Binding of a tightly folded artificial mitochondrial precursor protein to the mitochondrial outer membrane involves a lipid-mediated conformational change.
نویسندگان
چکیده
An artificial mitochondrial precursor protein (the presequence of cytochrome oxidase subunit IV fused to mouse dihydrofolate reductase) binds to isolated yeast mitochondrial outer membranes and to liposomes whose phospholipid composition resembles that of outer membranes. In both cases, binding is strongly inhibited by low temperature or methotrexate (which stabilizes the dihydrofolate reductase moiety) and partly inhibited by adriamycin (which binds to acidic phospholipids). Binding is accompanied by partial unfolding of the protein. Binding of the urea-denatured fusion protein to outer membranes or liposomes is insensitive to low temperature, methotrexate, or adriamycin. These results, and those reported in the accompanying paper (Eilers, M., Endo, T., and Schatz, G. (1989) J. Biol. Chem. 264, 2945-2950) suggest that import of this fusion protein into isolated mitochondria involves at least partial unfolding by acidic phospholipids on the mitochondrial surface.
منابع مشابه
A COMPARATIW STUDY ON THE BINDING OF HEXOKINASE TO THE OUTER MITOCHONDRIAL MEMBRANE AND A HYDROPHOBIC MATRIX
متن کامل
A water-soluble form of porin from the mitochondrial outer membrane of Neurospora crassa. Properties and relationship to the biosynthetic precursor form.
Mitochondrial porin, the outer membrane pore-forming protein, was isolated in the presence of detergents and converted into a water-soluble form. This water-soluble porin existed under nondenaturing conditions as a mixture of dimers and oligomers. The proportion of dimers increased with decreasing porin concentration during conversion. Water-soluble porin inserted spontaneously into artificial ...
متن کاملCharacterization of biophysical properties of single chloride channel in rat brain mitochondrial inner membrane by channel incorporation into bilayer lipid membrane
Introduction: Recent studies have shown the presence of Cl- channels in heart and liver mitochondrial membranes. In this work, we have characterized the functional profile of a Cl- channel from rat brain mitochondria. Methods: After removing and homogenizing the rat brain, the supernatant was separately centrifuged in MSEdigitonin, H2O and Na2CO3 and mitochondrial inner membrane vesicles wer...
متن کاملToxicity mechanisms of Cigarette Smoke on Eye and Kidney using Isolated Mitochondria
Cigarette smoking is one of the main risk factors for premature human death associated to a variety of respiratory and vascular diseases, and cancer due to containing Hundreds of toxicants. Rat mitochondria were obtained by differential ultracentrifugation and incubated with different concentrations (1, 10 and 100%) of standardized cigarette smoke extract (CSE). Our results showed that cigarett...
متن کاملDifferential interactions of apo- and holocytochrome c with acidic membrane lipids in model systems and the implications for their import into mitochondria.
Monomolecular layers of lipid extracts of microsomal, mitochondrial outer and inner membranes, and pure lipid species have been used to measure their interaction with apo- and holocytochrome c. Large differences were observed both with respect to the nature and the lipid specificity of the interaction. The initial electrostatic interaction of the hemefree precursor apocytochrome c with anionic ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 264 5 شماره
صفحات -
تاریخ انتشار 1989