M. Kiebler et al., THE MITOCHONDRIAL RECEPTOR COMPLEX - A CENTRAL ROLE OF MOM22 IN MEDIATING PREPROTEIN TRANSFER FROM RECEPTORS TO THE GENERAL INSERTION PORE, Cell, 74(3), 1993, pp. 483-492
The receptor complex in the mitochondrial outer membrane, which consis
ts of at least seven different proteins, is responsible for the recogn
ition and translocation of cytosolically synthesized preproteins. Two
of its subunits, MOM19 and MOM72, function as surface receptors for pr
eproteins. Four other subunits (MOM38, MOM30, MOM8, and MOM7) have bee
n suggested to constitute the general insertion pore (GIP). Here we re
port on the structure and function of MOM22. MOM22 is anchored in the
outer membrane by a single transmembrane segment. The highly negativel
y charged N-terminal domain is exposed to the cytosol and the C-termin
al domain to the intermembrane space. MOM22 appears to be a central co
mponent of the receptor complex, required for the transfer of preprote
ins from the receptors to the GIP. We speculate that the negatively ch
arged domain of MOM22 is involved in the transfer of positively charge
d signal sequences of preproteins.