The novel mitochondrial matrix protease Ste23 is required for efficient presequence degradation and processing.
Mol Biol Cell
; 28(8): 997-1002, 2017 Apr 15.
Article
in En
| MEDLINE
| ID: mdl-28228553
ABSTRACT
Approximately 70% of mitochondrial precursor proteins are imported from the cytosol via N-terminal presequences, which are cleaved upon exposure to the mitochondrial processing protease MPP in the matrix. Cleaved presequence peptides then need to be efficiently degraded, and impairment of this clearance step, for example, by amyloid ß peptides, causes feedback inhibition of MPP, leading ultimately to accumulation of immature precursor proteins within mitochondria. Degradation of mitochondrial peptides is performed by Cym1 in yeast and its homologue, PreP, in humans. Here we identify the novel mitochondrial matrix protease Ste23 in yeast, a homologue of human insulin-degrading enzyme, which is required for efficient peptide degradation. Ste23 and Cym1 tightly cooperate to ensure the correct functioning of the essential presequence processing machinery.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Metalloendopeptidases
/
Saccharomyces cerevisiae Proteins
/
Protein Degradation End Products
/
Mitochondria
Limits:
Humans
Language:
En
Journal:
Mol Biol Cell
Journal subject:
BIOLOGIA MOLECULAR
Year:
2017
Type:
Article
Affiliation country:
Germany