Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism.
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Human LONP1 selectively degrades mildly oxidized aconitase, whereas severe aggregation makes it a poor substrate.
"Lon protease, an ATP-stimulated mitochondrial matrix protein, selectively recognizes and degrades the oxidized, hydrophobic form of aconitase after mild oxidative modification, but that severe oxidation results in aconitase aggregation, which makes it a poor substrate for Lon."
DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate.
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Human LONP1 is a mitochondrial-matrix homo-oligomer that binds GT-rich single-stranded mtDNA.
"Eukaryotic Lon is a homo-oligomeric ring-shaped complex localized to the mitochondrial matrix. In vitro, human Lon binds specifically to a single-stranded GT-rich DNA sequence overlapping the light strand promoter of human mitochondrial DNA (mtDNA)."
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Human LONP1 co-immunoprecipitates with POLG and TWNK.
"Co-immunoprecipitation experiments show that Lon interacts with mtDNA polymerase gamma and the Twinkle helicase, which are components of mitochondrial nucleoids."
Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death.
HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells.
Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance.
The layered structure of human mitochondrial DNA nucleoids.
Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA.
Defining the membrane proteome of NK cells.
Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities.
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding.
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LONP1 has an ATPase-dependent but protease-independent role in maintaining mitochondrial chaperone solubility.
"LONP1 is required for DNAJA3 and mtHSP70 solubility, and its ATPase, but not its protease activity, is required for this function."
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LONP1 directly cooperates with mtHSP70 to stabilize an OXA1L folding intermediate.
"In vitro, LONP1 shows an intrinsic chaperone-like activity and collaborates with mtHSP70 to stabilize a folding intermediate of OXA1L."
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
A mitochondrial iron-responsive pathway regulated by DELE1.
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Basal DELE1 degradation is predominantly LONP1-dependent in the mitochondrial matrix.
"LONP1 siRNAs increased DELE1 at steady state, and almost completely prevented DELE1 degradation during the CHX-chase (Figure 1E)."
Multimodal cell maps as a foundation for structural and functional genomics.
A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.
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Recombinant truncated human LONP1 degrades alpha-casein in an ATP-dependent reaction.
"A truncated LON gene, in which translation was initiated at Met118 of the coding sequence, was expressed in Escherichia coli and produced a protease that degraded alpha-casein in vitro in an ATP-dependent manner and had other properties similar to E. coli Lon protease."
The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner.
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Human LONP1 positively binds TG-rich single-stranded mitochondrial promoter elements.
"human LON specifically binds to the TG-rich element only when it is presented in the context of a single DNA strand."
Synthesis, processing, and localization of human Lon protease.
Cleavage site selection within a folded substrate by the ATP-dependent lon protease.
Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors.
Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease.
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DNA-free TFAM, including phosphorylated TFAM released from DNA, is degraded by LONP1.
"We show that only DNA-free TFAM is degraded by the Lon protease, which is inhibited by the anticancer drug bortezomib."
The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.
Defective mitochondrial protease LonP1 can cause classical mitochondrial disease.
Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
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Human cryo-EM structures reveal nucleotide- and substrate-coupled conformations for unfolding and translocation into the proteolytic chamber.
"We show that, like bacterial Lon, human LONP1 adopts both an open and closed spiral staircase orientation dictated by the presence of substrate and nucleotide."
Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix.
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LONP1 has a protease-independent ATPase chaperone activity and a protease-dependent role in clearing aberrant imported proteins.
"The ATP hydrolysis activity, but not protease activity, of LONP1 is critical for its chaperone-like anti-aggregation activity."
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Human LONP1 forms a homohexameric ring-shaped assembly.
"Human ATP-dependent Lon protease (LONP1) forms homohexameric, ring-shaped complexes."
Catalytic cycling of human mitochondrial Lon protease.
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Sequential ATP hydrolysis drives substrate translocation by human LONP1.
"Our data indicate how sequential ATP hydrolysis controls substrate protein translocation in a 6-fold binding change mechanism."
UniProt record for human LONP1 (P36776)
LONP1 binds mitochondrial inner membrane proteins
Mitochondrial protein degradation
LONP1 degrades mitochondrial inner membrane proteins
LONP1 degrades mitochondrial matrix proteins
LONP1 binds mitochondrial matrix proteins
ATF5 activates expression of LONP1