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Open Access item FtsZ bacterial cytoskeletal polymers on curved surfaces: the importance of lateral interactions
|Citation:||Biophysical Journal, 94 (11) : L81-L83 (2008)|
|Abstract:||A recent theoretical article provided a mechanical explanation for the formation of cytoskeletal rings and helices in bacteria assuming that these shapes arise, at least in part, from the interaction of the inherent mechanical properties of the protein polymers and the constraints imposed by the curved cell membrane (Andrews, S., and A. P. Arkin. 2007. Biophys. J. 93:1872–1884). Due to the lack of experimental data regarding the bending rigidity and preferential bond angles of bacterial polymers, the authors explored their model over wide ranges of preferred curvature values. In this letter, we present the shape diagram of the FtsZ bacterial polymer on a curved surface but now including recent experimental data on the in vitro formed FtsZ polymers. The lateral interactions between filaments observed experimentally change qualitatively the shape diagram and indicate that the formation of rings over spirals is more energetically favored than estimated in the above-mentioned article.
In recent years, it has become evident that the bacterial cell contains a large number of organized elements that fit within the wide concept of cytoskeleton used in eukaryotes: stable or dynamic polymers of filamentous nature with long-range order that can assemble, disassemble, and redistribute rapidly within the cell in response to signals that regulate cellular functions [1.] and [2.]. Some of these polymers are bound to the inside of the cell membrane, forming rings or helices [3.], [4.], [5.] and [6.], and they can serve different functions that go from helping define the cell morphology (7); locating the cell division site (2); to forming a ring that contracts during cell division [8.] and [9.]. A recent theoretical analysis (10) characterizes the shape of the membrane-bound polymers with a sequence of turning angles (see Fig. 1 D). The energy was taken as a sum of independent contributions for each bond along the filament, assuming quadratic dependence of the bond energy with the deviations of the three angles with respect to their optimal values . Then, the minimum energy structures were morphologically associated to the cytoskeletal rings and helices formed by different bacterial proteins and used to estimate the preferential bond angles between these proteins|
|Description:||3 páginas, 1 figura -- PAGS nros. L81-L83|
|Publisher version (URL):||http://dx.doi.org/10.1529/biophysj.107.128363|
|E-ISSNmetadata.dc.identifier.doi = DOI:||1542-0086|
|Appears in Collections:||(CIB) Artículos|
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