Results 31 to 40 of about 63,350 (232)
Peroxisomal Proteostasis Involves a Lon Family Protein That Functions as Protease and Chaperone [PDF]
, 2012 Proteins are subject to continuous quality control for optimal proteostasis. The knowledge of peroxisome quality control systems is still in its infancy. Here we show that peroxisomes contain a member of the Lon family of proteases (Pln).
Aksam +58 more
core +4 more sources
YoeB toxin is activated during thermal stress. [PDF]
, 2015 Type II toxin-antitoxin (TA) modules are thought to mediate stress-responses by temporarily suppressing protein synthesis while cells redirect transcription to adapt to environmental change.
Garza-Sánchez, Fernando +2 more
core +1 more source
Multifunctional Mitochondrial AAA Proteases [PDF]
Frontiers in Molecular Biosciences, 2017 Mitochondria perform numerous functions necessary for the survival of eukaryotic cells. These activities are coordinated by a diverse complement of proteins encoded in both the nuclear and mitochondrial genomes that must be properly organized and maintained.
openaire +3 more sources
Protein unfolding and degradation by the AAA+ Lon protease [PDF]
Protein Science, 2012 AbstractAAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. What determines the ability of different AAA+ enzymes to unfold and thus degrade different native protein substrates is currently ...
Eyal, Gur +2 more
openaire +2 more sources
A Peroxisomal Lon Protease and Peroxisome Degradation by Autophagy Play Key Roles in Vitality of Hansenula polymorpha Cells [PDF]
, 2007 In eukaryote cells various mechanisms exist that are responsible for the removal of non-functional proteins. Here we show that in the yeast Hansenula polymorpha (H.
Bener Aksam, Eda +5 more
core +2 more sources
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