

| 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.” |
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