Sam50 Functions in Mitochondrial Intermembrane Space Bridging and Biogenesis of Respiratory Complexes
Author(s) -
Christine Ott,
Katharina Roß,
Sebastian Straub,
Bernd Thiede,
Monika Götz,
Christian Goosmann,
Markus Krischke,
Martin J. Mueller,
Georg Krohne,
Thomas Rudel,
Vera KozjakPavlovic
Publication year - 2012
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.06388-11
Subject(s) - biology , intermembrane space , mitochondrial intermembrane space , microbiology and biotechnology , mitochondrion , inner mitochondrial membrane , biogenesis , inner membrane , protein targeting , translocase of the outer membrane , translocase of the inner membrane , membrane protein , bacterial outer membrane , biochemistry , membrane , mitochondrial membrane transport protein , gene , escherichia coli
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 large protein complex together with the IMM proteins mitofilin and CHCHD3, which we term them itochondriali ntermembrane spaceb ridging (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).
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom