Mushajiang, Mierzhati2015-09-082015-09-082014-08https://hdl.handle.net/2144/12982Poster presentation at REU Summer's End Research Symposium, 2014, by REU participant Mierzhati Mushajiang, Bunker Hill Community College - Deborah Perlstein group, Eric Camire lab mentorThe Cytosolic Iron-Sulfur Cluster Assembly (CIA) pathway consists of eight proteins responsible for Iron-Sulfur cluster assembly and transfer to extramitochondrial apo-protein targets. Cfd1 and Nbp35 are two of these proteins that are responsible for assembling and transferring Iron-Sulfur clusters. Unlike other CIA proteins they also possess the ability to hydrolyze ATP. When both of them were purified in our lab, there are co-purified contaminants. It is unclear that if these co-purified contaminants contribute background activity to ATP hydrolysis. Therefore it has been my job to purify these proteins further and asses the affect of increased purity on ATPase activity by using an enzymatic readout of ATP hydrolysis. We found that most effective method for removing contaminants from Cfd1 and Nbp35 is using Co resin. Our results also suggest that co-purified contaminants are not ATPases.en-USCC0 1.0 Universalhttp://creativecommons.org/publicdomain/zero/1.0/Presentation