English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance This study develops and exploits an expanded single-molecule fluorescence technique to understand the molecular mechanism of assembly, translocation, and disassembly of a hexameric DNA motor, FtsK, which functions ubiquitously in bacterial chromosome segregation. Assembly of single hexamers on DNA and their subsequent rapid translocation were directly assayed. FtsK hexamers dissociated soon after encountering and activating XerCD-dif recombination complexes. This work contrasts with previously published reports, which suggested that FtsK can reverse spontaneously during translocation, or upon encountering XerCD-dif . Furthermore, in some previous assays, the readout was DNA looping; here, we show that looping does not occur with single hexamer translocation. The technique used provides a blueprint for mechanistic real-time studies of individual protein–nucleic acid complexes.

proceedings of the national academy of sciences of the united states of america

Assembly, translocation, and activation of XerCD- <i>dif</i> recombination by FtsK translocase analyzed in real-time by FRET and two-color tethered fluorophore motion

Assembly, translocation, and activation of XerCD- dif recombination by FtsK translocase analyzed in real-time by FRET and two-color tethered fluorophore motion