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Meinecke M, et al.  (2006) Tim50 maintains the permeability barrier of the mitochondrial inner membrane. Science 312(5779):1523-6

Abstract: Transport of metabolites across the mitochondrial inner membrane is highly selective, thereby maintaining the electrochemical proton gradient that functions as the main driving force for cellular adenosine triphosphate synthesis. Mitochondria import many preproteins via the presequence translocase of the inner membrane. However, the reconstituted Tim23 protein constitutes a pore remaining mainly in its open form, a state that would be deleterious in organello. We found that the intermembrane space domain of Tim50 induced the Tim23 channel to close. Presequences overcame this effect and activated the channel for translocation. Thus, the hydrophilic cis domain of Tim50 maintains the permeability barrier of mitochondria by closing the translocation pore in a presequence-regulated manner.

Status: Published Type: Journal Article | Research Support, Non-U.S. Gov't PubMed ID: 16763150

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PAM18 SSC1 TIM17 TIM21 TIM23 TIM44 TIM50
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