期刊
MOLECULAR CELL
卷 79, 期 2, 页码 293-+出版社
CELL PRESS
DOI: 10.1016/j.molcel.2020.06.034
关键词
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资金
- Agence Nationale pour la Recherche (France) grant HiResBacs [ANR-15-CE11-0023]
- Agence Nationale pour la Recherche (France) grant IBM [ANR-14-CE09-0025-01]
- ECOS-Sud program [A16B01]
- Program Investissements d'Avenir'' for the Labex NUMEV integrated into the I-Site MUSE [2011-LABX-076, AAP 2013-2-005, 2015-2-055, 2016-1-024]
- European Union's Horizon 2020 Research and Innovation Program [724429]
- French National Research Agency [ANR-10-INBS-04]
- French Ministere de l'Enseignement Superieur, de la Recherche et de l'Innovation
- European Research Council (ERC) [724429] Funding Source: European Research Council (ERC)
Liquid-liquid phase-separated (LLPS) states are key to compartmentalizing components in the absence of membranes; however, it is unclear whether LLPS condensates are actively and specifically organized in the subcellular space and by which mechanisms. Here, we address this question by focusing on the ParABS DNA segregation system, composed of a centromeric-like sequence (parS), a DNA-binding protein (ParB), and a motor (ParA). We show that parS and ParB associate to form nanometer-sized, round condensates. ParB molecules diffuse rapidly within the nucleoid volume but display confined motions when trapped inside ParB condensates. Single ParB molecules are able to rapidly diffuse between different condensates, and nucleation is strongly favored by parS. Notably, the ParA motor is required to prevent the fusion of ParB condensates. These results describe a novel active mechanism that splits, segregates, and localizes non-canonical LLPS condensates in the subcellular space.
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