Faculty, Staff and Student Publications

Language

English

Publication Date

5-1-2025

Journal

International Journal of Biological Macromolecules

DOI

10.1016/j.ijbiomac.2025.142691

PMID

40174834

PMCID

PMC12756933

PubMedCentral® Posted Date

1-2-2026

PubMedCentral® Full Text Version

Author MSS

Abstract

An increasing number of proteins involved in bacterial cell cycle events have been recently shown to form biomolecular condensates important for their functions that may play a role in development of antibiotic-tolerant persister cells. Here we report that the E. coli chromosomal Ter macrodomain organizer MatP, a division site selection protein coordinating chromosome segregation with cell division, formed biomolecular condensates in crowding cytomimetic systems preferentially localized at the membrane of microfluidics droplets. Condensates were antagonized and partially dislodged from the membrane by DNA sequences recognized by MatP (matS), which partitioned into them. FtsZ, a core component of the division machinery previously described to phase-separate, unexpectedly enhanced MatP condensation. Our biophysical analyses uncovered direct interaction between both proteins, disrupted by matS. This may have potential implications for midcell FtsZ ring positioning by the Ter-linkage, which comprises MatP and two other proteins bridging the canonical MatP-FtsZ interaction. FtsZ/MatP condensates interconverted with GTP-triggered bundles, suggesting that local fluctuations of GTP concentrations may regulate FtsZ/MatP phase separation. Consistent with discrete MatP foci previously reported in cells, phase separation might influence MatP-dependent chromosome organization, spatiotemporal coordination of cytokinesis and DNA segregation, which is potentially relevant for cell entry into dormant states that can resist antibiotic treatments.

Keywords

Escherichia coli Proteins, Escherichia coli, Cell Division, Bacterial Proteins, Cytoskeletal Proteins, Biomolecular Condensates, Chromosomes, Bacterial, Protein Binding, Chromosomal Proteins, Non-Histone, Macromolecular interactions, Biophysical techniques, Phase separation

Published Open-Access

yes

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