ArticleNucleic acids research2014
Structure and DNA-binding properties of the Bacillus subtilis SpoIIIE DNA translocase revealed by single-molecule and electron microscopies.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- A safeguarding factor monitors septal pore stability to secure compartmentalization during sporulation in Bacillus subtilis.Communications biology · 2026Article
- Genomic and Biological Insights of Bacteriophage ΦBc24 TargetingCurrent issues in molecular biology · 2025Article
- Chromosome Segregation and Peptidoglycan Remodeling Are Coordinated at a Highly Stabilized Septal Pore to Maintain Bacterial Spore Development.Developmental cell · 2021Article
- Structural, Metabolic and Evolutionary Comparison of Bacterial Endospore and Exospore Formation.Frontiers in microbiology · 2021Review
- Milestones inMicrobial cell (Graz, Austria) · 2020Review
- Cohesion of Sister Chromosome Termini during the Early Stages of Sporulation in Bacillus subtilis.Journal of bacteriology · 2020Article
- Shaping an Endospore: Architectural Transformations DuringAnnual review of microbiology · 2020Review
- The FtsK-like motor TraB is a DNA-dependent ATPase that forms higher-order assemblies.The Journal of biological chemistry · 2019Article
- Single-Molecule Tracking of DNA Translocases in Bacillus subtilis Reveals Strikingly Different Dynamics of SftA, SpoIIIE, and FtsA.Applied and environmental microbiology · 2018Article
- Sequence-dependent catalytic regulation of the SpoIIIE motor activity ensures directionality of DNA translocation.Scientific reports · 2018Article
- Xer Site Specific Recombination: Double and Single Recombinase Systems.Frontiers in microbiology · 2017Review
- Missense Mutations Allow a Sequence-Blind Mutant of SpoIIIE to Successfully Translocate Chromosomes during Sporulation.PloS one · 2016Article
- Two-subunit DNA escort mechanism and inactive subunit bypass in an ultra-fast ring ATPase.eLife · 2015Article
- Assembly, translocation, and activation of XerCD-dif recombination by FtsK translocase analyzed in real-time by FRET and two-color tethered fluorophore motion.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Visualization and functional dissection of coaxial paired SpoIIIE channels across the sporulation septum.eLife · 2015Article
- Mechanistic study of classical translocation-dead SpoIIIE36 reveals the functional importance of the hinge within the SpoIIIE motor.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
SpoIIIE/FtsK are a family of ring-shaped, membrane-anchored, ATP-fuelled motors required to segregate DNA across bacterial membranes. This process is directional and requires that SpoIIIE/FtsK recognize highly skewed octameric sequences (SRS/KOPS for SpoIIIE/FtsK) distributed along the chromosome. Two models have been proposed to explain the mechanism by which SpoIIIE/FtsK interact with DNA. The loading model proposes that SpoIIIE/FtsK oligomerize exclusively on SpoIIIE recognition sequence/orienting polar sequences (SRS/KOPS) to accomplish directional DNA translocation, whereas the target search and activation mechanism proposes that pre-assembled SpoIIIE/FtsK hexamers bind to non-specific DNA, reach SRS/KOPS by diffusion/3d hopping and activate at SRS/KOPS. Here, we employ single-molecule total internal reflection imaging, atomic force and electron microscopies and ensemble biochemical methods to test these predictions and obtain further insight into the SpoIIIE-DNA mechanism of interaction. First, we find that SpoIIIE binds DNA as a homo-hexamer with neither ATP binding nor hydrolysis affecting the binding mechanism or affinity. Second, we show that hexameric SpoIIIE directly binds to double-stranded DNA without requiring the presence of SRS or free DNA ends. Finally, we find that SpoIIIE hexamers can show open and closed conformations in solution, with open-ring conformations most likely resembling a state poised to load to non-specific, double-stranded DNA. These results suggest how SpoIIIE and related ring-shaped motors may be split open to bind topologically closed DNA.
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Registered trials
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