In:
eLife, eLife Sciences Publications, Ltd, Vol. 3 ( 2014-05-02)
Kurzfassung:
Bacterial cells come in a variety of different shapes, including spheres, rods, spirals, and crescents. Shape is important for bacterial cells because it plays a role in cell division, helps to maximize the uptake of nutrients, and aids cell movement. The shape of a cell is determined mainly by its cytoskeleton, a form of ‘scaffolding’ within the cell that is made of various protein filaments. The bacterial cytoskeleton was discovered over 20 years ago, but it has not been studied as much as the cytoskeletons of yeast, plant, animals, and other eukaryotes. Many of the bacterial proteins and filaments that make up the cytoskeleton are similar to those found in eukaryotes. A protein called MreB, for example, is the bacterial equivalent of actin, which performs a wide range of roles in eukaryotes. However, van den Ent, Izoré et al. have now shown that the detailed structure of MreB filaments is different to that of actin filaments. It has been known for some time that actin filaments are composed of two strands of actin proteins that are twisted and parallel with each other. MreB filaments are also made of two strands of MreB proteins, but van den Ent, Izoré et al. found that these strands are straight, not twisted, and that they are antiparallel rather than parallel. Thus, unlike other filaments of actin-like proteins, where the two ends of the filament are clearly different from each other, the antiparallel strands of MreB form a double filament without a clear direction. van den Ent, Izoré et al. also showed that MreB double filaments can bind to surfaces that mimic a bacterial cell membrane, and that mutant bacterial cells without these double filaments adopt the wrong cell shape. Further experiments exposed potential targets on the MreB filaments for antibiotics that could treat bacterial infections.
Materialart:
Online-Ressource
ISSN:
2050-084X
DOI:
10.7554/eLife.02634.001
DOI:
10.7554/eLife.02634.002
DOI:
10.7554/eLife.02634.003
DOI:
10.7554/eLife.02634.004
DOI:
10.7554/eLife.02634.005
DOI:
10.7554/eLife.02634.006
DOI:
10.7554/eLife.02634.007
DOI:
10.7554/eLife.02634.008
DOI:
10.7554/eLife.02634.009
DOI:
10.7554/eLife.02634.010
DOI:
10.7554/eLife.02634.011
DOI:
10.7554/eLife.02634.012
DOI:
10.7554/eLife.02634.013
DOI:
10.7554/eLife.02634.014
DOI:
10.7554/eLife.02634.015
DOI:
10.7554/eLife.02634.016
DOI:
10.7554/eLife.02634.017
DOI:
10.7554/eLife.02634.018
DOI:
10.7554/eLife.02634.019
DOI:
10.7554/eLife.02634.020
DOI:
10.7554/eLife.02634.021
DOI:
10.7554/eLife.02634.022
Sprache:
Englisch
Verlag:
eLife Sciences Publications, Ltd
Publikationsdatum:
2014
ZDB Id:
2687154-3
