%0 Journal Article
%A Monterroso, Begoña
%A Ahijado Guzmán, Rubén
%A Reija, Belén
%A Alfonso, Carlos
%A Zorrilla, Silvia
%A Minton, Allen 
%A Rivas, Germán
%T Mg2+-linked self-assembly of FtsZ in the presence of GTP or a GTP analogue involves the concerted formation of a narrow size distribution of oligomeric species
%D 2012
%@ 0006-2960
%U https://hdl.handle.net/20.500.14352/92115
%X The assembly of the bacterial cell division FtsZ protein in the presence of constantly replenished GTP was studied as a function of Mg2+ concentration (at neutral pH and 0.5 M potassium) under steady-state conditions by sedimentation velocity, concentration-gradient light scattering, fluorescence correlation spectroscopy, and dynamic light scattering. Sedimentation velocity measurements confirmed previous results indicating cooperative appearance of a narrow size distribution of finite oligomers with increasing protein concentration. The concentration dependence of light scattering and diffusion coefficients independently verified the cooperative appearance of a narrow distribution of high molecular weight oligomers, and in addition provided a measurement of the average size of these species, which corresponds to 100 ± 20 FtsZ protomers at millimolar Mg2+ concentration.
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