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

Lucas Schnabel, Manuel Osorio-Valeriano (), Cecilia Perez-Borrajero, Wieland Steinchen, Christopher-Nils Mais, Bernd Simon, Juri Hanßmann, Maria Thamm, Janosch Hennig, Gert Bange and Martin Thanbichler ()
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Lucas Schnabel: Marburg University
Manuel Osorio-Valeriano: Marburg University
Cecilia Perez-Borrajero: European Molecular Biology Laboratory (EMBL)
Wieland Steinchen: Marburg University
Christopher-Nils Mais: Marburg University
Bernd Simon: European Molecular Biology Laboratory (EMBL)
Juri Hanßmann: Marburg University
Maria Thamm: Marburg University
Janosch Hennig: European Molecular Biology Laboratory (EMBL)
Gert Bange: Marburg University
Martin Thanbichler: Marburg University

Nature Communications, 2025, vol. 16, issue 1, 1-20

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-63976-0

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