Journal of Molecular Biology
Volume 424, Issue 5, 14 December 2012, Pages 227-239
Impaired Folding of the Mitochondrial Small TIM Chaperones Induces Clearance by the i-AAA Protease
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Graphical Abstract
Highlights
► Individual cysteine residues of the CX3C motif in Tim9 and Tim10 are not essential for viability. ► A single disulfide bond in Tim9 and Tim10 is essential for function. ► Misfolded small TIM subunits are targeted for proteolytic degradation within mitochondria. ► Misfolded and unassembled small TIM subunits are degraded by Yme1.
Abbreviations
TOM
translocase of the outer membrane
TIM
translocase of the inner membrane
IMS
intermembrane space
MIA
mitochondrial IMS import and assembly machinery
AAA
ATPases associated with diverse cellular activities
BN-PAGE
blue native polyacrylamide gel electrophoresis
Yme1
yeast mitochondrial escape 1
5-FOA
5-fluoroorotic acid
AAC
ADP/ATP carrier
DHFR
dihydrofolate reductase
SAM
sorting and assembly machinery
TCA
trichloroacetic acid
i-AAA
IMS-AAA
Keywords
disulfide bond
intermembrane space
MIA
mitochondria
Yme1
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Copyright © 2012 Elsevier Ltd. Published by Elsevier Ltd.