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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Montagner, Caroline Forge, Vincent Chenal, Alexandre Barumandzadhe, Roya Vernier, Grégory Vitrac, Heidi |
| Description | Country affiliation: France Author Affiliation: Vernier G ( Laboratoire de Biophysique Moléculaire et Cellulaire, Unité Mixte de Recherche 5090, Département Réponse et Dynamique Cellulaires, CEA-Grenoble, 38054 Grenoble cedex 9, France.) |
| Abstract | The last step of the folding reaction of myoglobin is the incorporation of a prosthetic group. In cells, myoglobin is soluble, while heme resides in the mitochondrial membrane. We report here an exhaustive study of the interactions of apomyoglobin with lipid vesicles. We show that apomyoglobin interacts with large unilamellar vesicles under acidic conditions, and that this requires the presence of negatively charged phospholipids. The pH dependence of apomyoglobin interactions with membranes is a two-step process, and involves a partially folded state stabilized at acidic pH. An evident role for the interaction of apomyoglobin with lipid bilayers would be to facilitate the uptake of heme from the outer mitochondrial membrane. However, heme binding to apomyoglobin is observed at neutral pH when the protein remains in solution, and slows down as the pH becomes more favorable to membrane interactions. The effective incorporation of soluble heme into apomyoglobin at neutral pH suggests that the interaction of apomyoglobin with membranes is not necessary for the heme uptake from the lipid bilayer. In vivo, however, the ability of apomyoglobin to interact with membrane may facilitate its localization in the vicinity of the mitochondrial membranes, and so may increase the yield of heme uptake. Moreover, the behavior of apomyoglobin in the presence of membranes shows striking similarities with that of other proteins with a globin fold. This suggests that the globin fold is well adapted for soluble proteins whose functions require interactions with membranes. |
| ISSN | 09618368 |
| e-ISSN | 1469896X |
| Journal | Protein Science |
| Issue Number | 3 |
| Volume Number | 16 |
| Language | English |
| Publisher | Wiley-Blackwell (on behalf of The Protein Society) |
| Publisher Date | 2007-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Apoproteins Chemistry Heme Lipids Membranes, Artificial Myoglobin Circular Dichroism Hydrogen-ion Concentration Kinetics Lipid Bilayers Permeability Phosphatidic Acids Phosphatidylcholines Protein Binding Protein Folding Protein Structure, Secondary Scattering, Radiation Spectrometry, Fluorescence Research Support, Non-u.s. Gov't Discipline Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Biochemistry |
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