We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins.
- Authors
Nijtmans, L G; de Jong, L; Artal Sanz, M; Coates, P J; Berden, J A; Back, J W; Muijsers, A O; van der Spek, H; Grivell, L A
- Abstract
Prohibitins are ubiquitous, abundant and evolutionarily strongly conserved proteins that play a role in important cellular processes. Using blue native electrophoresis we have demonstrated that human prohibitin and Bap37 together form a large complex in the mitochondrial inner membrane. This complex is similar in size to the yeast complex formed by the homologues Phb1p and Phb2p. In yeast, levels of this complex are increased on co-overexpression of both Phb1p and Phb2p, suggesting that these two proteins are the only components of the complex. Pulse-chase experiments with mitochondria isolated from phb1/phb2-null and PHB1/2 overexpressing cells show that the Phb1/2 complex is able to stabilize newly synthesized mitochondrial translation products. This stabilization probably occurs through a direct interaction because association of mitochondrial translation products with the Phb1/2 complex could be demonstrated. The fact that Phb1/2 is a large multimeric complex, which provides protection of native peptides against proteolysis, suggests a functional homology with protein chaperones with respect to their ability to hold and prevent misfolding of newly synthesized proteins.
- Publication
The EMBO journal, 2000, Vol 19, Issue 11, p2444
- ISSN
0261-4189
- Publication type
Journal Article
- DOI
10.1093/emboj/19.11.2444