GFP-tagging sheds light on protein translocation

Green fluorescent protein (GFP) is a powerful tool for studying gene expression, protein localization, protein-protein interactions, calcium concentrations and redox potentials. However, GFP not only contains a chromophore, but is also tightly folded in a temperature-dependent manner. Recent experiments on the translocase of the mitochondrial outer membrane, the TOM complex, utilized the latter property for studying protein transport across and into biomembranes in vivo [1]. I will present this study and discuss the suitability of GFP as a valuable tool for the analysis of other protein translocases in a variety of organisms. Moreover, results from such analyses could be highly important for the interpretation of classical experiments using GFP-tagging.