TY - JOUR
T1 - The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins
AU - Becker, Thomas
AU - Wenz, Lena-Sophie
AU - Kruger, Vivien
AU - Lehmann, Waltraut
AU - Muller, Judith
AU - Goroncy, Luise
AU - Zufall, Nicole
AU - Lithgow, Trevor
AU - Guiard, Bernard
AU - Chacinska, Agnieszka
AU - Wagner, Richard
AU - Meisinger, Chris
AU - Pfanner, Nikolaus
PY - 2011
Y1 - 2011
N2 - The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of beta-barrel proteins of the outer membrane. Several alpha-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of alpha-helical outer membrane proteins with multiple transmembrane segments.
AB - The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of beta-barrel proteins of the outer membrane. Several alpha-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of alpha-helical outer membrane proteins with multiple transmembrane segments.
UR - http://www.ncbi.nlm.nih.gov/pubmed/21825073
U2 - 10.1083/jcb.201102044
DO - 10.1083/jcb.201102044
M3 - Article
VL - 194
SP - 387
EP - 395
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 3
ER -