvrD dimers, suggesting novel helicase efficiency.

Mersch et al. (2026) studied this question.

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Experiments demonstrate increased ssDNA translocation and unwinding in redox-activated E. coli UvrD dimers, suggesting novel helicase efficiency.