Molecular basis for ATPase-powered substrate translocation by the Lon AAA+ protease. [PDF]
J Biol Chem, 2021 The Lon AAA+ (adenosine triphosphatases associated with diverse cellular activities) protease (LonA) converts ATP-fuelled conformational changes into sufficient mechanical force to drive translocation of the substrate into a hexameric proteolytic chamber.
Li S +5 more
europepmc +2 more sources
Unique Structural Features of the Mitochondrial AAA+ Protease AFG3L2 Reveal the Molecular Basis for Activity in Health and Disease. [PDF]
Mol Cell, 2019 Mitochondrial AAA+ quality control proteases regulate diverse aspects of mitochondrial biology through specialized protein degradation, but the underlying molecular mechanisms that define the diverse activities of these enzymes remain poorly defined. The
Puchades C +5 more
europepmc +2 more sources
Proteolytic regulation of mitochondrial magnesium channel by m-AAA protease and prohibitin complex. [PDF]
GeneticsMitochondrial membrane phospholipid cardiolipin is essential for the stability of several inner mitochondrial membrane protein complexes. We recently showed that the abundance of mitochondrial magnesium channel MRS2 is reduced in models of Barth syndrome,
Joshi A +3 more
europepmc +2 more sources
Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease. [PDF]
Elife, 2021 The Lon AAA+ proteases (LonA) is a ubiquitous ATP-dependent proteolytic machine, which selectively degrades damaged proteins or native proteins carrying exposed motifs (degrons).
Tzeng SR +6 more
europepmc +2 more sources
Insight into the RssB-Mediated Recognition and Delivery of σs to the AAA+ Protease, ClpXP. [PDF]
Biomolecules, 2020 In Escherichia coli, SigmaS (σS) is the master regulator of the general stress response. The cellular levels of σS are controlled by transcription, translation and protein stability.
Micevski D +6 more
europepmc +2 more sources
A Membrane-Bound Transcription Factor is Proteolytically Regulated by the AAA+ Protease FtsH in Staphylococcus aureus. [PDF]
J Bacteriol, 2020 Staphylococcus aureus is an important pathogenic bacterium causing various diseases in humans. In the bacterium, transcription is typically regulated by the transcription factors located in the cytoplasm.
Yeo WS +9 more
europepmc +2 more sources
Astrocyte-specific deletion of the mitochondrial m-AAA protease reveals glial contribution to neurodegeneration. [PDF]
Glia, 2019 Mitochondrial dysfunction causes neurodegeneration but whether impairment of mitochondrial homeostasis in astrocytes contributes to this pathological process remains largely unknown.
Murru S +9 more
europepmc +2 more sources
Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease. [PDF]
EMBO J, 2020 Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive.
Began J +13 more
europepmc +2 more sources
Polymerase delta-interacting protein 38 (PDIP38) modulates the stability and activity of the mitochondrial AAA+ protease CLPXP. [PDF]
Commun Biol, 2020 Over a decade ago Polymerase δ interacting protein of 38 kDa (PDIP38) was proposed to play a role in DNA repair. Since this time, both the physiological function and subcellular location of PDIP38 has remained ambiguous and our present understanding of ...
Strack PR +11 more
europepmc +2 more sources
AAA Proteases: Guardians of Mitochondrial Function and Homeostasis [PDF]
Cells, 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