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Título: | Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads |
Autor: | Sobrinos-Sanguino, Marta CSIC ORCID ; Zorrilla, Silvia CSIC ORCID ; Monterroso, Begoña CSIC ORCID ; Minton, Allen P.; Rivas, Germán CSIC ORCID CVN | Fecha de publicación: | 20-oct-2017 | Editor: | Nature Publishing Group | Citación: | Scientific Reports 7: 13707 (2017) | Resumen: | ZipA protein from Escherichia coli is one of the essential components of the division proto-ring that provides membrane tethering to the septation FtsZ protein. A sedimentation assay was used to measure the equilibrium binding of FtsZ-GDP and FtsZ-GTP to ZipA immobilized at controlled densities on the surface of microbeads coated with a phospholipid mixture resembling the composition of E. coli membrane. We found that for both nucleotide-bound species, the amount of bound FtsZ exceeds the monolayer capacity of the ZipA immobilized beads at high concentrations of free FtsZ. In the case of FtsZ-GDP, equilibrium binding does not appear to be saturable, whereas in the case of FtsZ-GTP equilibrium binding appears to be saturable. The difference between the two modes of binding is attributed to the difference between the composition of oligomers of free FtsZ-GDP and free FtsZ-GTP formed in solution. | Descripción: | 9 p.-6 fig. | Versión del editor: | http://dx.doi.org/10.1038/s41598-017-14160-y | URI: | http://hdl.handle.net/10261/158725 | DOI: | 10.1038/s41598-017-14160-y | ISSN: | 2045-2322 | E-ISSN: | 2045-2322 |
Aparece en las colecciones: | (CIB) Artículos |
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Scientific Reports 2017.pdf | Artículo principal | 1,79 MB | Adobe PDF | Visualizar/Abrir |
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