title: Protein degradation in mitochondria.
abstract: The biogenesis of mitochondria and the maintenance of mitochondrial functions depends on an autonomous proteolytic system in the organelle which is highly conserved throughout evolution. Components of this system include processing peptidases and ATP-dependent proteases, as well as molecular chaperone proteins and protein complexes with apparently regulatory functions. While processing peptidases mediate maturation of nuclear-encoded mitochondrial preproteins, quality control within various subcompartments of mitochondria is ensured by ATP-dependent proteases which selectively remove non-assembled or misfolded polypeptides. Moreover; these proteases appear to control the activity- or steady-state levels of specific regulatory proteins and thereby ensure mitochondrial genome integrity, gene expression and protein assembly.
authors.affiliation: Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians-Universität München, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Käser
authors.forename: T
authors.initials: T
authors.lastname: Langer
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005656:Fungal Proteins / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D007425:Intracellular Membranes / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism
chemical_list: D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D011506:Proteins; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases