Assembly of bacterial cell division protein FtsZ into dynamic biomolecular condensates
| Autor: | Silvia Zorrilla, Germán Rivas, Miguel Ángel Robles-Ramos, Begoña Monterroso, William Margolin, Carlos de Alfonso |
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| Přispěvatelé: | Ministerio de Economía y Competitividad (España), Ministerio de Ciencia e Innovación (España), National Institutes of Health (US), Agencia Estatal de Investigación (España), European Commission, Zorrilla, Silvia [0000-0002-6309-9058], Alfonso, Carlos [0000-0001-7165-4800], Margolin, William [0000-0001-6557-7706], Rivas, Germán [0000-0003-3450-7478], Monterroso, Begoña [0000-0003-2538-084X], Zorrilla, Silvia, Alfonso, Carlos, Margolin, William, Rivas, Germán, Monterroso, Begoña |
| Rok vydání: | 2021 |
| Předmět: |
Cytoplasm
GTP' Cell division Microfluidics Phase separation macromolecular substances physiological processes Guanosine Diphosphate Article Bacterial cell structure 03 medical and health sciences Bacterial Proteins Protein Domains Nephelometry and Turbidimetry Escherichia coli Nucleoid Subcellular organization FtsZ Molecular Biology Sequence Deletion 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry A protein Cell Biology Microfluidic Analytical Techniques Bacterial Processes Cytoskeletal Proteins Microscopy Fluorescence Membraneless compartments biology.protein Biophysics bacteria biological phenomena cell phenomena and immunity Protein Multimerization Macromolecular crowding Cytokinesis |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname Biochim Biophys Acta Mol Cell Res |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2021.118986 |
| Popis: | 28 p.- 6 fig. Biomolecular condensation through phase separation may be a novel mechanism to regulate bacterial processes,including cell division. Previous work revealed that FtsZ, a protein essential for cytokinesis in most bacteria,forms biomolecular condensates with SlmA, a protein that protects the chromosome from damage inflicted by the division machinery in Escherichia coli. The absence of condensates composed solely of FtsZ under the conditions used in that study suggested this mechanism was restricted to nucleoid occlusion by SlmA or to bacteria containing this protein. Here we report that FtsZ alone, under physiologically relevant conditions, can demix into condensates in bulk and when encapsulated in synthetic cell-like systems generated by microfluidics. Condensate assembly depends on FtsZ being in the GDP-bound state and on conditions mimicking the crowded environment of the cytoplasm that promote its oligomerization. Condensates are dynamic and reversibly convert into filaments upon GTP addition. Notably, FtsZ lacking its C-terminal disordered region, a structural element likely to favor biomolecular condensation, also forms condensates, albeit less efficiently. The inherent tendency of FtsZ to form condensates susceptible to modulation by physiological factors, including binding partners, suggests that such mechanisms may play a more general role in bacterial division than initially envisioned. This work was supported by the Spanish Ministerio de Economía y Competitividad (BFU2014-52070-C2-2-P and BFU2016-75471-C2-1-P,AEI/FEDER, UE, to G.R.), by the Spanish Ministerio de Ciencia e Innovación(2019AEP088 and PID2019-104544GB-100/ AEI/ 10.13039/501100011033, to G.R. and S.Z.), and by the National Institutes of Health (GM131705, to W.M.). M.Á.R.-R. was supported by the Agencia Estatal de Investigación and the European Social Fund through grant BES-2017-082003. |
| Databáze: | OpenAIRE |
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