Tim23 links the inner and outer mitochondrial membranes
Article Abstract:
The N-terminal domain of Tim23, a key component of the mitochondrial preprotein translocase, is now known to be exposed on the surface of the outer mitochondrial membrane. The spanning of two membranes on the part of Tim 23 is novel in membrane biology.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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The MIM complex mediates preprotein translocation across the mitochondrial inner membrane and couples it to the mt-Hsp70/ATP driving system
Article Abstract:
Two new proteins MIM33 and MIM14 are components of the mitochondrial inner membrane (MIM) besides two known proteins MIM23 and MIM17 which also form a part of the complex. The import of nuclear mitochondrial preproteins takes place in a coordinated manner across the mitochondrial membrane. Translocation systems in both the outer and inner membranes take part in the process. The MIM complex can accept preproteins and cause reversible transmembrane movement with mitochondrial outer membrane and unidirectional transport through linkage with the ATP-dependent mt-Hsp70-MIM44 system.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Role of tim23 as voltage sensor and presequence receptor in protein import into mitochondria
Article Abstract:
Membrane potential promotes the formation of dimers that display dynamic behavior by Tim23, an important component of the protein import machinery of the mitochondria's inner membrane. In turn, dimer dissociation is triggered when a matrix targeting sequence binds to Tim23. These all show that Tim23 significantly influences protein import.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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