Studies on the dissociation and urea-induced unfolding of FtsZ support the dimer nucleus polymerization mechanism.

ABSTRACT: FtsZ 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-to-monomer and tetramer-to-dimer dissociation constants in the micromolar range. Meas

SUBMITTER: Montecinos-Franjola F 

PROVIDER: S-EPMC3341561 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature