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Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution

Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z‐ring from assembling anywhere but the mid‐cell, through an oscillatory diffusion‐reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymer...

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Autores principales: Szewczak‐Harris, Andrzej, Wagstaff, James, Löwe, Jan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771821/
https://www.ncbi.nlm.nih.gov/pubmed/31166018
http://dx.doi.org/10.1002/1873-3468.13471
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author Szewczak‐Harris, Andrzej
Wagstaff, James
Löwe, Jan
author_facet Szewczak‐Harris, Andrzej
Wagstaff, James
Löwe, Jan
author_sort Szewczak‐Harris, Andrzej
collection PubMed
description Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z‐ring from assembling anywhere but the mid‐cell, through an oscillatory diffusion‐reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymerization of cell division protein FtsZ into the Z‐ring. MinC and MinD form polymeric assemblies in solution and on cell membranes. Here, we report the high‐resolution cryo‐EM structure of the copolymeric filaments of Pseudomonas aeruginosa MinCD. The filaments consist of three protofilaments made of alternating MinC and MinD dimers. The MinCD protofilaments are almost completely straight and assemble as single protofilaments on lipid membranes, which we also visualized by cryo‐EM.
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spelling pubmed-67718212019-10-07 Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution Szewczak‐Harris, Andrzej Wagstaff, James Löwe, Jan FEBS Lett Editor's Choice Positioning of the division site in many bacterial species relies on the MinCDE system, which prevents the cytokinetic Z‐ring from assembling anywhere but the mid‐cell, through an oscillatory diffusion‐reaction mechanism. MinD dimers bind to membranes and, via their partner MinC, inhibit the polymerization of cell division protein FtsZ into the Z‐ring. MinC and MinD form polymeric assemblies in solution and on cell membranes. Here, we report the high‐resolution cryo‐EM structure of the copolymeric filaments of Pseudomonas aeruginosa MinCD. The filaments consist of three protofilaments made of alternating MinC and MinD dimers. The MinCD protofilaments are almost completely straight and assemble as single protofilaments on lipid membranes, which we also visualized by cryo‐EM. John Wiley and Sons Inc. 2019-06-14 2019-08 /pmc/articles/PMC6771821/ /pubmed/31166018 http://dx.doi.org/10.1002/1873-3468.13471 Text en © The Authors. FEBS Letters published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Editor's Choice
Szewczak‐Harris, Andrzej
Wagstaff, James
Löwe, Jan
Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
title Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
title_full Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
title_fullStr Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
title_full_unstemmed Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
title_short Cryo‐EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution
title_sort cryo‐em structure of the mincd copolymeric filament from pseudomonas aeruginosa at 3.1 å resolution
topic Editor's Choice
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6771821/
https://www.ncbi.nlm.nih.gov/pubmed/31166018
http://dx.doi.org/10.1002/1873-3468.13471
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