Results 61 to 70 of about 401,347 (255)
Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain [PDF]
, 2013 Mitochondrial maintenance crucially depends on the quality control of proteins by various chaperones, proteases and repair enzymes. While most of the involved components have been studied in some detail, little is known on the biological role of the ...
Fischer, Fabian +3 more
core +1 more source
Structure and function of the bacterial AAA protease FtsH [PDF]
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012 Proteolysis of regulatory proteins or key enzymes of biosynthetic pathways is a universal mechanism to rapidly adjust the cellular proteome to particular environmental needs. Among the five energy-dependent AAA(+) proteases in Escherichia coli, FtsH is the only essential protease.
Langklotz, Sina +2 more
openaire +2 more sources
Frontiers in Molecular Biosciences, 2017 Cellular proteostasis involves not only the expression of proteins in response to environmental needs, but also the timely repair or removal of damaged or unneeded proteins. AAA+ motor proteins are critically involved in these pathways.
Elizabeth C. Duran +2 more
doaj +1 more source
Mitochondrial AAA proteases: A stairway to degradation
Mitochondrion, 2019 Mitochondrial protein quality control requires the action of proteases to remove damaged or unnecessary proteins and perform key regulatory cleavage events. Important components of the quality control network are the mitochondrial AAA proteases, which capture energy from ATP hydrolysis to destabilize and degrade protein substrates on both sides of the ...
Tyler E, Steele, Steven E, Glynn
openaire +3 more sources
Same structure, different mechanisms?
eLife, 2020 Two interpretations of similar structures for the same molecular machine illustrate the limits of inferring biochemical mechanism from protein structure.
Francis TF Tsai, Christopher P Hill
doaj +1 more source
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching. [PDF]
, 2015 The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family.
Corbett, Kevin D +5 more
core +2 more sources
Polypeptide Translocation by the AAA+ ClpXP Protease Machine
Chemistry & Biology, 2009 In the AAA+ ClpXP protease, ClpX uses repeated cycles of ATP hydrolysis to pull native proteins apart and to translocate the denatured polypeptide into ClpP for degradation. Here, we probe polypeptide features important for translocation. ClpXP degrades diverse synthetic peptide substrates despite major differences in side-chain chirality, size, and ...
Barkow, Sarah R. +3 more
openaire +4 more sources
The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission
Journal of Cell Biology, 2014 OPA1 processing by YEM1L and OMA1 is dispensable for mitochondrial fusion and instead drives mitochondrial fragmentation, which is crucial for mitochondrial integrity and quality control.
Ruchika Anand +6 more
semanticscholar +1 more source
Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation. [PDF]
, 2019 The 26S proteasome is essential for proteostasis and the regulation of vital processes through ATP-dependent degradation of ubiquitinated substrates. To accomplish the multi-step degradation process, the proteasomes regulatory particle, consisting of lid
Aufderheide +42 more
core +1 more source
Engineering fluorescent protein substrates for the AAA+ Lon protease [PDF]
Protein Engineering Design and Selection, 2013 AAA+ proteases, such as Escherichia coli Lon, recognize protein substrates by binding to specific peptide degrons and then unfold and translocate the protein into an internal degradation chamber for proteolysis. For some AAA+ proteases, attaching specific degrons to the N- or C-terminus of green fluorescent protein (GFP) generates useful substrates ...
Matthew L, Wohlever +3 more
openaire +2 more sources