ArticleeLife2018
Mechanochemical coupling and bi-phasic force-velocity dependence in the ultra-fast ring ATPase SpoIIIE.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Connecting the dots: key insights on ParB for chromosome segregation from single-molecule studies.FEMS microbiology reviews · 2024Review
- Dynamic ParB-DNA interactions initiate and maintain a partition condensate for bacterial chromosome segregation.Nucleic acids research · 2023Article
- Membrane fission during bacterial spore development requires cellular inflation driven by DNA translocation.Current biology : CB · 2022Article
- Optical tweezers in single-molecule biophysics.Nature reviews. Methods primers · 2021Article
- Milestones inMicrobial cell (Graz, Austria) · 2020Review
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Multi-subunit ring-shaped ATPases are molecular motors that harness chemical free energy to perform vital mechanical tasks such as polypeptide translocation, DNA unwinding, and chromosome segregation. Previously we reported the intersubunit coordination and stepping behavior of the hexameric ring-shaped ATPase SpoIIIE (Liu et al., 2015). Here we use optical tweezers to characterize the motor's mechanochemistry. Analysis of the motor response to external force at various nucleotide concentrations identifies phosphate release as the likely force-generating step. Analysis of SpoIIIE pausing indicates that pauses are off-pathway events. Characterization of SpoIIIE slipping behavior reveals that individual motor subunits engage DNA upon ATP binding. Furthermore, we find that SpoIIIE's velocity exhibits an intriguing bi-phasic dependence on force. We hypothesize that this behavior is an adaptation of ultra-fast motors tasked with translocating DNA from which they must also remove DNA-bound protein roadblocks. Based on these results, we formulate a comprehensive mechanochemical model for SpoIIIE.
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Registered trials
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