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- W2073071019 abstract "Septins are a family of GTP-binding cytoskeletal proteins conserved in all eukaryotes (except higher plants) that have roles in erecting diffusion barriers, affecting membrane curvature, and providing protein scaffolding. Budding yeast (Saccaromyces cerevisiae) is a convenient organism for investigating septin organization and function because of the wide variety of tools available. Because septins are conserved, understanding the principles that dictate how the yeast proteins organize should provide insight into septin structure and function in higher eukaryotes, including humans. Single-particle EM analysis has revealed that septin subunits associate to form linear apolar hetero-octameric rods. In vitro, septin rods polymerize end-on-end into long, straight paired filament. However, no facile method has existed for studying the polymerization of septin hetero-octamers in vitro in real time. We have previously generated yeast septin complexes wherein all endogenous Cys residues were eliminated by site-directed mutagenesis, except either one native Cys (C43) or an introduced E294C mutation in Cdc11. Because Cdc11 is the terminal subunit in hetero-octamers, derivatization of the single Cys residue with organic dyes should permit the use of Förster resonance energy transfer (FRET) to monitor filament assembly. In initial experiments conducted with mixtures of donor- and acceptor-labeled hetero-octamers, the expected FRET is exhibited under conditions that favor polymerization (low salt), but not under conditions known to prevent polymerization (high salt). Furthermore, the amount of FRET observed depends on the input concentrations and relative ratios of the donor and acceptor dye-labeled rods. These findings are fully consistent with previous observations made by EM and indicate that the observed FRET is providing a reliable solution-based assay for the end-to-end assembly of hetero-octamers into filaments. This assay can now be exploited to study the effects of septin concentration, cofactors (e.g., guanine nucleotides) and septin-interacting proteins." @default.
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- W2073071019 date "2014-01-01" @default.
- W2073071019 modified "2023-09-26" @default.
- W2073071019 title "A FRET-Based Method for Measurement of Yeast Septin Filament Formation In Vitro" @default.
- W2073071019 doi "https://doi.org/10.1016/j.bpj.2013.11.385" @default.
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