Aviso: para depositar documentos, por favor, inicia sesión e identifícate con tu cuenta de correo institucional de la UCM con el botón MI CUENTA UCM. No emplees la opción AUTENTICACIÓN CON CONTRASEÑA
 

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

Loading...
Thumbnail Image

Full text at PDC

Publication date

2012

Advisors (or tutors)

Editors

Journal Title

Journal ISSN

Volume Title

Publisher

ACS Publications
Citations
Google Scholar

Citation

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

Abstract

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.

Research Projects

Organizational Units

Journal Issue

Description

Unesco subjects

Keywords

Collections