L L Pearce, R E Gandley, W Han, K Wasserloos, M Stitt, A J Kanai, M K McLaughlin, B R Pitt, E S Levitan
Although the function of metallothionein (MT), a 6- to 7-kDa cysteine-rich metal binding protein, remains unclear, it has been suggested from in vitro studies that MT is an important component of intracellular redox signaling, including being a target for nitric oxide (NO). To directly study the interaction between MT and NO in live cells, we generated a fusion protein consisting of MT sandwiched between two mutant green fluorescent proteins (GFPs). In vitro studies with this chimera (FRET-MT) demonstrate that fluorescent resonance energy transfer (FRET) can be used to follow conformational changes indicative of metal release from MT...
January 4, 2000: Proceedings of the National Academy of Sciences of the United States of America