Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45
نویسندگان
چکیده
منابع مشابه
Mitochondrial inner-membrane protease Yme1 degrades outer-membrane proteins Tom22 and Om45.
Mitochondria are double-membraned organelles playing essential metabolic and signaling functions. The mitochondrial proteome is under surveillance by two proteolysis systems: the ubiquitin-proteasome system degrades mitochondrial outer-membrane (MOM) proteins, and the AAA proteases maintain the proteostasis of intramitochondrial compartments. We previously identified a Doa1-Cdc48-Ufd1-Npl4 comp...
متن کاملStructure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing.
We present an atomic model of a substrate-bound inner mitochondrial membrane AAA+ quality control protease in yeast, YME1. Our ~3.4-angstrom cryo-electron microscopy structure reveals how the adenosine triphosphatases (ATPases) form a closed spiral staircase encircling an unfolded substrate, directing it toward the flat, symmetric protease ring. Three coexisting nucleotide states allosterically...
متن کاملThe Extractability of Inner-Membrane Proteins from Salmonella typhimurium Intact Cells, Spheroplasts and Inner-Membrane Fragments by Non-Denaturing Detergents
The effect of Triton X-100, Na cholate and Tween 80 on the solubilization of integral membrane proteins in intact cells, spheroplasts and inner-membrane fragments of Salmonella typhimurium was studied. The detergents were used in various concentrations (1.6 to 64 mM) and cytochromes b and d were used as marker to monitor the solubilization of membrane-bound proteins. Results showed that no inne...
متن کاملSorting pathways of mitochondrial inner membrane proteins.
Two distinct pathways of sorting and assembly of nuclear-encoded mitochondrial inner membrane proteins are described. In the first pathway, precursor proteins that carry amino-terminal targeting signals are initially translocated via contact sites between both mitochondrial membranes into the mitochondrial matrix. They become proteolytically processed, interact with the 60-kDa heat-shock protei...
متن کاملA novel import route for an N-anchor mitochondrial outer membrane protein aided by the TIM23 complex.
The membrane topology of Om45 in the yeast mitochondrial outer membrane (OM) is under debate. Here, we confirm that Om45 is anchored to the OM from the intermembrane space (IMS) by its N-terminal hydrophobic segment. We show that import of Om45 requires the presequence receptors, Tom20 and Tom22, and the import channel of Tom40. Unlike any of the known OM proteins, Om45 import requires the TIM2...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Cell Biology
سال: 2017
ISSN: 0021-9525,1540-8140
DOI: 10.1083/jcb.201702125