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Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads

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 t...

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Autores principales: Sobrinos-Sanguino, Marta, Zorrilla, Silvia, Monterroso, Begoña, Minton, Allen P., Rivas, Germán
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651908/
https://www.ncbi.nlm.nih.gov/pubmed/29057931
http://dx.doi.org/10.1038/s41598-017-14160-y
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author Sobrinos-Sanguino, Marta
Zorrilla, Silvia
Monterroso, Begoña
Minton, Allen P.
Rivas, Germán
author_facet Sobrinos-Sanguino, Marta
Zorrilla, Silvia
Monterroso, Begoña
Minton, Allen P.
Rivas, Germán
author_sort Sobrinos-Sanguino, Marta
collection PubMed
description 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.
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spelling pubmed-56519082017-10-26 Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads Sobrinos-Sanguino, Marta Zorrilla, Silvia Monterroso, Begoña Minton, Allen P. Rivas, Germán Sci Rep Article 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. Nature Publishing Group UK 2017-10-20 /pmc/articles/PMC5651908/ /pubmed/29057931 http://dx.doi.org/10.1038/s41598-017-14160-y Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Sobrinos-Sanguino, Marta
Zorrilla, Silvia
Monterroso, Begoña
Minton, Allen P.
Rivas, Germán
Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
title Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
title_full Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
title_fullStr Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
title_full_unstemmed Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
title_short Nucleotide and receptor density modulate binding of bacterial division FtsZ protein to ZipA containing lipid-coated microbeads
title_sort nucleotide and receptor density modulate binding of bacterial division ftsz protein to zipa containing lipid-coated microbeads
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5651908/
https://www.ncbi.nlm.nih.gov/pubmed/29057931
http://dx.doi.org/10.1038/s41598-017-14160-y
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