ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae

Citation
L. Van Dyck et T. Langer, ATP-dependent proteases controlling mitochondrial function in the yeast Saccharomyces cerevisiae, CELL MOL L, 56(9-10), 1999, pp. 825-842
Citations number
136
Language
INGLESE
art.tipo
Review
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELLULAR AND MOLECULAR LIFE SCIENCES
ISSN journal
1420-682X → ACNP
Volume
56
Issue
9-10
Year of publication
1999
Pages
825 - 842
Database
ISI
SICI code
1420-682X(19991130)56:9-10<825:APCMFI>2.0.ZU;2-1
Abstract
Regulated protein degradation by ATP-dependent proteases plays a fundamenta l role in the biogenesis of mitochondria. Membrane-bound and soluble ATP-de pendent proteases have been identified in various subcompartments of this o rganelle. Subunits composing these proteases are evolutionarily conserved f rom yeast to humans and, in support of an endosymbiotic origin of mitochond ria, evolved from prokaryotic ancestors: the PIM1/Lon protease is active in the matrix of mitochondria, while the i-AAA protease and the m-AAA proteas e mediate the turnover of inner membrane proteins. Most of the knowledge co ncerning the biogenesis and the physiological role of ATP-dependent proteas es comes from studies in the yeast Saccharomyces cerevisiae. Proteases were found to be required for mitochondrial stasis, for the maintenance of the morphology of the organelle and for mitochondrial genome integrity. ATP-dep endent proteolysis is crucial for the expression of mitochondrially encoded subunits of respiratory chain complexes and for the assembly of these comp lexes. Hence, mitochondrial ATP-dependent proteases exert multiple roles wh ich are essential for the maintenance of cellular respiratory competence.