title: Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes.
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.
authors.affiliation: From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and.
authors.forename: Rakhi
authors.initials: R
authors.lastname: Bajaj
authors.affiliation: From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and the German Center for Neurodegenerative Diseases (DZNE), 37077 Göttingen and.
authors.forename: Francesca
authors.initials: F
authors.lastname: Munari
authors.affiliation: From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and.
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.affiliation: From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and the German Center for Neurodegenerative Diseases (DZNE), 37077 Göttingen and the Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), University Medicine Göttingen, 37073 Göttingen, Germany markus.zweckstetter@dzne.de.
authors.forename: Markus
authors.initials: M
authors.lastname: Zweckstetter
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002308:Cardiolipins / Q000494:pharmacology; D002417:Cattle; D057927:Hydrophobic and Hydrophilic Interactions; D008081:Liposomes / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000378:metabolism*; D051336:Mitochondrial Membranes / Q000187:drug effects / Q000378:metabolism*; D000090622:Mitochondrial Precursor Protein Import Complex Proteins; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D021381:Protein Transport; D012441:Saccharomyces cerevisiae; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D002308:Cardiolipins; D008081:Liposomes; D026901:Membrane Transport Proteins; D000090622:Mitochondrial Precursor Protein Import Complex Proteins; D029701:Saccharomyces cerevisiae Proteins; C083081:TIM23 protein, S cerevisiae
keywords: Lipid; Membrane; Mitochondria; Nuclear Magnetic Resonance (NMR); Protein Import; Protein Translocation