| Literature DB >> 2557158 |
T Söllner1, G Griffiths, R Pfaller, N Pfanner, W Neupert.
Abstract
We have identified a 19 kd protein of the mitochondrial outer membrane (MOM19). Monospecific IgG and Fab fragments directed against MOM19 inhibit import of precursor proteins destined for the various mitochondrial subcompartments, including porin, cytochrome c1, Fe/S protein, F0 ATPase subunit 9, and F1 ATPase subunit beta. Inhibition occurs at the level of high affinity binding of precursors to mitochondria. Consistent with previous functional studies that suggested the existence of distinct import sites for ADP/ATP carrier and cytochrome c, we find that import of those precursors is not inhibited. We conclude that MOM19 is identical to, or closely associated with, a specific mitochondrial import receptor.Entities:
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Year: 1989 PMID: 2557158 DOI: 10.1016/0092-8674(89)90762-9
Source DB: PubMed Journal: Cell ISSN: 0092-8674 Impact factor: 41.582