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Literature summary for 3.6.4.7 extracted from
- Peroxisomal proteostasis involves a Lon family protein that functions as protease and chaperone (2012), J. Biol. Chem., 287, 27380-27395.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene Lonp2, DNA and amino acid sequence determination and analysis, genetic structure | Rattus norvegicus |
| gene pln, recombinant expression of GFP-tagged enzyme in GFP-SKL protoplasts, recombinant expression of Pln protein fused to maltose-binding protein (MBP) at the N-terminus and a His6-tag at the C-terminus, with a tobacco etch virus (TEV) cleavage site between MBP and Pln, in Escherichia coli strain Rosetta 2 | Penicillium chrysogenum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S815A | site-directed mutagensis, a single amino acid substitution in the conserved catalytic dyad leads to a proteolytically inactive variant Plnin | Penicillium chrysogenum |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| additional information | immunohistochemic subcellular localization study | Rattus norvegicus | - |
- |
| peroxisome | - |
Penicillium chrysogenum | 5777 | - |
| peroxisome | peroxisome-specific isoform of Lon protease, peroxisomal proteome analysis | Rattus norvegicus | 5777 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 147000 | - |
7 * 147000, small-angle X-ray scattering, SAXS, analysis | Penicillium chrysogenum |
| 1100000 | - |
small-angle X-ray scattering, SAXS, analysis | Penicillium chrysogenum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Rattus norvegicus | identification of a peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity | ? | - |
? |  |
| additional information | Penicillium chrysogenum | Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease | ? | - |
? | |
| additional information | Penicillium chrysogenum DS54465 | Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Penicillium chrysogenum | - |
gene pln | - |
| Penicillium chrysogenum DS54465 | - |
gene pln | - |
| Rattus norvegicus | Q3MIB4 | Lon protease homolog 2, peroxisomal; gene Lonp2 | - |
Oxidation Stability
| Oxidation Stability | Organism |
|---|---|
| enzyme Pln enzyme is sensitive to oxidative damage | Penicillium chrysogenum |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| partially, peroxisomes isolated from rat liver by usual cell fractionation are further purified by immunoisolation using a specific antibody raised against a peroxisomal membrane protein, PMP70 | Rattus norvegicus |
| recombinant MBP-fusion enzyme from Escherichia coli strain Rosetta 2 to homogeneity | Penicillium chrysogenum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Rattus norvegicus | - |
| mycelium | - |
Penicillium chrysogenum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-casein + H2O | ATP-driven proteolytic activity against unfolded model protein | Penicillium chrysogenum | ? | - |
? | |
| alpha-casein + H2O | ATP-driven proteolytic activity against unfolded model protein | Penicillium chrysogenum DS54465 | ? | - |
? | |
| beta-casein + H2O | ATP-driven proteolytic activity against unfolded model protein | Penicillium chrysogenum | ? | - |
? | |
| beta-casein + H2O | ATP-driven proteolytic activity against unfolded model protein | Penicillium chrysogenum DS54465 | ? | - |
? | |
| additional information | identification of a peroxisome-specific isoform of Lon protease, an ATP-dependent protease with chaperone-like activity | Rattus norvegicus | ? | - |
? | |
| additional information | Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease | Penicillium chrysogenum | ? | - |
? | |
| additional information | Pln has chaperone activity in vitro | Penicillium chrysogenum | ? | - |
? | |
| additional information | Pln is a bifunctional protein with chaperone and protease activities, it acts as an ATP-fueled protease and chaperone. Oxidatively damaged, but not the native protein, is a substrate of the Pln protease | Penicillium chrysogenum DS54465 | ? | - |
? | |
| additional information | Pln has chaperone activity in vitro | Penicillium chrysogenum DS54465 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heptamer | 7 * 147000, small-angle X-ray scattering, SAXS, analysis | Penicillium chrysogenum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP-dependent lon protease | - |
Penicillium chrysogenum |
| lon protease | - |
Penicillium chrysogenum |
| lon protease | - |
Rattus norvegicus |
| Pln | - |
Penicillium chrysogenum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Penicillium chrysogenum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Penicillium chrysogenum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Penicillium chrysogenum | |
| ATP | - |
Rattus norvegicus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | in cells of a PLN deletion strain, peroxisomes contain protein aggregates, a major component of which is catalase-peroxidase. Cells of the pln mutant strain contain enhanced levels of catalase-peroxidase protein but reduced catalase-peroxidase enzyme activities. And the absence of Pln results in the formation of protein aggregates in the peroxisomal matrix | Penicillium chrysogenum |
| metabolism | the enzyme is involved in the peroxisome quality control system | Penicillium chrysogenum |
| additional information | molecular structure modeling | Penicillium chrysogenum |
| physiological function | Pln is an ATP-dependent protease that digests unfolded substrates e.g. oxidatively damaged catalase-peroxidase, and displays chaperone-like activity, circumventing accumulation of protein aggregates in peroxisomes that compromise organelle function. Peroxisomal proteostasis involves the Lon family protein that functions as protease and chaperone, Pln is crucial for peroxisome proteostasis | Penicillium chrysogenum |
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