Tim23 mediates protein translocation into mitochondria. Although inserted into the inner membrane, the dynamic association of its intermembrane space (IMS) domain with the outer membrane promotes protein import. However, little is known about the molecular basis of this interaction. Here, we demonstrate that the IMS domain of Tim23 tightly associates with both inner and outer mitochondrial membrane-like membranes through a hydrophobic anchor at its N terminus. The structure of membrane-bound Tim23(IMS) is highly dynamic, allowing recognition of both the incoming presequence and other translocase components at the translocation contact. Cardiolipin enhances Tim23 membrane attachment, suggesting that cardiolipin can influence preprotein import.

Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes

Munari, Francesca;
2014-01-01

Abstract

Tim23 mediates protein translocation into mitochondria. Although inserted into the inner membrane, the dynamic association of its intermembrane space (IMS) domain with the outer membrane promotes protein import. However, little is known about the molecular basis of this interaction. Here, we demonstrate that the IMS domain of Tim23 tightly associates with both inner and outer mitochondrial membrane-like membranes through a hydrophobic anchor at its N terminus. The structure of membrane-bound Tim23(IMS) is highly dynamic, allowing recognition of both the incoming presequence and other translocase components at the translocation contact. Cardiolipin enhances Tim23 membrane attachment, suggesting that cardiolipin can influence preprotein import.
2014
Lipid; Membrane; Mitochondria; Nuclear Magnetic Resonance (NMR); Protein Import; Protein Translocation; Amino Acid Sequence; Animals; Cardiolipins; Cattle; Hydrophobic and Hydrophilic Interactions; Liposomes; Membrane Transport Proteins; Mitochondrial Membranes; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; Protein Transport; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11562/973687
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