Medicine / Institute for Cytobiology
Biochemistry / Cell biology
Robert-Koch-Straße 6, 35037 Marburg
+49-6421 28 66449
The Lill group elucidates the molecular mechanisms underlying the biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes. Fe/S proteins play important roles in, e.g., mitochondrial respiration, ribosomal protein translation, DNA synthesis and repair, and antiviral response. Eukaryotic Fe/S protein biogenesis involves more than 30 cellular proteins and its failure is associated with human disease. Mitochondrial Fe/S proteins require the iron-sulfur cluster assembly (ISC) machinery which was inherited from bacteria during evolution. Cytosolic and nuclear Fe/S protein maturation also depends on this machinery, yet additionally requires the mitochondrial ABC transporter Atm1 and the cytosolic iron-sulfur protein assembly (CIA) machinery.
Human cell culture
1. Lill, R. & Freibert, S.A. (2020). Mechanisms of mitochondrial iron-sulfur protein biogenesis. Annu. Rev. Biochem. 89, in press.
2. Stehling, O., Jeoung, J.H., Freibert, S.A., Paul, V.D., Bänfer, S., Niggemeyer, B., Rösser, R., Dobbek, H., & Lill, R. (2018). Function and crystal structure of the dimeric P-loop ATPase CFD1 coordinating an exposed [4Fe-4S] cluster for transfer to apoproteins. Proc. Natl. Acad. Sci. U.S.A. 115, E9085-E9094.
3. Freibert, S.A., Goldberg, A.V., Hacker, C., Molik, S., Dean, P., Williams, T.A., Nakjang, S., Long, S., Sendra, K., Bill, E., Heinz, E., Hirt, R.P., Lucocq, J.M., Embley, T.M., & Lill, R. (2017). Evolutionary conservation and in vitro reconstitution of microsporidian iron-sulfur cluster biosynthesis. Nat. Commun. 8, 13932.