MMS19 Assembles Iron-Sulfur Proteins Required for DNA Metabolism and Genomic Integrity
2012
Stehling, Oliver | Vashisht, Ajay A. | Mascarenhas, Judita | Jonsson, Zophonias O. | Sharma, Tanu | Netz, Daili J. A. | Pierik, Antonio J. | Wohlschlegel, James A. | Lill, Roland
MMS19 Joins the CIA Iron-sulfur (Fe-S) proteins play a critical role in cell metabolism and particularly in DNA repair and replication. Mutants in eukaryotic gene MMS19 are particularly sensitive to DNA damaging agents, suggesting that it is involved in DNA repair, but the mutations can also have other wide-ranging effects on the cell (see the Perspective by Gottschling). Now, Stehling et al. (p. 195, published online 7 June) and Gari et al. (p. 243, published online 7 June) show that in both yeast and humans, MMS19 functions as part of the cytosolic Fe-S protein assembly (CIA) machinery. The MMS19 is part of a specialized CIA targeting complex that plays a role late in cytosolic Fe-S protein assembly to direct Fe-S cluster transfer from the CIA scaffold complex to a subset of Fe-S proteins, including a number associated with DNA metabolism.
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