MPP hydrolyzes presequence of inner membrane precursors

Stable Identifier
R-SCE-1268019
Type
Reaction [transition]
Species
Saccharomyces cerevisiae
Compartment
General
SVG |   | PPTX  | SBGN
MPP hydrolyzes presequence of inner membrane precursors

The alpha subunit (MAS2, Alpha-MPP) of the mitochondrial processing peptidase (MPP) binds presequences of mitochondrial precursors and the beta subunit (MAS1, Beta-MPP) cleaves the presequence (Yang et al. 1991, Geli 1993, Luciano et al. 1997, Luciano et al. 1998, Taylor et al. 2001, Dvorakova-Hola et al. 2010). After cleavage, proteins destined for the inner membrane are released laterally from TIM23 SORT into the membrane.

Literature References
PubMed ID Title Journal Year
11470436 Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences

Taylor, AB, Smith, BS, Kitada, S, Kojima, K, Miyaura, H, Otwinowski, Z, Ito, A, Deisenhofer, J

Structure 2001
2007593 The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein

Yang, MJ, Geli, V, Oppliger, W, Suda, K, James, P, Schatz, G

J Biol Chem 1991
8327505 Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits

Géli, V

Proc Natl Acad Sci U S A 1993
9654444 The mitochondrial processing peptidase behaves as a zinc-metallopeptidase

Luciano, P, Tokatlidis, K, Chambre, I, Germanique, JC, Géli, V

J Mol Biol 1998
20053354 Glycine-rich loop of mitochondrial processing peptidase alpha-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20

Dvoráková-Holá, K, Matusková, A, Kubala, M, Otyepka, M, Kucera, T, Vecer, J, Herman, P, Parkhomenko, N, Kutejova, E, Janata, J

J Mol Biol 2010
9299349 Functional cooperation of the mitochondrial processing peptidase subunits

Luciano, P, Geoffroy, S, Brandt, A, Hernandez, JF, Géli, V

J Mol Biol 1997
Participants
Catalyst Activity

metalloendopeptidase activity of Mitochondrial processing peptidase [mitochondrial matrix]

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