His team uncovered an extensive network of redox activity, identifying 176 proteins that are sensitive to signaling in this manner. Before this study, just 75 of those proteins were known to be part of a redox signaling network. The scientists found that the system is involved in all the major processes of a cell which genes are turned on and off, for example, as well as how the cell maintains its molecular machinery and converts energy into fuel.
Central to the work are the chemical probes Wright developed that are able to cross the cell membrane and get into the cytoplasm of the cell. The probes flag redox events by binding to certain forms of the amino acid cysteine, which is a known player in many of these interactions. Then the probes and the interactions they flag are subjected to scrutiny at EMSL, the DOE's Environmental Molecular Sciences Laboratory on the PNNL campus, where instruments detect redox activity through various means, such as through fluorescent imaging and mass spectrometry. The analysis tells scientists about when and where within the cell redox activity occurred.
"Knowing the proteins that are sensitive to redox signaling lets us know where to look as we test out new methods for working with this organism," said Wright. "We can tinker with a specific protein, for instance, and then watch the effects immediately.
"This is the type of information we really must have if we want organisms like this to produce substances that make a difference, like biofuels, chemicals or potential medicines," he added.
|Contact: Tom Rickey|
DOE/Pacific Northwest National Laboratory