Figure 7: The IMS domain of ATOM14 interacts with precursor proteins. | Scientific Reports

Figure 7: The IMS domain of ATOM14 interacts with precursor proteins.

From: Mitochondrial protein import - Functional analysis of the highly diverged Tom22 orthologue of Trypanosoma brucei

Figure 7

(A) Coomassie-stain of an SDS-gel showing total cellular extracts (T) and purified protein fractions (B) of E. coli cell lines expressing either the GST-tagged IMS domain of ATOM14 or unfused GST. (B) Binding of a mixture of precursor proteins to the Sepharose bound IMS domain of ATOM14. The gel shows an autoradiography of 2.5% of the input fraction consisting of the indicated [35S]-Met-labeled precursor proteins, and 100% of the eluates from the glutathione Sepharose beads. Two conditions were tested: in the first one the equal protein amounts (unfused and fused GST, ctrl 1) and in the second one equal bed volumes of the resin were compared (ctrl 2).

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