The plant i-AAA protease controls the turnover of an essential mitochondrial protein import component.
J Cell Sci
; 131(2)2018 01 29.
Article
in En
| MEDLINE
| ID: mdl-28264925
ABSTRACT
Mitochondria are multifunctional organelles that play a central role in energy metabolism. Owing to the life-essential functions of these organelles, mitochondrial content, quality and dynamics are tightly controlled. Across the species, highly conserved ATP-dependent proteases prevent malfunction of mitochondria through versatile activities. This study focuses on a molecular function of the plant mitochondrial inner membrane-embedded AAA protease (denoted i-AAA) FTSH4, providing its first bona fide substrate. Here, we report that the abundance of the Tim17-2 protein, an essential component of the TIM1723 translocase (Tim17-2 together with Tim50 and Tim23), is directly controlled by the proteolytic activity of FTSH4. Plants that are lacking functional FTSH4 protease are characterized by significantly enhanced capacity of preprotein import through the TIM1723-dependent pathway. Taken together, with the observation that FTSH4 prevents accumulation of Tim17-2, our data point towards the role of this i-AAA protease in the regulation of mitochondrial biogenesis in plants.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Membrane Transport Proteins
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Arabidopsis Proteins
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Mitochondrial Membrane Transport Proteins
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Metalloproteases
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ATPases Associated with Diverse Cellular Activities
Language:
En
Journal:
J Cell Sci
Year:
2018
Document type:
Article