ATP hydrolysis tunes specificity of a AAA+ protease. [PDF]
Cell Rep, 2022 SummaryIn bacteria, AAA+ proteases such as Lon and ClpXP degrade substrates with exquisite specificity. These machines capture the energy of ATP hydrolysis to power unfolding and degradation of target substrates. Here, we show that a mutation in the ATP binding site of ClpX shifts protease specificity to promote degradation of normally Lon-restricted ...
Mahmoud SA, Aldikacti B, Chien P.
europepmc +5 more sources
A proteomic study of
BMC Microbiology, 2007 Background The influence of the membrane-bound AAA+ protease FtsH on membrane and cytoplasmic proteins of Corynebacterium glutamicum was investigated in this study.
Schluesener Daniela +4 more
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Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing. [PDF]
Science, 2017 Puchades C +6 more
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The membrane scaffold SLP2 anchors a proteolytic hub in mitochondria containing PARL and the i-AAA protease YME1L. [PDF]
EMBO Rep, 2016 Wai T +11 more
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Identification of a Degradation Signal Sequence within Substrates of the Mitochondrial i-AAA Protease. [PDF]
J Mol Biol, 2017 Rampello AJ, Glynn SE.
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ATPase and protease domain movements in the bacterial AAA+ protease FtsH are driven by thermal fluctuations [PDF]
Journal of Molecular Biology, 2018 AAA+ proteases are essential players in cellular pathways of protein degradation. Elucidating their conformational behavior is key for understanding their reaction mechanism and, importantly, for elaborating our understanding of mutation-induced protease
Martine Ruer +3 more
semanticscholar +3 more sources
Cryo-EM structure of the entire FtsH-HflKC AAA protease complex.
Cell Reports, 2022 The membrane-bound AAA protease FtsH is the key player controlling protein quality in bacteria. Two single-pass membrane proteins, HflK and HflC, interact with FtsH to modulate its proteolytic activity. Here, we present structure of the entire FtsH-HflKC
Z. Qiao +7 more
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The FASEB Journal, 2023 Cerebral ischemia–reperfusion (I/R) injury as the consequence of revascularization after ischemic stroke is associated with mitochondrial dysfunction, oxidative stress, and neuron loss.
Xiaosheng Yang +4 more
semanticscholar +1 more source
Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7. [PDF]
PLoS ONE, 2009 Paraplegin is an m-AAA protease of the mitochondrial inner membrane that is linked to hereditary spastic paraplegias. The gene encodes an FtsH-homology protease domain in tandem with an AAA+ homology ATPase domain.
Tobias Karlberg +6 more
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Structures of the human LONP1 protease reveal regulatory steps involved in protease activation
Nature Communications, 2021 The human mitochondrial protease LONP1 is an AAA+ ATP-dependent quality control protease. Here, the authors present the cryo-EM structures of human LONP1 in three distinct states and provide insights into the mechanism and regulation of this important ...
Mia Shin +7 more
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