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The Tim9p–Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier
TLDR
Results from inductively coupled plasma–mass spectrometry studies failed to detect zinc in the Tim9p–Tim10p complex, but the cysteine residues seemingly formed disulfide linkages and may prevent aggregation of the unfolded carrier proteins in the aqueous intermembrane space. Expand
Human deafness dystonia syndrome is a mitochondrial disease.
TLDR
It is shown that DDP is a mitochondrial protein and similar to five small proteins of the yeast mitochondrial intermembrane space that mediate the import of metabolite transporters from the cytoplasm into the mitochondrial inner membrane and interact structurally and functionally with Tim8p and Tim13p. Expand
Presence of a Member of the Mitochondrial Carrier Family in Hydrogenosomes: Conservation of Membrane-Targeting Pathways between Hydrogenosomes and Mitochondria
  • S. Dyall, C. Koehler, +5 authors Patricia J. Johnson
  • Biology, Medicine
  • Molecular and Cellular Biology
  • 1 April 2000
TLDR
These findings indicate that the membrane carriers and membrane protein-targeting machinery of hydrogenosomes and mitochondria have a common evolutionary origin and provide strong evidence that a single endosymbiont evolved into a progenitor organelle in early eukaryotic cells that ultimately give rise to these two distinct organelles. Expand
Tim18p, a New Subunit of the TIM22 Complex That Mediates Insertion of Imported Proteins into the Yeast Mitochondrial Inner Membrane
  • C. Koehler, Michael P. Murphy, +6 authors E. Or
  • Biology, Medicine
  • Molecular and Cellular Biology
  • 15 February 2000
TLDR
It is suggested that Tim18p functions in the assembly and stabilization of the TIM22 complex but does not directly participate in protein insertion into the inner membrane. Expand
The role of the Tim8p–Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins
TLDR
This study shows that Tim23p crosses the outer membrane as a loop before inserting into the inner membrane, and suggests that this translocation mechanism may be conserved. Expand
Different import pathways through the mitochondrial intermembrane space for inner membrane proteins
TLDR
Yeast mitochondria use multiple pathways for escorting hydrophobic inner membrane proteins across the aqueous intermembrane space and can transfer these proteins to one of three different membrane insertion sites: the TIM22 complex, the TIM23 complex or an as yet uncharacterized insertion site. Expand
The Role of Hot13p and Redox Chemistry in the Mitochondrial TIM22 Import Pathway*
TLDR
Results suggest that the small TIM complexes have a specialized assembly pathway in the intermembrane space and that the local redox state of the TIM complexes may mediate translocation of inner membrane proteins. Expand
The Essential Function of the Small Tim Proteins in the TIM22 Import Pathway Does Not Depend on Formation of the Soluble 70-Kilodalton Complex
TLDR
It is suggested that the 70-kDa complexes facilitate import, similar to the outer membrane receptors of the TOM (hetero-oligomeric translocase of the outer membranes) complex, and the essential role of Tim9p and Tim10p may be to mediate protein insertion in the inner membrane with the TIM22 complex. Expand
The Role of Tim9p in the Assembly of the TIM22 Import Complexes
TLDR
It is suggested that residues near the ‘twin CX3C’ motif are important for the assembly of Tim9p in both theTim9p–Tim10p complex and the 300‐kDa membrane complex. Expand
Tim54p connects inner membrane assembly and proteolytic pathways in the mitochondrion
TLDR
Tim54p has two independent functions: scaffolding/stability for the TIM22 membrane complex and assembly of Yme1p into a proteolytically active complex and links protein import, assembly, and turnover pathways in the mitochondrion. Expand
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