Behaviour of bacterial division protein FtsZ under a monolayer with phospholipid domains.
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.
Lafontaine
Céline
C
Polymères, Biopolymères, Membranes, UMR 6522 CNRS, Université de Rouen, UFR des Sciences, 76821, Mont Saint Aignan Cedex, France.
Valleton
Jean-Marc
JM
Orange
Nicole
N
Norris
Vic
V
Mileykovskaya
Eugenia
E
Alexandre
Stéphane
S
D001426:Bacterial Proteins / Q000737:chemistry*; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D010714:Phosphatidylethanolamines / Q000737:chemistry*; D010715:Phosphatidylglycerols / Q000737:chemistry*; D017434:Protein Structure, Tertiary
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; C007445:1,2-dilauroylphosphatidylethanolamine; C030345:1,2-dipalmitoylphosphatidylglycerol