Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation

DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-forming CTPase ParB. The lifetime of these interactions is limited by the ParB-dependent activation of ParA ATPase activity. Here, we elucidate the functional interplay between ParA and ParB in the model bacterium Myxococcus xanthus. We demonstrate that the N-terminal ParA-binding motif of ParB associates with a conserved bipartite binding pocket at the ParA dimer interface, in a manner dependent on ParB clamp closure. Moreover, we show that ParB and non-specific DNA interact cooperatively with ParA and synergistically induce structural changes in its Walker A and Walker B motifs that correlate with the activation of ParA ATPase activity. These results advance our understanding of the mechanism underlying DNA transport by the ParABS system and may help to unravel the mode of action of related cargo-positioning systems.

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Publication Details

Journal
Nature Communications
Published
2025-09-25
DOI
https://doi.org/10.1038/s41467-025-63976-0
Citations
5
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
9.09
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article

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation

Juri Hanßmann, Christopher-Nils Mais, Bernd Simon, Martin Thanbichler et al.
5 citations
Nature Communications
Bacterial Genetics and Biotechnology
9.09
article

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation

Juri Hanßmann, Christopher-Nils Mais, Bernd Simon, Martin Thanbichler, Gert Bange, Janosch Hennig, Cecilia Perez-Borrajero, Manuel Osorio‐Valeriano, Lucas Schnabel, Markus Thamm, Wieland Steinchen
article en
5 citations

Abstract

DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-forming CTPase ParB. The lifetime of these interactions is limited by the ParB-dependent activation of ParA ATPase activity. Here, we elucidate the functional interplay between ParA and ParB in the model bacterium Myxococcus xanthus. We demonstrate that the N-terminal ParA-binding motif of ParB associates with a conserved bipartite binding pocket at the ParA dimer interface, in a manner dependent on ParB clamp closure. Moreover, we show that ParB and non-specific DNA interact cooperatively with ParA and synergistically induce structural changes in its Walker A and Walker B motifs that correlate with the activation of ParA ATPase activity. These results advance our understanding of the mechanism underlying DNA transport by the ParABS system and may help to unravel the mode of action of related cargo-positioning systems.

Nature CommunicationsVol. 16(1)
Harvard University (US), Philipps University of Marburg (DE), European Molecular Biology Laboratory (DE), Loewe Center for Synthetic Microbiology (DE), European Molecular Biology Laboratory (DE), Max Planck Institute for Terrestrial Microbiology (DE), University of Bayreuth (DE), Phillips University (US), UConn Health (US)
Openalex Percentile: Top 2%
Bacterial Genetics and Biotechnology
9.09
DOIOpen Access PDFOpenAlex
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