Active membrane viscoelasticity by the bacterial FtsZ-division protein.

@article{LpezMontero2012ActiveMV,
  title={Active membrane viscoelasticity by the bacterial FtsZ-division protein.},
  author={Iv{\'a}n L{\'o}pez-Montero and Pablo Mateos-Gil and Michele Sferrazza and Pilar L{\'o}pez Navajas and Germ{\'a}n Rivas and Marisela V{\'e}lez and Francisco Monroy},
  journal={Langmuir : the ACS journal of surfaces and colloids},
  year={2012},
  volume={28 10},
  pages={4744-53}
}
At the early stages of the division process in Escherichia coli, the protein FtsZ forms a septal ring at the midcell. This Z-ring causes membrane constriction during bacterial division. The Z-ring associates to the lipid membrane through several membrane proteins, ZipA among them. Here, a simplified FtsZ-ZipA model was reconstituted onto Langmuir monolayers based in E. coli polar lipid extract. Brewster angle and atomic force microscopy have revealed membrane FtsZ-polymerization upon GTP… CONTINUE READING

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