Large-scale analysis of diffusional dynamics of proteins in living yeast cells using fluorescence correlation spectroscopy.

摘要: Abstract In the living cells, majority of proteins does not work alone, but interact with other or biomolecules to maintain cellular function, constituting a “protein community”. Previous efforts on mass spectroscopy-based protein interaction networks, interactomes, have provided picture community. However, these were static information after cells disrupted. For better understanding community in it is important know properties intracellular dynamics and interactions. Since hydrodynamic size mobility are related into such properties, direct measurement diffusional motion single will be helpful for uncovering properties. Here we completed diffusion homo-oligomeric 369 cytoplasmic GFP-fusion yeast Saccharomyces cerevisiae using fluorescence correlation spectroscopy (FCS). The large-scale analysis showed that motions obeyed two-component (i.e. slow fast components) model. Remarkably, both two components diffused more slowly than expected monomeric states. addition, further suggested existed as states previously expected. Our study, which characterizes large-scale, global view understand