Conformational changes in BID, a pro-apoptotic BCL-2 family member, upon membrane binding

A site-directed spin labeling study

Joon Oh Kyoung, Scott Barbuto, Natalie Meyer, Ryung S. Kim, M. John Collier, Stanley J. Korsmeyer

Research output: Contribution to journalArticle

69 Citations (Scopus)

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 δ-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 α-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.

Original languageEnglish (US)
Pages (from-to)753-767
Number of pages15
JournalJournal of Biological Chemistry
Volume280
Issue number1
DOIs
StatePublished - Jan 7 2005
Externally publishedYes

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Labeling
Colicins
Diphtheria Toxin
Binding Sites
Lipid Bilayers
Membranes
Lipid bilayers
Protein Structural Homology
Bacterial Toxins
Protein Unfolding
Electron Spin Resonance Spectroscopy
Mitochondrial Membranes
Endotoxins
Proteins
Die casting inserts
Spectrum Analysis
Apoptosis
Paramagnetic resonance
Lipids
Conformations

ASJC Scopus subject areas

  • Biochemistry

Cite this

Conformational changes in BID, a pro-apoptotic BCL-2 family member, upon membrane binding : A site-directed spin labeling study. / Kyoung, Joon Oh; Barbuto, Scott; Meyer, Natalie; Kim, Ryung S.; Collier, M. John; Korsmeyer, Stanley J.

In: Journal of Biological Chemistry, Vol. 280, No. 1, 07.01.2005, p. 753-767.

Research output: Contribution to journalArticle

Kyoung, Joon Oh ; Barbuto, Scott ; Meyer, Natalie ; Kim, Ryung S. ; Collier, M. John ; Korsmeyer, Stanley J. / Conformational changes in BID, a pro-apoptotic BCL-2 family member, upon membrane binding : A site-directed spin labeling study. In: Journal of Biological Chemistry. 2005 ; Vol. 280, No. 1. pp. 753-767.
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