Unknown

Dataset Information

0

Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes.


ABSTRACT: Mitochondria possess an outer membrane (OMM) and an inner membrane (IMM), which folds into invaginations called cristae. Lipid composition, membrane potential, and proteins in the IMM influence organization of cristae. Here we show an essential role of the OMM protein Sam50 in the maintenance of the structure of cristae. Sam50 is a part of the sorting and assembly machinery (SAM) necessary for the assembly of ?-barrel proteins in the OMM. We provide evidence that the SAM components exist in a large protein complex together with the IMM proteins mitofilin and CHCHD3, which we term the mitochondrial intermembrane space bridging (MIB) complex. Interactions between OMM and IMM components of the MIB complex are crucial for the preservation of cristae. After destabilization of the MIB complex, we observed deficiency in the assembly of respiratory chain complexes. Long-term depletion of Sam50 influences the amounts of proteins from all large respiratory complexes that contain mitochondrially encoded subunits, pointing to a connection between the structural integrity of cristae, assembly of respiratory complexes, and/or the maintenance of mitochondrial DNA (mtDNA).

SUBMITTER: Ott C 

PROVIDER: S-EPMC3295012 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes.

Ott Christine C   Ross Katharina K   Straub Sebastian S   Thiede Bernd B   Götz Monika M   Goosmann Christian C   Krischke Markus M   Mueller Martin J MJ   Krohne Georg G   Rudel Thomas T   Kozjak-Pavlovic Vera V  

Molecular and cellular biology 20120117 6


Mitochondria possess an outer membrane (OMM) and an inner membrane (IMM), which folds into invaginations called cristae. Lipid composition, membrane potential, and proteins in the IMM influence organization of cristae. Here we show an essential role of the OMM protein Sam50 in the maintenance of the structure of cristae. Sam50 is a part of the sorting and assembly machinery (SAM) necessary for the assembly of β-barrel proteins in the OMM. We provide evidence that the SAM components exist in a la  ...[more]

Similar Datasets

| S-EPMC5665436 | biostudies-literature
| S-EPMC5203823 | biostudies-literature
| S-EPMC2662054 | biostudies-literature
| S-EPMC6808451 | biostudies-literature
| S-EPMC4485110 | biostudies-literature
| S-EPMC4620870 | biostudies-literature
| S-EPMC1221585 | biostudies-other
| S-EPMC5636749 | biostudies-literature
| S-EPMC6013907 | biostudies-literature
| S-EPMC6362269 | biostudies-literature