caa a22 4500 477082971 CHVBK 20180405111455.0 cr unu---uuuuu 170330e19961201xx s 000 0 eng 10.1007/BF01952104 doi (NATIONALLICENCE)springer-10.1007/BF01952104 Regulated protein degradation in mitochondria [Elektronische Daten] [T. Langer, W. Neupert] Various adenosine triphosphate (ATP)-dependent proteases were identified within mitochondria which mediate selective mitochondrial protein degradation and fulfill crucial functions in mitochondrial biogenesis. The matrix-localized PIM1 protease, a homologue of theEscherichia coli Lon protease, is required for respiration and maintenance of mitochondrial genome integrity. Degradation of non-native polypeptides by PIM1 protease depends on the chaperone activity of the mitochondrial Hsp70 system, posing intriguing questions about the relation between the proteolytic system and the folding machinery in mitochondria. The mitochondrial inner membrane harbors two ATP-dependent metallopeptidases, them- and thei-AAA protease, which expose their catalytic sites to opposite membrane surfaces and cooperate in the degradation of inner membrane proteins. In addition to its proteolytic activity, them-AAA protease has chaperone-like activity during the assembly of respiratory and ATP-synthase complexes. It constitutes a quality control system in the inner membrane for membrane-embedded protein complexes. Birkhäuser Verlag, 1996 Mitochondria nationallicence proteolysis nationallicence PIM1 protease nationallicence AAA protease nationallicence chaperone nationallicence Langer T. Institut für Physiologische Chemie der Universität München, Goethestr. 33, D-80336, München, (Germany) aut Neupert W. Institut für Physiologische Chemie der Universität München, Goethestr. 33, D-80336, München, (Germany) aut Experientia Birkhäuser-Verlag 52/12(1996-12-01), 1069-1076 0014-4754 52:12<1069 1996 52 18 https://doi.org/10.1007/BF01952104 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01952104 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Langer T. Institut für Physiologische Chemie der Universität München, Goethestr. 33, D-80336, München, (Germany) aut NATIONALLICENCE 700 1- Neupert W. Institut für Physiologische Chemie der Universität München, Goethestr. 33, D-80336, München, (Germany) aut NATIONALLICENCE 773 0- Experientia Birkhäuser-Verlag 52/12(1996-12-01), 1069-1076 0014-4754 52:12<1069 1996 52 18 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer