Specifically, Wood and his colleagues found that when encountering oxidative stress, their bacterial cells initiated a process through which an antitoxin called MqsA was degraded, in turn allowing the toxin MqsR to degrade all of the cells' messenger RNA. This messenger RNA, Wood explains, plays a critical intermediate role in the cell's process of manufacturing proteins, so without it the cell can't make proteins. With the protein-manufacturing factory shut down, the bacterial cell goes dormant, and an antibiotic cannot "lock on" to the cell. When the stressor is removed, the bacterial cells eventually come back online and resume their normal activities, Wood says.
"It was the combination of the genetic studies at Texas A&M with our structural studies at Brown University that demonstrated that the proteins MqsR:MqsA form an entirely new family of toxin:antitoxin systems," Page says. "Remarkably, we have shown this system not only controls its own genes, but also many other genes in E. coli, including the gene that controls the response to oxidative stress."
This response mechanism, Wood emphasizes, does not replace the mutation-based approaches that have for years characterized cell behavior; it's merely another method in a multifaceted approach undertaken by bacteria to ensure survival.
"A small community of bacteria is in a sense hedging its bet against a threat to its survival by taking another approach," Wood says. "To the bacteria, this is always a numbers game. In one milliliter you can have a trillion bacterial cells, and they don't always do the same thing under stress.
|Contact: Ryan Garcia|
Texas A&M University