3-D Holiday Gift Could Help Scientists Regulate Iron

The study, featured in the December issue of Science, contains some significant surprises about the structure and protein plasticity of IRP1 and the mRNA. Dr. Theil chairs the Council on BioIron at CHORI and is a professor at the University of California, Berkeley. She co-authored the study with William Walden, Ph.D. a professor of microbiology and immunology and his colleague, Karl Voltz, Ph.D., an associate professor at the University of Illinois at Chicago.

The researchers found that when mRNA and IRP1 join they change shapes to fit each other. In addition, the IRP1 changes its role from being an enzyme to an iron regulator. Each mRNA codes one or two proteins in the body. In this case the coded protein was Ferritin, which is essential for managing iron in the body. This discovery could help researchers design medications for patients with iron overload that occurs in hemochromotosis, Sickle Cell Disease and Thalassemia.

"Currently, there are medications available that are based on DNA structures such as anti-cancer drugs. Unfortunately, the problem with targeting DNA is that both healthy and cancerous cells have the same DNA, but they also have different mRNAs. Consequently, our research findings could help scientists design medications that target mRNAs," said Dr. Theil.