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Authordc.contributor.authorMontecinos Franjola, Felipe 
Authordc.contributor.authorRoss, Justin A. es_CL
Authordc.contributor.authorSánchez, Susana A. es_CL
Authordc.contributor.authorBrunet, Juan E. es_CL
Authordc.contributor.authorLagos Mónaco, Rosalba es_CL
Authordc.contributor.authorJameson, David M. es_CL
Authordc.contributor.authorMonasterio Opazo, Octavio es_CL
Admission datedc.date.accessioned2014-01-07T18:57:33Z
Available datedc.date.available2014-01-07T18:57:33Z
Publication datedc.date.issued2012-05
Cita de ítemdc.identifier.citationBiophysical Journal. Volume 102, Issue 9, 2 May 2012, Pages 2176–2185en_US
Identifierdc.identifier.otherDOI: 10.1016/j.bpj.2012.03.064
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/119647
General notedc.descriptionArtículo de publicación ISIen_US
Abstractdc.description.abstractFtsZ is a major protein in bacterial cytokinesis that polymerizes into single filaments. A dimer has been proposed to be the nucleating species in FtsZ polymerization. To investigate the influence of the self-assembly of FtsZ on its unfolding pathway, we characterized its oligomerization and unfolding thermodynamics. We studied the assembly using size-exclusion chromatography and fluorescence spectroscopy, and the unfolding using circular dichroism and two-photon fluorescence correlation spectroscopy. The chromatographic analysis demonstrated the presence of monomers, dimers, and tetramers with populations dependent on protein concentration. Dilution experiments using fluorescent conjugates revealed dimer-tomonomer and tetramer-to-dimer dissociation constants in the micromolar range. Measurements of fluorescence lifetimes and rotational correlation times of the conjugates supported the presence of tetramers at high protein concentrations and monomers at low protein concentrations. The unfolding study demonstrated that the three-state unfolding of FtsZ was due to the mainly dimeric state of the protein, and that the monomer unfolds through a two-state mechanism. The monomer-to-dimer equilibrium characterized here (Kd ¼ 9 mM) indicates a significant fraction (~10%) of stable dimers at the critical concentration for polymerization, supporting a role of the dimeric species in the first steps of FtsZ polymerization.en_US
Lenguagedc.language.isoen_USen_US
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile*
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/*
Títulodc.titleStudies on the Dissociation and Urea-Induced Unfolding of FtsZ Support the Dimer Nucleus Polymerization Mechanismen_US
Document typedc.typeArtículo de revistaen_US


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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile