RT Journal Article
T1 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
A1 Monterroso, Begoña
A1 Ahijado Guzmán, Rubén
A1 Reija, Belén
A1 Alfonso, Carlos
A1 Zorrilla, Silvia
A1 Minton, Allen
A1 Rivas, Germán
AB 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.
PB ACS Publications
SN 0006-2960
YR 2012
FD 2012
LK https://hdl.handle.net/20.500.14352/92115
UL https://hdl.handle.net/20.500.14352/92115
LA eng
NO Begoña Monterroso, Rubén Ahijado-Guzmán, Belén Reija, Carlos Alfonso, Silvia Zorrilla, Allen P. Minton, and Germán Rivas Biochemistry 2012 51 (22), 4541-4550 DOI: 10.1021/bi300401b
DS Docta Complutense
RD 12 abr 2025