The lab of Cheryl Kerfeld at Michigan State University has created a synthetic nano-sized factory, based on natural ones found in bacteria. This research could someday lead to new medical, industrial or bioenergy applications.
The new study is published in Metabolic Engineering (“A designed bacterial microcompartment shell with tunable composition and precision cargo loading”).
Natural nanofactories are found in bacteria all over the planet. Some make nutrients. Others sequester toxic materials that would otherwise make the bacteria sick — or even die.
But all factories share a common exterior, a shell made of protein tiles. Scientists want to design new factories, based on those found in bacteria naturally, for use in biotechnology.
One way to direct useful enzymes to these factories is by physically attaching them to the tail ends of the proteins that make up the factory shells. But there is a catch.
The ends, or termini, of most shell proteintiles face the outside of a factory. So any molecules fused to the protein ends will end up on the outside surface and not the inside. This is a problem if the goal is to keep one or more enzymes inside a factory separated from the rest of the cell.
“In order to send proteins to the inside of the factory, we needed a new kind of building block that still assembled into shells,” said Bryan Ferlez, a post doctorate researcher in the Kerfeld lab. “We aimed to redesign a shell protein so its termini face the inside. The end result is that cargo connected to this shell protein would also end up inside the shell.”

Image Credit:  Michigan State University


News This Week

Light-controlled reactions at the nanoscale

Controlling strong electromagnetic fields on nanoparticles is the key to triggering targeted molecular reactions on their surfaces. Such control over strong fields is achieved via laser light. Although laser-induced formation and breaking of molecular [...]