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J. Biol. Chem., Vol. 280, Issue 1, 753-767, January 7, 2005
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From the
Howard Hughes Medical Institute, the Department of Pathology and Medicine, Harvard Medical School, Dana-Farber Cancer Institute, the Department of Biostatistics, Harvard School of Public Health, and the ¶Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115
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 
-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 
-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.
Received for publication, May 17, 2004 , and in revised form, October 5, 2004.
* This work was supported in part by National Institutes of Health Grant PO1 CA68484 and the Dana-Farber Cancer Institute Multidisciplinary High-Tech Fund. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
|| To whom correspondence should be addressed: Howard Hughes Medical Institute, Dept. of Pathology and Medicine, Harvard Medical School, Dana-Farber Cancer Institute, Boston, MA 02115. Tel.: 617-632-6402; Fax: 617-632-6401; E-mail: Stanley_korsmeyer{at}dfci.harvard.edu.
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