Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrix.

ABSTRACT: More than 70% of mitochondrial proteins utilize N-terminal presequences as targeting signals. Presequence interactions with redundant cytosolic receptor domains of the translocase of the outer mitochondrial membrane (TOM) are well established. However, after the presequence enters the protein-conducting Tom40 channel, the recognition events that occur at the trans side leading up to the engagement of the presequence with inner membrane-bound receptors are less well defined. Using a photoaffinity-labeling approach with modified presequence peptides, we identified Tom40 as a presequence interactor of the TOM complex. Utilizing mass spectrometry, we mapped Tom40's presequence-interacting regions to both sides of the β-barrel. Analysis of a phosphorylation site within one of the presequence-in

SUBMITTER: Melin J 

PROVIDER: S-EPMC4135617 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature