Min protein oscillations position the bacterial cell division machinery at the cell center through a reaction‐diffusion mechanism. Here we report the successful encapsulation of the oscillating Min protein system in giant unilamellar vesicles (GUVs). Using confocal fluorescence microscopy, we identify several distinct modes of spatiotemporal patterns inside spherical GUVs. Interestingly, for osmotically deflated GUVs, we observe that the vesicle shape actively changes in concert with the Min oscillations. Our results show that the periodic relocation of Min proteins from the vesicle lumen to the membrane and back is accompanied by drastic changes in the mechanical properties of the lipid bilayer. In particular, two types of oscillating membrane‐shape changes are highlighted: (i) GUVs that repeatedly undergo fission into two connected compartments and fusion of these compartments back into a dumbbell‐shape, and (ii) GUVs that show periodic budding and subsequent merging of the buds with the mother vesicle, accompanied by an overall shape change of the vesicle, reminiscent of a bouncing ball. These findings demonstrate how reaction‐diffusion based protein self‐organization can directly yield visible mechanical effects on membrane compartments, even up to autonomous division, without the need for coupling to cytoskeletal elements. This offers fascinating perspectives for the bottom‐up design of minimal cell division.
:Users/mh/Documents/Mendeley Desktop/Litschel et al/2018/Litschel et al.\_2018\_Beating Vesicles Encapsulated Protein Oscillations Cause Dynamic Membrane Deformations.pdf:pdf
%0 Journal Article
%1 Litschel2018
%A Litschel, Thomas
%A Ramm, Beatrice
%A Maas, Roel
%A Heymann, Michael
%A Schwille, Petra
%D 2018
%J Angewandte Chemie International Edition
%K myown
%N 50
%P 16286--16290
%R 10.1002/anie.201808750
%T Beating Vesicles: Encapsulated Protein Oscillations Cause Dynamic Membrane Deformations
%U http://doi.wiley.com/10.1002/anie.201808750
%V 57
%X Min protein oscillations position the bacterial cell division machinery at the cell center through a reaction‐diffusion mechanism. Here we report the successful encapsulation of the oscillating Min protein system in giant unilamellar vesicles (GUVs). Using confocal fluorescence microscopy, we identify several distinct modes of spatiotemporal patterns inside spherical GUVs. Interestingly, for osmotically deflated GUVs, we observe that the vesicle shape actively changes in concert with the Min oscillations. Our results show that the periodic relocation of Min proteins from the vesicle lumen to the membrane and back is accompanied by drastic changes in the mechanical properties of the lipid bilayer. In particular, two types of oscillating membrane‐shape changes are highlighted: (i) GUVs that repeatedly undergo fission into two connected compartments and fusion of these compartments back into a dumbbell‐shape, and (ii) GUVs that show periodic budding and subsequent merging of the buds with the mother vesicle, accompanied by an overall shape change of the vesicle, reminiscent of a bouncing ball. These findings demonstrate how reaction‐diffusion based protein self‐organization can directly yield visible mechanical effects on membrane compartments, even up to autonomous division, without the need for coupling to cytoskeletal elements. This offers fascinating perspectives for the bottom‐up design of minimal cell division.
@article{Litschel2018,
abstract = {Min protein oscillations position the bacterial cell division machinery at the cell center through a reaction‐diffusion mechanism. Here we report the successful encapsulation of the oscillating Min protein system in giant unilamellar vesicles (GUVs). Using confocal fluorescence microscopy, we identify several distinct modes of spatiotemporal patterns inside spherical GUVs. Interestingly, for osmotically deflated GUVs, we observe that the vesicle shape actively changes in concert with the Min oscillations. Our results show that the periodic relocation of Min proteins from the vesicle lumen to the membrane and back is accompanied by drastic changes in the mechanical properties of the lipid bilayer. In particular, two types of oscillating membrane‐shape changes are highlighted: (i) GUVs that repeatedly undergo fission into two connected compartments and fusion of these compartments back into a dumbbell‐shape, and (ii) GUVs that show periodic budding and subsequent merging of the buds with the mother vesicle, accompanied by an overall shape change of the vesicle, reminiscent of a bouncing ball. These findings demonstrate how reaction‐diffusion based protein self‐organization can directly yield visible mechanical effects on membrane compartments, even up to autonomous division, without the need for coupling to cytoskeletal elements. This offers fascinating perspectives for the bottom‐up design of minimal cell division.},
added-at = {2019-11-28T11:57:04.000+0100},
author = {Litschel, Thomas and Ramm, Beatrice and Maas, Roel and Heymann, Michael and Schwille, Petra},
biburl = {https://puma.ub.uni-stuttgart.de/bibtex/259776f72652dc678f211903783e9737d/michaelheymann},
doi = {10.1002/anie.201808750},
file = {:Users/mh/Documents/Mendeley Desktop/Litschel et al/2018/Litschel et al.{\_}2018{\_}Beating Vesicles Encapsulated Protein Oscillations Cause Dynamic Membrane Deformations.pdf:pdf},
interhash = {eacbd40de102df05f50d54f9855152db},
intrahash = {59776f72652dc678f211903783e9737d},
issn = {14337851},
journal = {Angewandte Chemie International Edition},
keywords = {myown},
month = dec,
number = 50,
pages = {16286--16290},
timestamp = {2019-11-28T12:54:55.000+0100},
title = {{Beating Vesicles: Encapsulated Protein Oscillations Cause Dynamic Membrane Deformations}},
url = {http://doi.wiley.com/10.1002/anie.201808750},
volume = 57,
year = 2018
}
