The mammalian proteins MMS19, MIP18, and ANT2 are involved in cytoplasmic iron-sulfur cluster protein assembly.
|Authors||van Wietmarschen N, Moradian A, Morin GB, Lansdorp PM & Uringa EJ.|
|Abstract||Iron-sulfur (Fe-S) clusters are essential cofactors of proteins with a wide range of biological functions. A dedicated cytosolic Fe-S cluster assembly (CIA) system is required to assemble Fe-S clusters into cytosolic and nuclear proteins. Here, we show that the mammalian MMS19 nucleotide excision repair protein homolog (MMS19) can simultaneously bind Probable cytosolic iron-sulfur protein assembly protein CIAO1 (CIAO1) and Fe-S proteins, confirming it is a central protein of the CIA machinery that brings Fe-S cluster donor proteins and receiving apoproteins into proximity. In addition, we show that Mitotic spindle-associated MMXD complex subunit MIP18 (MIP18) also interacts with both CIAO1 and Fe-S proteins. Specifically, it binds the Fe-S cluster coordinating regions in Fe-S proteins. Furthermore, we show that ADP/ATP translocase 2 (ANT2) interacts with Fe-S apoproteins and MMS19 in the CIA complex, but not with the individual proteins. Together, these results elucidate the composition and interactions within the late CIA complex.|
|Journal Name and Citation||
J Biol Chem. 2012 Nov 13. [Epub ahead of print]
|Date of Publication||2012/11/13|