Chaperoning through the mitochondrial intermembrane space.
The first high-resolution structure of a mitochondrial translocase complex, the Tim9-Tim10 chaperone, is reported by Webb et al. (2006) in a recent issue of Molecular Cell, providing important insight in the transport of hydrophobic proteins through the aqueous intermembrane space and the mechanisms of protein assembly.
Wiedemann
Nils
N
Institut für Biochemie und Molekularbiologie, Universität Freiburg, Hermann-Herder-Strasse 7, D-79104 Freiburg, Germany.
Pfanner
Nikolaus
N
Chacinska
Agnieszka
A
D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D024101:Mitochondrial Proteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D046912:Multiprotein Complexes
D029968:Escherichia coli Proteins; D024101:Mitochondrial Proteins; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; C478387:TIM10 protein, E coli; C478388:TIM9 protein, E coli