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Literature summary for 3.6.4.7 extracted from

  • Aksam, E.B.; Koek, A.; Kiel, J.A.; Jourdan, S.; Veenhuis, M.; van der Klei, I.J.
    A peroxisomal Lon protease and peroxisome degradation by autophagy play key roles in vitality of Hansenula polymorpha cells (2007), Autophagy, 3, 96-105.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene Lon1, phylogenetic tree Zea mays
gene Lonp2, phylogenetic tree Mus musculus
gene NCU08303, phylogenetic tree Neurospora crassa
gene PLN, phylogenetic tree, recombinant expression of HpPln, a GFP-PLN hybrid gene under control of the PLN promoter, constructed for the subcellular localization study, coexpression of te peroxisomal marker GFP-SKL in Hansenula polymorpha Ogataea angusta
gene YALI0F23595g, phylogenetic tree Yarrowia lipolytica

Protein Variants

Protein Variants Comment Organism
additional information construction of the various disrup­tion strains of the Hansenula polymorpha PLN gene, the pln deletion cells grow normally like wild-type cells on methanol at 37°C. Growth is also unaffected at elevated growth temperatures (45°C) or upon heat shock Ogataea angusta

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
Mus musculus 5777
-
peroxisome
-
Zea mays 5777
-
peroxisome
-
Yarrowia lipolytica 5777
-
peroxisome
-
Neurospora crassa 5777
-
peroxisome HpPln is localized in peroxisomes in Hansenula polymorpha, subcellular localization study Ogataea angusta 5777
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
104900
-
about, sequence calculation Ogataea angusta

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Ogataea angusta the enzyme degrades soluble unfolded and non-assembled peroxi­somal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein ?
-
?
additional information Ogataea angusta NCYC495 the enzyme degrades soluble unfolded and non-assembled peroxi­somal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein ?
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9DBN5 Lon protease homolog 2, peroxisomal
-
Neurospora crassa Q7SA85 Lon protease homolog 2, peroxisomal; gene NCU08303
-
Ogataea angusta Q2V573 PLN, Lon protease homolog 2, peroxisomal; i.e. Pichia angusta
-
Ogataea angusta NCYC495 Q2V573 PLN, Lon protease homolog 2, peroxisomal; i.e. Pichia angusta
-
Yarrowia lipolytica Q6C0L7 Lon protease homolog 2, peroxisomal; i.e. Candida lipolytica, gene YALI0F23595g
-
Zea mays P93647 Lon protease homolog 2, peroxisomal
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme degrades soluble unfolded and non-assembled peroxi­somal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein Ogataea angusta ?
-
?
additional information the enzyme degrades soluble unfolded and non-assembled peroxi­somal proteins, e.g. of a mutant form of dihydrofolate reductase (DHFR) that contains three amino acid substitutions that destabilize the structure of the protein Ogataea angusta NCYC495 ?
-
?

Subunits

Subunits Comment Organism
More the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789) Ogataea angusta

Synonyms

Synonyms Comment Organism
HpPln
-
Ogataea angusta
LONP2
-
Mus musculus
LONP2
-
Zea mays
LONP2
-
Yarrowia lipolytica
LONP2
-
Neurospora crassa
Mm-p
-
Mus musculus
Nc-p
-
Neurospora crassa
peroxisomal Lon protease
-
Ogataea angusta
peroxisomal Lon protease
-
Mus musculus
peroxisomal Lon protease
-
Zea mays
peroxisomal Lon protease
-
Yarrowia lipolytica
peroxisomal Lon protease
-
Neurospora crassa
Pln
-
Ogataea angusta
Yl-p
-
Yarrowia lipolytica
Zm-p
-
Zea mays

Expression

Organism Comment Expression
Ogataea angusta the expression of PLN is not significantly enhanced in glucose-grown cells upon heat shock as reported for the mitochondrial Lon protease, PIM1, of Saccharomyces cerevisiae additional information

General Information

General Information Comment Organism
evolution Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases Mus musculus
evolution Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases Zea mays
evolution Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases Yarrowia lipolytica
evolution Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases Neurospora crassa
evolution Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases. Peroxismal Lon protease from Hansenula polymorpha shows 39% sequence identity with the putative peroxisomal Lon protease of Mus musculus Ogataea angusta
malfunction the absence of enzyme HpPln affects the viability of cells blocked in pexophagy, but does not affect cell growth. The number of peroxisomes is enhanced in enzyme deletion mutant cells Ogataea angusta
additional information the enzyme contains an AAA-domain (aa 447-586) and a proteolytic domain (aa 665-857), which harbors the conserved active site serine residue (aa 789). The ATPase domain in Lon proteases is required for ATP?dependent unfolding of the target protein, prior to degradation by the protease domain Ogataea angusta
physiological function most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality Mus musculus
physiological function most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality Zea mays
physiological function most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality Yarrowia lipolytica
physiological function most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality Neurospora crassa
physiological function most peroxisomal proteins are folded and assembled prior to import. The peroxisomal Lon protease, Pln, plays a role in degradation of unfolded and non-assembled peroxisomal matrix proteins. Whole peroxisomes are constitutively degraded by autophagy during normal vegetative growth of wild-type cells. The peroxisomal Lon protease and degradation of peroxisomes by autophagy are important for cell vitality, although the enzyme is not important for the viability Ogataea angusta