FAT10 is a small protein with a huge effect. Its attachment to a target protein is a signal for its degradation. FAT10 is a marking system for degradation that seems to be inefficient. In contrast to its biological competitor, ubiquitin, which is recycled, FAT10 is degraded along with its target protein which appears wasteful at first glance. So, why does this seemingly inefficient FAT10-system exist at all? Professor Marcus Groettrup, head of the immunology working group at the University of Konstanz, and his team have been carrying out research on FAT10 for many years. Now they have achieved a breakthrough that made it possible to determine the high-resolution structure of FAT10. This success was enabled through another achievement. In collaboration with Dr. Annette Aichem from the Biotechnology Institute Thurgau (BITg), Konstanz chemist Professor Christine Peter and structural biologist Dr. Silke Wiesner from the University of Regensburg, the team developed a molecular technique to produce stable and highly-concentrated FAT10 with a high degree of purity. As a consequence, the researchers could carry out a structure analysis of FAT10 via x-ray crystallography and magnetic resonance spectroscopy. The results were published online on August 20, 2018 in Nature Communications. The open-access article is titled “The Structure of the Ubiquitin-Like Modifier FAT10 Reveals an Alternative Targeting Mechanism for Proteasomal Degradation.” "We found a mechanism in FAT10 that is entirely different from ubiquitin. This mechanism is very interesting for the entire ubiquitin field,” says Dr. Groettrup. In contrast to ubiquitin with one domain, FAT10 has two domains, i.e., folds that enable the proteins to function.
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