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Literature summary for 3.4.21.53 extracted from

  • Karlowicz, A.; Wegrzyn, K.; Gross, M.; Kaczynska, D.; Ropelewska, M.; Siemiatkowska, M.; Bujnicki, J.M.; Konieczny, I.
    Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates (2017), J. Biol. Chem., 292, 7507-7518 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
ATP activates the enzyme activity Escherichia coli
DNA activates the enzyme activity Escherichia coli
additional information the enzyme activity of Lon can be stimulated by the presence of unfolded proteins (e.g. apomyoglobin, glucagon, and alpha-casein) as well as inorganic polyphosphate accumulated during amino acid starvation Escherichia coli

Protein Variants

Protein Variants Comment Organism
K371E/K376E/R379E site-directed mutagenesis, mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous Escherichia coli
additional information generation of mutant LonDELTANP lacking the ATP domain. Deletion of Lon's ATPase domain abrogates interactions with DNA. The DNA-binding defect of Lon protease affects TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex Escherichia coli
R306E/K308E/K310E/K311E site-directed mutagenesis, the mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
alpha-casein + H2O Escherichia coli
-
 ?
-
 ?
TrfA + H2O Escherichia coli
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-casein + H2O
-
 Escherichia coli ?
-
 ?
TrfA + H2O
-
 Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
hexamer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
EcLon
-
 Escherichia coli
EcLon protease
-
 Escherichia coli
lon
-
 Escherichia coli
lon protease
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP required, protein degradation by Lon is dependent on energy obtained from ATP hydrolysis, modelng of the structure of hexameric ATPase domain of EcLon protease using the comparative modeling approach, overview Escherichia coli

General Information

General Information Comment Organism
malfunction deletion of Lon's ATPase domain abrogates interactions with DNA. Substitution of positively charged amino acids in this domain in full-length Lon with residues conferring a net negative charge disrupts binding of Lon to DNA. These changes also affect the degradation of nucleic acid binding protein substrates of Lon, intracellular localization of Lon, and cell morphology. The DNA-binding defect of Lon protease affects plasmid replication initiator protein TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex. The phenotype of the DNA binding-defective Lon mutants is similar to that observed for Lon-deficient strains Escherichia coli
physiological function Lon-DNA interactions are essential for Lon activity in cell division control. The ability of Lon to bind DNA is determined by its ATPase domain. This binding is required for processing protein substrates in nucleoprotein complexes, and Lon may help regulate DNA replication in response to growth conditions Escherichia coli