Mechanisms of protein translocation into mitochondria |
| |
| Institution: | 1. Laboratory of Lymphocyte Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA;2. The Rockefeller Graduate Program, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA;3. Current address: Department of Biology, Harvey Mudd College, 301 Platt Bvd, Claremont, CA 91711, USA;1. The Royal Free Sheila Sherlock Liver Centre and Institute of Liver and Digestive Health, University College London and Royal Free Hospital, London, UK;2. Department of Clinical and Molecular Biomedicine, University of Catania, Garibaldi Hospital, Catania, Italy;3. Academic Department of Endocrinology, Royal Free Hospital, London, UK;1. Department of Medicine, Chi Mei Medical Center, Tainan, Taiwan;2. Department of Health and Nutrition, Chia Nan University of Pharmacy and Science, Tainan, Taiwan;3. Department of Intensive Care Medicine, Liouying, Tainan, Taiwan;4. Department of Nursing, Chi Mei Medical Center, Liouying, Tainan, Taiwan;1. Max Planck Institute for Chemical Ecology, Department of Evolutionary Neuroethology, 07745 Jena, Germany;1. Department of Anesthesiology, Beijing Tian Tan Hospital, Capital Medical University, #6 Tian Tan Xi Li, Beijing 100050, PR China;2. Department of Anesthesiology, Beijing Children’s Hospital, Capital Medical University, National Center for Children’s Health, #56 Nan Li Shi Lu, Beijing 100045, PR China;3. Department of Neurobiology and Beijing Institute for Neuroscience, Capital Medical University, #10 You An Men Wai Xi TouTiao, Beijing 100069, PR China;4. Department of Anesthesiology, University of California San Diego, 3350 La Jolla Village Dr., San Diego, CA 92161, USA;1. Department of Microbiology and Immunology, Meharry Medical College, Nashville, TN, USA;2. University of Pennsylvania, Philadelphia, USA |
| |
| Abstract: | Mitochondrial biogenesis utilizes a complex proteinaceous machinery for the import of cytosolically synthesized preproteins. At least three large multisubunit protein complexes, one in the outer membrane and two in the inner membrane, have been identified. These translocase complexes cooperate with soluble proteins from the cytosol, the intermembrane space and the matrix. The translocation of presequence-containing preproteins through the outer membrane channel includes successive electrostatic interactions of the charged mitochondrial targeting sequence with a chain of import components. Translocation across the inner mitochondrial membrane utilizes the energy of the proton motive force of the inner membrane and the hydrolysis of ATP. The matrix chaperone system of the mitochondrial heat shock protein 70 forms an ATP-dependent import motor by interaction with the polypeptide chain in transit and components of the inner membrane translocase. The precursors of integral inner membrane proteins of the metabolite carrier family interact with newly identified import components of the intermembrane space and are inserted into the inner membrane by a second translocase complex. A comparison of the full set of import components between the yeast Sacccharomyces cerevisiae and the nematode Caenorhabditis elegans demonstrates an evolutionary conservation of most components of the mitochondrial import machinery with a possible greater divergence for the import pathway of the inner membrane carrier proteins. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
