PMID:21518899

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Citation

Arias-Cartin, R, Grimaldi, S, Pommier, J, Lanciano, P, Schaefer, C, Arnoux, P, Giordano, G, Guigliarelli, B and Magalon, A (2011) Cardiolipin-based respiratory complex activation in bacteria. Proc. Natl. Acad. Sci. U.S.A. 108:7781-6

Abstract

Anionic lipids play a variety of key roles in membrane function, including functional and structural effects on respiratory complexes. However, little is known about the molecular basis of these lipid-protein interactions. In this study, NarGHI, an anaerobic respiratory complex of Escherichia coli, has been used to investigate the relations in between membrane-bound proteins with phospholipids. Activity of the NarGHI complex is enhanced by anionic phospholipids both in vivo and in vitro. The anionic cardiolipin tightly associates with the NarGHI complex and is the most effective phospholipid to restore functionality of a nearly inactive detergent-solubilized enzyme complex. A specific cardiolipin-binding site is identified on the basis of the available X-ray diffraction data and of site-directed mutagenesis experiment. One acyl chain of cardiolipin is in close proximity to the heme b(D) center and is responsible for structural adjustments of b(D) and of the adjacent quinol substrate binding site. Finally, cardiolipin binding tunes the interaction with the quinol substrate. Together, our results provide a molecular basis for the activation of a bacterial respiratory complex by cardiolipin.

Links

PubMed PMC3093509 Online version:10.1073/pnas.1010427108

Keywords

Binding Sites; Cardiolipins/chemistry; Cardiolipins/metabolism; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins/chemistry; Electron Transport Chain Complex Proteins/genetics; Electron Transport Chain Complex Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Heme/chemistry; Membrane Lipids/chemistry; Membrane Lipids/metabolism; Models, Molecular; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/metabolism; Mutagenesis, Site-Directed; Mutant Proteins/chemistry; Mutant Proteins/genetics; Mutant Proteins/metabolism; Nitrate Reductase/chemistry; Nitrate Reductase/genetics; Nitrate Reductase/metabolism; Oxidoreductases/chemistry; Oxidoreductases/metabolism; Phospholipids/chemistry; Phospholipids/metabolism; Protein Interaction Domains and Motifs; Proteolipids/metabolism; Static Electricity

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