Depolymerization dynamics of individual filaments of bacterial cytoskeletal protein FtsZ.

Proceedings of the National Academy of Sciences of the United States of America
Pablo Mateos-GilMarisela Vélez

Abstract

We report observation and analysis of the depolymerization filaments of the bacterial cytoskeletal protein FtsZ (filament temperature-sensitive Z) formed on a mica surface. At low concentration, proteins adsorbed on the surface polymerize forming curved filaments that close into rings that remain stable for some time before opening irreversibly and fully depolymerizing. The distribution of ring lifetimes (T) as a function of length (N), shows that the rate of ring aperture correlates with filament length. If this ring lifetime is expressed as a bond survival time, (T(b) ≡ NT), this correlation is abolished, indicating that these rupture events occur randomly and independently at each monomer interface. After rings open irreversibly, depolymerization of the remaining filaments is fast, but can be slowed down and followed using a nonhydrolyzing GTP analogue. The histogram of depolymerization velocities of individual filaments has an asymmetric distribution that can be fit with a computer model that assumes two rupture rates, a slow one similar to the one observed for ring aperture, affecting monomers in the central part of the filaments, and a faster one affecting monomers closer to the open ends. From the quantitative analysis, ...Continue Reading

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Citations

Dec 10, 2013·Nature Cell Biology·Martin Loose, Timothy J Mitchison
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Jul 11, 2013·Langmuir : the ACS Journal of Surfaces and Colloids·Mario EncinarMarisela Vélez

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