TY - JOUR
T1 - The three domains of the mitochondrial outer membrane protein Mim1 have discrete functions in assembly of the TOM complex
AU - Lueder, Franziska B
AU - Lithgow, Trevor James
PY - 2009
Y1 - 2009
N2 - The assembly of mitochondrial outer membrane proteins is an essential process, mediated by the SAM complex and a set of additional protein modules. We show that one of these, Mim1, is anchored in the outer membrane with its N-terminus exposed to the cytosol and its C-terminus in the mitochondrial intermembrane space. Using an in vitro assay to measure the multi-step pathway for assembly of Tom40 into the TOM complex, we find that an early reaction mediated by the SAM complex is regulated by the N-terminal domain of Mim1. In addition, a late reaction catalysed by the Sam37 subunit of the SAM complex is also influenced by Mim1. Thus, Mim1 participates at multiple stages in the assembly of the TOM complex.
AB - The assembly of mitochondrial outer membrane proteins is an essential process, mediated by the SAM complex and a set of additional protein modules. We show that one of these, Mim1, is anchored in the outer membrane with its N-terminus exposed to the cytosol and its C-terminus in the mitochondrial intermembrane space. Using an in vitro assay to measure the multi-step pathway for assembly of Tom40 into the TOM complex, we find that an early reaction mediated by the SAM complex is regulated by the N-terminal domain of Mim1. In addition, a late reaction catalysed by the Sam37 subunit of the SAM complex is also influenced by Mim1. Thus, Mim1 participates at multiple stages in the assembly of the TOM complex.
UR - http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19345216
U2 - 10.1016/j.febslet.2009.03.064
DO - 10.1016/j.febslet.2009.03.064
M3 - Article
SN - 0014-5793
VL - 583
SP - 1475
EP - 1480
JO - FEBS Letters
JF - FEBS Letters
IS - 9
ER -