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Literature summary for 3.4.21.53 extracted from

  • Wohlever, M.L.; Baker, T.A.; Sauer, R.T.
    Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity (2014), Mol. Microbiol., 91, 66-78.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.53

Activating Compound

Activating Compound Comment Organism Structure
degron degron binding to this site is not required for proteolysis of sul20-tagged substrates in vitro but enhances degradation by allosterically activating protease activity. Sul20 degron from the cell-division inhibitor SulA binds to the N domain of the enzyme, determination of the recognition site, overview. Allosteric role for the sul20-binding site in the N domain Escherichia coli

Protein Variants

Protein Variants Comment Organism
E424Q site-directed mutagenesis, the mutant is unable to inactivate SulA in vivo and displays reduced rates of both basal and substrate-stimulated ATP hydrolysis. The mutant translocates and degrades CM-titinI27-sul20 and CM-titinI27-beta20 at a very slow rate. The mutation stabilizes the enzyme conformation that is active in relieving stress Escherichia coli
E424Q/S679A site-directed mutagenesis, the mutant is unable to inactivate SulA in vivo and displays reduced rates of both basal and substrate-stimulated ATP hydrolysis Escherichia coli
additional information construction of enzyme mutants, fusion of the Lon N domain to Escherichia coli ClpXDELTAN, a AAA+ enzyme that forms stable ring hexamers. Chimera307 contained the entire Lon N domain (residues 1-307) fused to ClpXDELTAN, whereas chimera211 contains the first 211 residues of Lon, which includes a globular region of the N domain but not an extended helical region. In addition, chimera211 contains disulfide bonds between the subunits of ClpXDELTAN, which have been shown to stabilize functional covalent hexamers. The ClpXDELTAN hexamerization is required for functional interaction with ClpP Escherichia coli
S679A site-directed mutagenesis, the S679A mutation destabilizes the enzyme conformation that is active in relieving stress Escherichia coli
Y398A site-directed mutagenesis, the mutant has basal ATP-hydrolysis activity similar to wild-type Lon, but displays substantially reduced rates of ATP hydrolysis in the presence of sul20- or beta20-tagged substrates Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
SulA + H2O Escherichia coli inactivation of SulA through the enzyme in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
SulA + H2O inactivation of SulA through the enzyme in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
AAA+ Lon protease
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 Escherichia coli
AAA+ protease
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 Escherichia coli
lon
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 Escherichia coli
lon protease
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 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP dependent on Escherichia coli

General Information

General Information Comment Organism
additional information the AAA+ ATPase module and protease domain of Lon are part of a single polypeptide Escherichia coli
physiological function the enzyme can function as a protease or a chaperone and reveal that some of its ATP-dependent biological activities do not require translocation. Enzyme-mediated relief of proteotoxic stress and protein aggregation in vivo can also occur without degradation but is not dependent on robust ATP hydrolysis. Degron binding regulates the activities of the AAA+ Lon protease in addition to targeting proteins for degradation, degron binding regulates Lon ATPase and protease activity in addition to serving a recognition function. Inactivation of cell-division inhibitor SulA in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber Escherichia coli