TY - JOUR TI - The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC protein Rli1 for iron-sulfur cluster insertion AU - Paul, Viktoria Désirée AU - Mühlenhoff, Ulrich AU - Stümpfig, Martin AU - Seebacher, Jan AU - Kugler, Karl G AU - Renicke, Christian AU - Taxis, Christof AU - Gavin, Anne-Claude AU - Pierik, Antonio J AU - Lill, Roland A2 - Dean, Dennis VL - 4 PY - 2015 DA - 2015/07/16 SP - e08231 C1 - eLife 2015;4:e08231 DO - 10.7554/eLife.08231 UR - https://doi.org/10.7554/eLife.08231 AB - Cytosolic and nuclear iron-sulfur (Fe-S) proteins are involved in many essential pathways including translation and DNA maintenance. Their maturation requires the cytosolic Fe-S protein assembly (CIA) machinery. To identify new CIA proteins we employed systematic protein interaction approaches and discovered the essential proteins Yae1 and Lto1 as binding partners of the CIA targeting complex. Depletion of Yae1 or Lto1 results in defective Fe-S maturation of the ribosome-associated ABC protein Rli1, but surprisingly no other tested targets. Yae1 and Lto1 facilitate Fe-S cluster assembly on Rli1 in a chain of binding events. Lto1 uses its conserved C-terminal tryptophan for binding the CIA targeting complex, the deca-GX3 motifs in both Yae1 and Lto1 facilitate their complex formation, and Yae1 recruits Rli1. Human YAE1D1 and the cancer-related ORAOV1 can replace their yeast counterparts demonstrating evolutionary conservation. Collectively, the Yae1-Lto1 complex functions as a target-specific adaptor that recruits apo-Rli1 to the generic CIA machinery. KW - post-translational modification KW - metal biology KW - iron-sulfur protein biogenesis KW - CIA machinery KW - mitochondria JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -