Studies on a possible molecular basis for the structure of mitochondrial cristae.
We have investigated a possible molecular basis for mitochondrial cristae formation. Proteoliposomes containing electron transport proteins, cytochrome oxidase, or complex III in their proper orientation bind to pig heart mitoplasts but not pig heart mitochondria. Using Leydig tumor cells, we have confirmed earlier reports that chloramphenicol causes a diminution in cristae content and a change in its characteristic lamellar form. We show that the proteoliposomes containing cytochrome oxidase or complex III in the proper orientation bind to mitoplasts from Leydig tumor cells but do not bind as well to mitoplasts from chloramphenicol-treated Leydig tumor cells. These experiments provide a possible mechanism to explain cristae formation.
Sumegi
B
B
Pre-clinical Science Unit, VA Medical Center, Dallas, TX 75216.
Freeman
D A
DA
Inman
L
L
Srere
P A
PA
D000818:Animals; D002701:Chloramphenicol / Q000494:pharmacology; D014450:Electron Transport Complex III / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000378:metabolism; D066298:In Vitro Techniques; D008081:Liposomes; D008854:Microscopy, Electron; D008929:Mitochondria, Heart / Q000378:metabolism / Q000648:ultrastructure; D011510:Proteolipids / Q000378:metabolism; D013367:Submitochondrial Particles / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D013552:Swine; D014407:Tumor Cells, Cultured / Q000187:drug effects / Q000378:metabolism / Q000648:ultrastructure
D008081:Liposomes; D011510:Proteolipids; C020485:proteoliposomes; D002701:Chloramphenicol; D003576:Electron Transport Complex IV; D014450:Electron Transport Complex III