Characterization of the Cytochrome c Membrane‐Binding Site Using Cardiolipin‐Containing Bicelles with NMR. Issue 45 (10th October 2016)

• Record Type: Journal Article
• Authors: Kobayashi, Hisashi; Nagao, Satoshi; Hirota, Shun
• Is Part Of: Angewandte Chemie international edition. Volume 55:Issue 45(2016)
• Page Start: 14019
• Page End: 14022
• Publication Date: 2016-10-10
• Subjects: bicelles -- cytochrome c -- membrane proteins -- protein–lipid interaction -- solution NMR; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201607419
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: Cytochrome (cyt) c transports electrons from Complex III to Complex IV in mitochondria. Cyt c is ordinarily anchored to the mitochondrial membrane through interaction with cardiolipin (CL), however its release into the cytosol initiates apoptosis. The cyt c interaction site with CL‐containing bicelles was characterized by NMR spectroscopy. Chemical shift perturbations in cyt c signals upon interaction with bicelles revealed that a relatively wide region, which includes the A‐site, the CXXCH motif, and the N‐ and C‐terminal helices, and contains multiple Lys residues, interacts cooperatively with CL. The specific cyt c –CL interaction increased with increasing CL molecules in the bicelles. The location of the cyt c interaction site for CL was similar to those for Complex III and Complex IV, thus indicating that cyt c recognizes lipids and partner proteins in a similar way. In addition to elucidating the cyt c membrane‐binding site, these results provide insight into the dynamic aspect of cyt c interactions in mitochondria. Abstract : Let's get together : The cytochrome (cyt) c interaction site for cardiolipin (CL)‐containing bicelles was characterized by solution NMR spectroscopy. Chemical shift perturbations in the cyt c signals upon interaction with the bicelles revealed that the location of the cyt c interaction site for CL was similar to those for Complex III and Complex IV.