Analyse eines unkonventionellen Vitamin-Transporters

Forster resonance energy transfer (FRET) identifies the co-localization of fluorescent macromolecules on a nanometer scale. FRET between nonidentical and identical fluorophores is called HeteroFRET or HomoFRET, respectively. We applied FRET techniques to analyze the oligomeric state of the core component (BioY) of a bacterial biotin transporter. BioY was fused to fluorescent proteins suitable for Hetero- and HomoFRET analyses. Spectrometric and imaging experiments with living cells strongly support a model with oligomers of BioY as the functional state of the core unit.