Signal recognition initiates reorganization of the presequence translocase during protein import.
The mitochondrial presequence translocase interacts with presequence-containing precursors at the intermembrane space (IMS) side of the inner membrane to mediate their translocation into the matrix. Little is known as too how these matrix-targeting signals activate the translocase in order to initiate precursor transport. Therefore, we analysed how signal recognition by ... the presequence translocase initiates reorganization among Tim-proteins during import. Our analyses revealed that the presequence receptor Tim50 interacts with Tim21 in a signal-sensitive manner in a process that involves the IMS-domain of the Tim23 channel. The signal-driven release of Tim21 from Tim50 promotes recruitment of Pam17 and thus triggers formation of the motor-associated form of the TIM23 complex required for matrix transport.
Mesh Terms:
Binding Sites, Carrier Proteins, Membrane Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Models, Molecular, Protein Binding, Protein Interaction Domains and Motifs, Protein Sorting Signals, Protein Structure, Secondary, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity
Binding Sites, Carrier Proteins, Membrane Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Models, Molecular, Protein Binding, Protein Interaction Domains and Motifs, Protein Sorting Signals, Protein Structure, Secondary, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Substrate Specificity
EMBO J.
Date: Mar. 20, 2013
PubMed ID: 23403928
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