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Behaviour of bacterial division protein FtsZ under a monolayer with phospholipid domains |
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| Authors: | Cé line Lafontaine,Nicole Orange,Eugenia Mileykovskaya |
| Affiliation: | a Polymères, Biopolymères, Membranes, UMR 6522 CNRS, Université de Rouen, UFR des Sciences, 76821 Mont Saint Aignan Cedex, France b Laboratoire de Microbiologie du Froid, UPRES 2123 , Université de Rouen, IUT d'Evreux, 55 Rue Saint-Germain, 27000 Evreux, France c Assemblages Moléculaires: Modélisation et Imagerie SIMS, FRE 2829 CNRS, Université de Rouen, UFR des Sciences, 76821 Mont-Saint-Aignan, France d Epigenomics Project, genopole®, 91000 Evry, France e Department of Biochemistry and Molecular Biology, University of Texas-Houston Medical School, P.O. Box 20708, Houston, Texas 77225, USA |
| Abstract: | Assembly of the tubulin-like protein FtsZ at or near the cytoplasmic membrane is one of the earliest steps in division of bacteria such as Escherichia coli. Exactly what constitutes the site at which FtsZ acts is less clear. To investigate the influence of the membrane phospholipids on FtsZ localization and assembly, we have elaborated with the Langmuir technique a two-lipid monolayer made of dilauryl-phosphatidylethanolamine (DLPE) and dipalmitoyl-phosphatidylglycerol (DPPG). This monolayer comprised stable condensed domains in an expanded continuous phase. In the presence of GTP, FtsZ assembly disrupts the condensed domains within 5 min. After several hours, with or without GTP, FtsZ assembled into large aggregates at the domain interface. We suggest that the GTP-induced polymerization of FtsZ is coupled to the association of FtsZ protofilaments with domain interfaces. |
| Keywords: | FtsZ Lipid domain Membrane model Monolayer Interface Cell division |
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