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Although substantial progress has been made in understanding the mechanisms underlying the expression of mtDNA-encoded polypeptides, the regulatory factors involved in mitoribosome-mediated synthesis and simultaneous insertion of mitochondrial oxidative phosphorylation (OXPHOS) polypeptides into the inner membrane of mitochondria are still unclear. In the present study, disruption of the mouse Crif1 gene, which encodes a mitochondrial protein, resulted in a profound deficiency in OXPHOS caused by the disappearance of OXPHOS subunits and complexes in vivo. CRIF1 was associated with large mitoribosomal subunits that were located close to the polypeptide exit tunnel, and the elimination of CRIF1 led to both aberrant synthesis and defective insertion of mtDNA-encoded nascent OXPHOS polypeptides into the inner membrane. CRIF1 interacted with nascent OXPHOS polypeptides and molecular chaperones, e.g., Tid1. Taken together, these results suggest that CRIF1 plays a critical role in the integration of OXPHOS polypeptides into the mitochondrial membrane in mammals. Copyright © 2012 Elsevier Inc. All rights reserved.


Soung Jung Kim, Min-chul Kwon, Min Jeong Ryu, Hyo Kyun Chung, Surendar Tadi, Yong Kyung Kim, Jin Man Kim, Sang Hee Lee, Ji Hoon Park, Gi Ryang Kweon, Seung-Wook Ryu, Young Suk Jo, Chul-Ho Lee, Hideyuki Hatakeyama, Yu-ichi Goto, Yong-Hyeon Yim, Jongkyeong Chung, Young-Yun Kong, Minho Shong. CRIF1 is essential for the synthesis and insertion of oxidative phosphorylation polypeptides in the mammalian mitochondrial membrane. Cell metabolism. 2012 Aug 8;16(2):274-83

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PMID: 22819524

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