TY - JOUR
T1 - FtsZ rings and helices
T2 - Physical mechanisms for the dynamic alignment of biopolymers in rod-shaped bacteria
AU - Fischer-Friedrich, Elisabeth
AU - Friedrich, Benjamin M.
AU - Gov, Nir
N1 - Minerva foundation; German Academic Exchange Service; BSF [2006285]; Minerva Foundation [710589]We thank Sam Safran, Itzhak Fishov and Mario Feingold for many useful discussions and advice about FtsZ, and Yair Shokef for useful comments on the manuscript. We gratefully acknowledge funding from the Minerva foundation (EFF), the German Academic Exchange Service (BMF), as well as support by the BSF (grant no 2006285) and the Minerva Foundation (grant no 710589). This research is made possible in part by the historic generosity of the Harold Perlman Family.
PY - 2012/2
Y1 - 2012/2
N2 - In many bacterial species, the protein FtsZ forms a cytoskeletal ring that marks the future division site and scaffolds the division machinery. In rod-shaped bacteria, most frequently membrane-attached FtsZ rings or ring fragments are reported and occasionally helices. By contrast, axial FtsZ clusters have never been reported. In this paper, we investigate theoretically how dynamic FtsZ aggregates align in rod-shaped bacteria. We study systematically different physical mechanisms that affect the alignment of FtsZ polymers using a computational model that relies on autocatalytic aggregation of FtsZ filaments at the membrane. Our study identifies a general tool kit of physical and geometrical mechanisms by which rod-shaped cells align biopolymer aggregates. Our analysis compares the relative impact of each mechanism on the circumferential alignment of FtsZ as observed in rod-shaped bacteria. We determine spontaneous curvature of FtsZ polymers and axial confinement of FtsZ on the membrane as the strongest factors. Including Min oscillations in our model, we find that these stabilize axial and helical clusters on short time scales, but promote the formation of an FtsZ ring at the cell middle at longer times. This effect could provide an explanation to the long standing puzzle of transiently observed oscillating FtsZ helices in Escherichia coli cells prior to cell division.
AB - In many bacterial species, the protein FtsZ forms a cytoskeletal ring that marks the future division site and scaffolds the division machinery. In rod-shaped bacteria, most frequently membrane-attached FtsZ rings or ring fragments are reported and occasionally helices. By contrast, axial FtsZ clusters have never been reported. In this paper, we investigate theoretically how dynamic FtsZ aggregates align in rod-shaped bacteria. We study systematically different physical mechanisms that affect the alignment of FtsZ polymers using a computational model that relies on autocatalytic aggregation of FtsZ filaments at the membrane. Our study identifies a general tool kit of physical and geometrical mechanisms by which rod-shaped cells align biopolymer aggregates. Our analysis compares the relative impact of each mechanism on the circumferential alignment of FtsZ as observed in rod-shaped bacteria. We determine spontaneous curvature of FtsZ polymers and axial confinement of FtsZ on the membrane as the strongest factors. Including Min oscillations in our model, we find that these stabilize axial and helical clusters on short time scales, but promote the formation of an FtsZ ring at the cell middle at longer times. This effect could provide an explanation to the long standing puzzle of transiently observed oscillating FtsZ helices in Escherichia coli cells prior to cell division.
UR - http://www.scopus.com/inward/record.url?scp=84856957095&partnerID=8YFLogxK
U2 - 10.1088/1478-3975/9/1/016009
DO - 10.1088/1478-3975/9/1/016009
M3 - مقالة
SN - 1478-3967
VL - 9
JO - Physical Biology
JF - Physical Biology
IS - 1
M1 - 016009
ER -