Results 11 to 20 of about 63,350 (232)

AAA Proteases: Guardians of Mitochondrial Function and Homeostasis [PDF]

open access: yesCells, 2018
Mitochondria are dynamic, semi-autonomous organelles that execute numerous life-sustaining tasks in eukaryotic cells. Functioning of mitochondria depends on the adequate action of versatile proteinaceous machineries. Fine-tuning of mitochondrial activity
Magdalena Opalińska, Hanna Jańska
doaj   +3 more sources

Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines [PDF]

open access: yesNature Reviews Microbiology, 2015
To maintain protein homeostasis, AAA+ proteolytic machines degrade damaged and unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP-dependent unfolding of a target protein and its subsequent translocation into a self-compartmentalized proteolytic chamber.
Adrian O Olivares   +2 more
exaly   +4 more sources

ATP hydrolysis tunes specificity of a AAA+ protease. [PDF]

open access: yesCell 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 Corynebacterium glutamicum AAA+ protease FtsH [PDF]

open access: yesBMC 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
doaj   +4 more sources

AAA+ protease-adaptor structures reveal altered conformations and ring specialization. [PDF]

open access: yesNat Struct Mol Biol, 2022
Abstract ClpAP, a two-ring AAA+ protease, degrades N-end-rule proteins bound by the ClpS adaptor. Here we present high-resolution cryo-EM structures of Escherichia coli ClpAPS complexes, showing how ClpA pore loops interact with the ClpS N-terminal extension (NTE), which is ...
Kim S, Fei X, Sauer RT, Baker TA.
europepmc   +4 more sources

Structural basis for distinct operational modes and protease activation in AAA+ protease Lon. [PDF]

open access: yesSci Adv, 2020
Substrate-free and -bound states of Lon reveal distinct operational modes used by the enzyme to process protein substrates.
Shin M   +7 more
europepmc   +4 more sources

Structure of the mitochondrial inner membrane AAA+ protease YME1 gives insight into substrate processing. [PDF]

open access: yesScience, 2017
Puchades C   +6 more
europepmc   +2 more sources

An FtsH protease is recruited to the mitochondrion of Plasmodium falciparum. [PDF]

open access: yesPLoS ONE, 2013
The two organelles, apicoplast and mitochondrion, of the malaria parasite Plasmodium falciparum have unique morphology in liver and blood stages; they undergo complex branching and looping prior to division and segregation into daughter merozoites ...
Aiman Tanveer   +5 more
doaj   +1 more source

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