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Literature summary for 3.4.21.53 extracted from

  • Lee, I.; Suzuki, C.K.
    Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates (2008), Biochim. Biophys. Acta, 1784, 727-735.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information oligomerization is stimulated by unfolded protein Mycolicibacterium smegmatis
additional information protein substrate stimulates DNA binding Homo sapiens
Polyphosphate stimulates lon-mediated proteolysis of free ribosomal proteins and thereby down-regulates translation Escherichia coli

Application

Application Comment Organism
additional information functions in protein quality control Escherichia coli
additional information induction of lon contributes to the adaptive resistance of the organism towards antibiotic treatment Pseudomonas aeruginosa
additional information stress response network between the endoplasmic reticulum, nucleus and mitochondrion up-regulates the expression, thereby providing a cytoprotective function during endoplasmic reticulum stress and hypoxia Homo sapiens
additional information stress response network between the endoplasmic reticulum, nucleus and mitochondrion up-regulates the expression, thereby providing a cytoprotective function during endoplasmic reticulum stress and hypoxia Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E614K mixed oligomeric complexes composed of wild-type lon and the inactive lon E614K mutant, results in an enzymatically inactive protein Escherichia coli
additional information absence of lon, results in a lack of ATP-dependent proteolysis in the mitochondrial matrix, accumulation of electron dense aggregates and large mitochondrial DNA deletions. Mutant lacking both ATPase and protease activity also fails to suppress COX assembly defects Saccharomyces cerevisiae
additional information lon gene mutants, form long undivided filaments upon UV irradiation Escherichia coli
additional information lon-depleted cells show little if any mitochondrial DNA damage Homo sapiens
S679W proteolytically inactive mutant. ATPase activity is affected by a variety of mutations generated at the vicinity of the proteolytic site Ser 679. Mutation of the ATP-binding site abolishes both the ATPase and protease activities of lon Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
anti-sense morpholino oligonucleotide causes defects in mitochondrial membrane potential, respiration and morphology, as well as apoptotic cell death Homo sapiens
ATP ATP-binding inhibits DNA binding Homo sapiens
bacteriophage T4 PinA protein specifically inhibits Escherichia coli Lon Escherichia coli
MG262 i.e. Cb2-Leu-Leu-Leu-bornic acid Salmonella enterica subsp. enterica serovar Typhimurium
additional information expression of an inducible short hairpin RNA leading to lon depletion in a colon adenocarcinoma cell line for 14 days does not lead to cell death. Even after RNAi knockdown for 3 weeks, these cells continue to survive, although they no longer proliferate Homo sapiens
Polyphosphate competitively blocks DNA binding by lon in vitro and in vivo Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Escherichia coli 5829
-
mitochondrion
-
Homo sapiens 5739
-
mitochondrion
-
Rattus norvegicus 5739
-
mitochondrion
-
Saccharomyces cerevisiae 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ oligomerization is dependent on Mg2+ Escherichia coli
Mg2+ oligomerization is dependent on Mg2+ Mycolicibacterium smegmatis
additional information maintenance of the holoenzyme does not require the addition of Mg2+ Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Brucella abortus
-
-
-
Caulobacter vibrioides
-
-
-
Escherichia coli
-
-
-
Homo sapiens
-
-
-
Mycolicibacterium smegmatis
-
-
-
Pseudomonas aeruginosa
-
-
-
Rattus norvegicus
-
-
-
Saccharomyces cerevisiae
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-
Thermoplasma acidophilum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli
-
Saccharomyces cerevisiae
-
Mycolicibacterium smegmatis

Source Tissue

Source Tissue Comment Organism Textmining
colonic adenocarcinoma cell line
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bacteriophage lambda N protein + H2O
-
Escherichia coli ?
-
?
casein + H2O
-
Escherichia coli ?
-
?
CcdA + H2O
-
Escherichia coli ?
-
?
Cox4-1 + H2O
-
Homo sapiens ?
-
?
DNA methyltransferase + H2O selectively degrades cell-cycle-regulated DNA methyltransferase thereby regulating methylation of chromosomal DNA and cellular differentiation Caulobacter vibrioides ?
-
?
HilA + H2O mediates proteolysis of the central transcription regulatory factor HilA, which controls the correct timing for the expression of virulence genes necessary for host invasion Salmonella enterica subsp. enterica serovar Typhimurium ?
-
?
HilA + H2O mediates proteolysis of the central transcription regulatory factor HilA, which controls the correct timing for the expression of virulence genes necessary for host invasion Brucella abortus ?
-
?
mitochondrial processing peptidase alpha subunit + H2O is degraded only when it is folded, trypsin-resistant and competent for assembly into an active enzyme Homo sapiens ?
-
?
additional information endogenous substrates, which are misfolded or unassembled subunits of electron transport chain complexes, ribosomal proteins and metabolic enzymes Saccharomyces cerevisiae ?
-
?
Rcs + H2O
-
Escherichia coli ?
-
?

Subunits

Subunits Comment Organism
heptamer cryoelectron microscopy and analytic ultracentrifugation Saccharomyces cerevisiae
hexamer analytical ultracentrifugation Mycolicibacterium smegmatis
hexamer electron microscopy Escherichia coli

Synonyms

Synonyms Comment Organism
ATP-dependent lon protease
-
Salmonella enterica subsp. enterica serovar Typhimurium
ATP-dependent lon protease
-
Escherichia coli
ATP-dependent lon protease
-
Homo sapiens
ATP-dependent lon protease
-
Rattus norvegicus
ATP-dependent lon protease
-
Saccharomyces cerevisiae
ATP-dependent lon protease
-
Mycolicibacterium smegmatis
ATP-dependent lon protease
-
Pseudomonas aeruginosa
ATP-dependent lon protease
-
Thermoplasma acidophilum
ATP-dependent lon protease
-
Brucella abortus
ATP-dependent lon protease
-
Caulobacter vibrioides
lon
-
Salmonella enterica subsp. enterica serovar Typhimurium
lon
-
Escherichia coli
lon
-
Homo sapiens
lon
-
Rattus norvegicus
lon
-
Saccharomyces cerevisiae
lon
-
Mycolicibacterium smegmatis
lon
-
Pseudomonas aeruginosa
lon
-
Thermoplasma acidophilum
lon
-
Brucella abortus
lon
-
Caulobacter vibrioides
lon protease
-
Salmonella enterica subsp. enterica serovar Typhimurium
lon protease
-
Escherichia coli
lon protease
-
Homo sapiens
lon protease
-
Rattus norvegicus
lon protease
-
Saccharomyces cerevisiae
lon protease
-
Mycolicibacterium smegmatis
lon protease
-
Pseudomonas aeruginosa
lon protease
-
Thermoplasma acidophilum
lon protease
-
Brucella abortus
lon protease
-
Caulobacter vibrioides

Cofactor

Cofactor Comment Organism Structure
additional information maintenance of the holoenzyme does not require the addition of ATP. ATP binding induces conformational changes in the holoenzyme Saccharomyces cerevisiae
additional information oligomerization is independent of ATP Escherichia coli
additional information oligomerization is independent of ATP Mycolicibacterium smegmatis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0000066
-
MG262
-
Salmonella enterica subsp. enterica serovar Typhimurium