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  Membrane mediated phase separation of the bacterial nucleoid occlusion protein Noc

Babl, L., Salomon, A. M., Kanwa, N., & Schwille, P. (2022). Membrane mediated phase separation of the bacterial nucleoid occlusion protein Noc. Scientific Reports, 12(1): 17949. doi:10.1038/s41598-022-22680-5.

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 Creators:
Babl, Leon1, 2, Author           
Salomon, A. Merino1, 2, Author           
Kanwa, Nishu1, Author           
Schwille, Petra1, Author           
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
2IMPRS-ML: Martinsried, Max Planck Institute of Biochemistry, Max Planck Society, ou_3531125              

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Free keywords: CELL-DIVISION; LIQUID-PHASE; Z-RING; FTSZ; DNA; MICROCOMPARTMENTATION; ASSOCIATION; TRANSITION; VESICLES; MONOMERScience & Technology - Other Topics;
 Abstract: Liquid-liquid phase separation is a fundamental biophysical process to organize eukaryotic and prokaryotic cytosols. While many biomolecular condensates are formed in the vicinity of, or even on lipid membranes, little is known about the interaction of protein condensates and lipid bilayers. In this study, we characterize the recently unknown phase behavior of the bacterial nucleoid occlusion protein Noc. We find that, similarly to other ParB-like proteins, CTP binding tightly regulates Noc's propensity to phase separate. As CTP-binding and hydrolysis also allows Noc to bind and spread on membranes, we furthermore establish Noc condensates as model system to investigate how lipid membranes can influence protein condensation and vice versa. Last, we show that Noc condensates can recruit FtsZ to the membrane, while this does not happen in the non-phase separated state. These findings suggest a new model of Noc mediated nucleoid occlusion, with membrane-mediated liquid-liquid phase separation as underlying principle of complex formation and regulation thereof.

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Language(s): eng - English
 Dates: 2022-10-26
 Publication Status: Published online
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
 Creator(s):
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 12 (1) Sequence Number: 17949 Start / End Page: - Identifier: ISSN: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322