PMID:15501827
| Citation |
Oh, KJ, Barbuto, S, Meyer, N, Kim, RS, Collier, RJ and Korsmeyer, SJ (2005) Conformational changes in BID, a pro-apoptotic BCL-2 family member, upon membrane binding. A site-directed spin labeling study. J. Biol. Chem. 280:753-67 |
|---|---|
| Abstract |
The BCL-2 family proteins constitute a critical control point in apoptosis. BCL-2 family proteins display structural homology to channel-forming bacterial toxins, such as colicins, transmembrane domain of diphtheria toxin, and the N-terminal domain of delta-endotoxin. By analogy, it has been hypothesized the BCL-2 family proteins would unfold and insert into the lipid bilayer upon membrane association. We applied the site-directed spin labeling method of electron paramagnetic resonance spectroscopy to the pro-apoptotic member BID. Here we show that helices 6-8 maintain an alpha-helical conformation in membranes with a lipid composition resembling mitochondrial outer membrane contact sites. However, unlike colicins and the transmembrane domain of diphtheria toxin, these helices of BID are bound to the lipid bilayer without adopting a transmembrane orientation. Our study presents a more detailed model for the reorganization of the structure of tBID on membranes. |
| Links |
PubMed Online version:10.1074/jbc.M405428200 |
| Keywords |
Amino Acid Sequence; Animals; BH3 Interacting Domain Death Agonist Protein; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Cattle; Cell Membrane/metabolism; Electron Spin Resonance Spectroscopy; Humans; Mice; Molecular Sequence Data; Molecular Structure; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Binding; Protein Conformation; Protein Structure, Secondary; Proto-Oncogene Proteins c-bcl-2/chemistry; Proto-Oncogene Proteins c-bcl-2/metabolism; Sequence Alignment; Spin Labels |
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