Many mitochondrial proteins perform their functions as components of large, multimeric complexes. Chemical crosslinking is a powerful method to analyze protein-protein interactions within such complexes. Using membrane-permeable crosslinkers and isolated intact mitochondria, protein-protein interactions that are secluded by two mitochondrial membranes can be readily analyzed in physiologically active, isolated organelles under a variety of physiological and pathophysiological conditions. Here, we describe two methods for chemical crosslinking in intact yeast mitochondria. The first method enables the analysis of ATP-dependent remodeling of mitochondrial protein complexes while the second one allows the identification of crosslinking partners of a protein of interest.
CITATION STYLE
Banerjee, R., Günsel, U., & Mokranjac, D. (2017). Chemical crosslinking in intact mitochondria. In Methods in Molecular Biology (Vol. 1567, pp. 139–154). Humana Press Inc. https://doi.org/10.1007/978-1-4939-6824-4_9
Mendeley helps you to discover research relevant for your work.