Interaction of Dystrophin Rod Domain with Membrane Phospholipids
| العنوان: | Interaction of Dystrophin Rod Domain with Membrane Phospholipids |
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| المؤلفون: | Jacques Gallay, Michel Vincent, Yann Fichou, François Gaboriau, Elisabeth Le Rumeur, Sandrine Pottier, Arnaud Bondon, Corinne Rondeau-Mouro |
| المساهمون: | Laboratoire de résonance magnétique en biologie et en médecine, Université de Rennes (UR)-IFR91, Groupe de Recherche en Thérapeutique Anticancéreuse (Faculté de Médecine), Groupe de Recherche en Thérapeutique Anticancéreuse - Faculté de Médecine, Laboratoire pour l'utilisation du rayonnement électromagnétique (LURE), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-MENRT-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | Journal of Biological Chemistry Journal of Biological Chemistry, 2003, 278 (8), pp.5993-6001. ⟨10.1074/jbc.M207321200⟩ |
| بيانات النشر: | Elsevier BV, 2003. |
| سنة النشر: | 2003 |
| مصطلحات موضوعية: | 0303 health sciences, Quenching (fluorescence), Chemistry, [SDV]Life Sciences [q-bio], Vesicle, Membrane lipids, Tryptophan, Cell Biology, Biochemistry, 03 medical and health sciences, Crystallography, 0302 clinical medicine, Membrane, Protein structure, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, Protein folding, Molecular Biology, 030217 neurology & neurosurgery, 030304 developmental biology, Binding domain |
| الوصف: | International audience; Dystrophin is assumed to act via the central rod domain as a flexible linker between the amino-terminal actin binding domain and carboxyl-terminal proteins associated with the membrane. The rod domain is made up of 24 spectrin-like repeats and has been shown to modify the physical properties of lipid membranes. The nature of this association still remains unclear. Trypto-phan residues tend to cluster at or near to the water-lipid interface of the membrane. To assess dystrophin rod domain-membrane interactions, tryptophan residues properties of two recombinant proteins of the rod domain were examined by 1 H NMR and fluorescence techniques in the presence of membrane lipids. F114 (residues 439-553) is a partly folded protein as inferred from 1 H NMR, tryptophan fluorescence emission intensity , and the excited state lifetime. By contrast, F125 (residues 439-564) is a folded compact protein. Trypto-phan fluorescence quenching shows that both proteins are characterized by structural fluctuations with their tryptophan residues only slightly buried from the surface. In the presence of negatively charged small vesi-cles, the fluorescence characteristics of F125 change dramatically, indicating that tryptophan residues are in a more hydrophobic environment. Interestingly, these modifications are not observed with F114. Fluorescence quenching experiments confirm that tryptophan residues are shielded from the solvent in the complex F125 lipids by a close contact with lipids. The use of membrane bound quenchers allowed us to conclude that dys-trophin rod domain lies along the membrane surface and may be involved in a structural array comprising membrane and cytoskeletal proteins as well as membrane lipids. |
| تدمد: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.m207321200 |
| DOI: | 10.1074/jbc.M207321200⟩ |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75e2a98c0ecadf79a3da4be9df381407 https://doi.org/10.1074/jbc.m207321200 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....75e2a98c0ecadf79a3da4be9df381407 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 00219258 1083351X |
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| DOI: | 10.1074/jbc.m207321200 |