caa a22 4500 477082939 CHVBK 20180405111455.0 cr unu---uuuuu 170330e19961201xx s 000 0 eng 10.1007/BF01952105 doi (NATIONALLICENCE)springer-10.1007/BF01952105 The mitochondrial processing peptidase: Function and specificity [Elektronische Daten] [P. Luciano, V. Géli] Targeting signals of mitochondrial precursors are cleaved in the matrix during or after import by the mitochondrial processing peptidase (MPP). This enzyme consists of two nonidenticalα- andβ-subunits each of molecular weight of about 50 kDa. In mammals and fungi, MPP is soluble in the matrix, whereas in plants the enzyme is part of the cytochromebc 1 complex. MPP is a metalloendopeptidase which has been classified as a member of the pitrilysin family on the basis of the HXXEHX76E zinc-binding motif present inβ-MPP. Both subunits of MPP are required for processing activity. Theα-subunit of MPP, which probably recognizes a three-dimensional motif adopted by the presequence, presents the presequence toβ-MPP, which carries the catalytic active site. MPP acts as an endoprotease on chemically synthesized peptides corresponding to mitochondrial presequences. Matrix-targeting signals and MPP cleavage signals seem to be distinct, although the two signals may overlap within a given presequence. The structural element helix-turn-helix, that cleavable presequences adopt in a membrane mimetic environment, may be required for processing but is not sufficient for proteolysis. Binding of the presequence byα-MPP tolerates a high degree of mutations of the presequence.α-MPP may present a degenerated cleavage site motif toβ-MPP in an accessible conformation for processing. The conformation of mitochondrial presequences bound to MPP remains largely unknown. Birkhäuser Verlag, 1996 Mitochondrial import nationallicence metallopeptidases nationallicence processing nationallicence matrix-targeting sequences nationallicence zinc-binding motif nationallicence holoenzyme nationallicence Luciano P. Laboratoire d'Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, F-13402, Marseille Cedex 20, (France) aut Géli V. Laboratoire d'Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, F-13402, Marseille Cedex 20, (France) aut Experientia Birkhäuser-Verlag 52/12(1996-12-01), 1077-1082 0014-4754 52:12<1077 1996 52 18 https://doi.org/10.1007/BF01952105 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF01952105 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Luciano P. Laboratoire d'Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, F-13402, Marseille Cedex 20, (France) aut NATIONALLICENCE 700 1- Géli V. Laboratoire d'Ingéniérie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, F-13402, Marseille Cedex 20, (France) aut NATIONALLICENCE 773 0- Experientia Birkhäuser-Verlag 52/12(1996-12-01), 1077-1082 0014-4754 52:12<1077 1996 52 18 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer