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evolution
Arabidopsis contains four Lon protease-like proteins (AtLon1-AtLon4), predicted to be localized in different cellular organelles, including mitochondria, peroxisomes and plastids. AtLon2 is clustered in group II together with several Lon orthologues, which lack putative organelle N-terminal pre-sequences but contain the peroxisomal C-terminal localization signal, suggesting that plant orthologues within this group are localized to the peroxisomes
evolution
enzymes Pex1 and Pex6 are type-2 AAA+ ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
evolution
Lon is a highly conserved ATP-stimulated protease, which belongs to the family of AAA-ATPases
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
evolution
Pex1 and Pex6 are members of the AAA family of ATPases
evolution
Pex1p and Pex6p belong to the group of type-II AAA proteins characterized by the presence of two AAA-domains, termed D1 and D2, post-positioned to an N-terminal domain
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase
evolution
the enzyme belongs to the a member of the Lon-family of proteases in the AAA+ ATPase superfamily, type I AAA+ ATPase. Based on the domain composition and sequence characteristic of the domains, the Lon-proteases are subdivided into two classes, LonA and LonB. The LonA subfamily are soluble enzymes,which function in the bacterial cytosol and the mitochondrial matrix, whereas LonB predominates in Archaea
evolution
the enzyme belongs to the AAA+ ATPase family. AAA-proteins belong to the class of P-loop NTPases defined by conserved motifs for NTP-binding (Walker A motif) and hydrolysis (Walker B motif) which are assisted by Mg2+ as cofactor. Pex1p and Pex6p are evolutionary related to Cdc48p/p97
evolution
the enzyme belongs to the AAA+ ATPase superfamily
evolution
the enzyme belongs to the AAA+ ATPase superfamily
evolution
the enzyme belongs to the AAA+ ATPase superfamily
evolution
the enzyme belongs to the type II AAA+ ATPases, which by definition contain two conserved nucleotide-binding domains (D1 and D2) in tandem flanked by less conserved N- and C-terminal regions
evolution
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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
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malfunction
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in fibroblasts from patients defective in Pex1, Pex6 and Pex26, (all of which are required for Pex5 export) Pex5 stability is decreased
malfunction
a deletion of peroxisomal Lon results in a specific growth defect on media containing oleic acid as a sole carbon source, conditions which require peroxisomal enzymes of the beta-oxidation pathway, the growth defect is accompanied by the formation of protein aggregates in the peroxisomal matrix
malfunction
a Lon protease deletion strain does not display a growth defect but a decreased viability of the cells
malfunction
a mutation of the conserved Walker A lysine in the D1 domain of Pex1, but not Pex6, dramatically affects the recovery of fully assembled recombinant hexamer
malfunction
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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
malfunction
Lon2 absence leads to accumulation of enzymes in peroxisomes and results in an accelerated peroxisome degradation by pexophagy
malfunction
mutation of the Walker B motif in one D2 domain leads to ATP hydrolysis in the neighbouring domain
malfunction
mutations in the PEX1 gene, which encodes a protein required for peroxisome biogenesis, are themost common cause of the Zellweger spectrum diseases, the by far most abundant Pex1pG843D variation impairs the binding between Pex1p and Pex6p
malfunction
mutations in the proteins frequently cause peroxisomal diseases
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
malfunction
the Arabidopsis apem10 mutant displays accelerated peroxisome degradation and a dramatically reduces number of peroxisomes. LON2 deficiency causes enhanced peroxisome degradation by autophagy, and peroxisomal proteins accumulates in the cytosol due to a decrease in the number of peroxisomes. The loss of function of LON2 leads to accelerated autophagy, accumulation of electron-dense inclusions in the peroxisome matrix and a delay in the elimination of glyoxysomal enzymes during post-germinative growth. apem10 phenotype, overview
malfunction
the PEX6-deletion strain has the most pronounced survival defects of all strains affected in peroxisome function
malfunction
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enzyme complex absence results in the selective degradation of the peroxisome. Loss of the enzyme complex does not prevent matrix protein import, but instead causes an upregulation of peroxisome degradation by macroautophagy, or pexophagy. The loss of enzyme complex function in cells results in the accumulation of ubiquitinated PEX5 on the peroxisomal membrane that signals pexophagy
malfunction
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mutations in Pex1 and Pex6 cause more than 80% of peroxisome biogenesis disorder cases, including Zellweger syndrome
malfunction
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mutations in Pex1 and Pex6 cause peroxisome biogenesis disorders
malfunction
Q9FNP1; Q8RY16
PEX6 mutants show growth defects, impaired matrix protein processing and decreased PEX5 levels
malfunction
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the receptor Pex5p is released from the membrane back to the cytosol in an ATP-dependent manner by the AAA-type ATPases Pex1p and Pex6p
malfunction
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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
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malfunction
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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
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metabolism
the enzyme is involved in LON2- and autophagy-dependent degradation pathways during the functional transition of peroxisomes, two hypothetical mechanisms proposed for the functional transition of glyoxysomes to leaf peroxisomes, modeling
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis
metabolism
the enzyme is involved in peroxisome biogenesis, proteins that play a role in peroxisome biogenesis are collectively called peroxins. Function of Pex1p and Pex6p in peroxisomal matrix protein import, overview
metabolism
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the enzyme is involved in the peroxisome quality control system
metabolism
turnover of peroxisomal enzymes may be regulated by a peroxisomal homologue of the mitochondrial Lon protease
metabolism
Q9FNP1; Q8RY16
a complex of the PEX1 and PEX6 ATPases and the PEX26 tail-anchored membrane protein removes ubiquitinated PEX5 from the peroxisomal membrane
metabolism
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Pex5p recognition by the peroxisomal AAA complex depends on the presence of the ubiquitin moiety and is mediated by enzyme Pex1p
metabolism
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the ATPases Pex1p and Pex6p form a heterohexameric complex, which is recruited to the peroxisomal import machinery by the membrane anchor protein Pex15p. The Pex1p/Pex6p complex recognizes the ubiquitinated import receptors, pulls them out of the membrane and releases them into the cytosol
metabolism
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the peroxisomal enzyme-complex is required to remove the ubiquitinated form of the shuttling peroxisomal matrix protein receptor, PEX5, from the peroxisomal membrane
metabolism
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the two AAA-ATPases Pex1p and Pex6p are required for biogenesis of peroxisomes. At the peroxisomal membrane, the enzyme complex is responsible for the release of the import receptor Pex5p at the end of the matrix protein import cycle
metabolism
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the enzyme is involved in the peroxisome quality control system
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physiological function
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results identify AWP1 as a novel cofactor of Pex6 involved in the regulation of Pex5 export during peroxisome biogenesis
physiological function
ATP hydrolysis at both Pex1p/Pex6p complex sites is needed for cell viability
physiological function
LON2 is involved in the peroxisomal functional transition and basal quality control of peroxisomes. Chaperone and protease functions of LON protease 2 modulate the peroxisomal transition and degradation with autophagy. Proteolytic consequence of LON2 for the degradation of peroxisomal proteins, unnecessary proteins are eliminated by LON2- and autophagy-dependent degradation pathways during the functional transition of peroxisomes. LON2 plays dual roles as an ATP-dependent protease and a chaperone. The chaperone domain of LON2 is essential for the suppression of autophagy, whereas its peptidase domain interferes with this chaperone function, indicating that intramolecular modulation between the proteolysis and chaperone functions of LON2 regulates degradation of peroxisomes by autophagy
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
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
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
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
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
physiological function
Pex1 and Pex6 are required for the de novo biogenesis of peroxisomes. The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. The recombinant Pex1-FLAG/His-Pex6 complex is an active ATPase
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex1p in peroxisomal matrix protein import, overview
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex1p/Pex6p in peroxisomal matrix protein import, overview
physiological function
Pex1p and Pex6p are crucial for peroxisome biogenesis, Pex6p functions together with Pex1p in peroxisome biogenesis. The ATP hydrolysis cycle of the AAA+-ATPases is supposed to regulate the assembly and disassembly of the Pex1p-Pex6p complex and its membrane association and release. Role of Pex6p in peroxisomal matrix protein import, overview
physiological function
Pex6p functions together with Pex1p in peroxisome biogenesis
physiological function
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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
physiological function
the enzyme is essentially involved in peroxisome biogenesis, Pex1p provides the energy for import of peroxisomal matrix proteins. Peroxisomal matrix proteins are synthesized on free ribosomes in the cytosol and guided to the peroxisomal membrane by specific soluble receptors. At the membrane, the cargo-loaded receptors bind to a docking complex and the receptor-docking complex assembly is thought to form a dynamic pore which enables the transition of the cargo into the organellar lumen. The import cycle is completed by ubiquitination- and ATP-dependent dislocation of the receptor from the membrane to the cytosol, which is performed by the AAA-peroxins. Receptor ubiquitination and dislocation are the only energy-dependent steps in peroxisomal protein import. The export-driven import model suggests that the AAA-peroxins might function as motor proteins in peroxisomal import by coupling ATP-dependent removal of the peroxisomal import receptor and cargo translocation into the organelle
physiological function
the enzyme is essentially involved in peroxisome biogenesis, Pex6p provides the energy for import of peroxisomal matrix proteins. Peroxisomal matrix proteins are synthesized on free ribosomes in the cytosol and guided to the peroxisomal membrane by specific soluble receptors. At the membrane, the cargo-loaded receptors bind to a docking complex and the receptor-docking complex assembly is thought to form a dynamic pore which enables the transition of the cargo into the organellar lumen. The import cycle is completed by ubiquitination- and ATP-dependent dislocation of the receptor from the membrane to the cytosol, which is performed by the AAA-peroxins. Receptor ubiquitination and dislocation are the only energy-dependent steps in peroxisomal protein import. The export-driven import model suggests that the AAA-peroxins might function as motor proteins in peroxisomal import by coupling ATP-dependent removal of the peroxisomal import receptor and cargo translocation into the organelle. Pex6p might also have additional functions that appear not to be related to peroxisomes, yeast Pex6p acts as a suppressor for aging defects in mitochondria. Overexpression of Pex6p, but not of Pex1p, restores the import defect of mutant ATP2, the gene encoding the beta-subunit of mitochondrial F1,F0-ATPase, into mitochondria. Function for Pex6p in the prevention of necrotic cell death in yeast
physiological function
the enzyme is involved in peroxisome biogenesis abd associated with peroxisomal quality control. The Lon protease functions in the degradation of mutated or abnormal proteins as well as short-lived regulatory proteins, in particular those produced under stress conditions
physiological function
the enzyme is involved in peroxisome biogenesis and associated with peroxisomal quality control
physiological function
the enzyme is involved in peroxisome biogenesis and associated with peroxisomal quality control. Lon2 is required for the elimination of unnecessary proteins during the functional transition of glyoxysomes to peroxisomes
physiological function
the enzyme is involved in peroxisome biogenesis and associated with peroxisomal quality control. The peroxisomal Lon and autophagy function together in peroxisomal quality control
physiological function
the peroxisomal matrix protein import is facilitated by soluble receptor molecules which cycle between cytosol and the peroxisomal membrane. At the end of the receptor cycle, the import receptors are exported back to the cytosol in an ATP-dependent manner catalyzed by a complex of Pex1p and Pex6p
physiological function
the peroxisomal proteins Pex1 and Pex6 complex fuels essential protein transport across peroxisomal membranes. ATP hydrolysis results in a pumping motion of the complex, suggesting that Pex1/6 function involves substrate translocation through its central channel. ATPase activity of Pex6 D2 domains drive conformational changes, Pex1/6 movements during ATP binding and hydrolysis, overview
physiological function
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the enzyme complex Pex1/Pex6 plays a role in mechanical unfolding of peroxins or their extraction from the peroxisomal membrane during matrix-protein import
physiological function
Q9FNP1; Q8RY16
the enzyme complex plays a role in the import and export of peroxisomal proteins and in oil body utilization
physiological function
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the enzyme plays a role in many processes, including endoplasmic reticulum-associated protein degradation
physiological function
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the peroxisomal enzyme-complex is required for peroxisome quality control
physiological function
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the Pex1/Pex6 complex dislocates and recycles the transport receptor Pex5 from the peroxisomal membrane during peroxisomal protein import
physiological function
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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
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physiological function
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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
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additional information
enzyme Pex1p/Pex6p complex structure modeling using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 assemble into hexameric double rings and perform vital functions, structure-function relationship, molecular models. Comparison of the structures of the Pex1/Pex6 complex determined in presence of ATPgammaS and ADP
additional information
enzyme Pex1p/Pex6p complex structure modeling using a computational approach that combines Monte Carlo placement of structurally homologous domains into density maps with energy minimization and refinement protocols. Pex1 and Pex6 assemble into hexameric double rings and perform vital functions, structure-function relationship, molecular models. Comparison of the structures of the Pex1/Pex6 complex determined in presence of ATPgammaS and ADP
additional information
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molecular structure modeling
additional information
Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP
additional information
Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP
additional information
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Pex1p and Pex6p interact and form a heteromeric complex. Disassembly of the complex into its Pex1p and Pex6p subunits is observed upon ATP-depletion, indicating that formation of the Pex1p/Pex6p-complex requires the presence of ATP
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
structure-function analysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may provide the driving force for conformational changes triggered by the AAA-peroxins
additional information
structure-function analysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may provide the driving force for conformational changes triggered by the AAA-peroxins
additional information
structure-function analysis. The D1 of Pex6p does not contain a functional Walker B motif for ATP hydrolysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may providethe driving force for conformational changes triggered by the AAA-peroxins
additional information
structure-function analysis. The D1 of Pex6p does not contain a functional Walker B motif for ATP hydrolysis. AAA-peroxins defective in ATP-hydrolysis of D1 are at least partially functional. In contrast, ATP-hydrolysis of the conserved AAA-domains (D2) of both AAA-peroxins is essential for their function. The conserved D2-domains of Pex1p and Pex6p require hydrolysis of ATP for their function in peroxisome biogenesis, indicating that they may providethe driving force for conformational changes triggered by the AAA-peroxins
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
additional information
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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
additional information
the murine Pex1p N-terminal domain lacks hydrophobic amino acids. Structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
the murine Pex1p N-terminal domain lacks hydrophobic amino acids. Structural organization and localization of peroxisomal AAA+ ATPases, molecular organization of the Pex1p-Pex6p complex, modeling of the Pex1p-Pex6p mode of action, overview
additional information
within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6
additional information
within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6
additional information
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within the Pex1/Pex6 complex, only the D2 ATPase ring hydrolyzes ATP, while nucleotide binding in the D1 ring promotes complex assembly. ATP hydrolysis by Pex1 is highly coordinated with that of Pex6
additional information
yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview
additional information
yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview
additional information
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yeast Pex1/6 complex structure analysis, structural insights into inter-domain communication of these unique heterohexameric AAA+ assemblies. While the C-terminal nucleotide-binding domains (D2) of Pex6 constitute the main ATPase activity of the complex, both D2 harbour essential substrate-binding motifs. The Pex1/6 complex assembles in the presence of a nucleotide, ATP or ATPgammaS, structure modeling, overview
additional information
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molecular structure modeling
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additional information
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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
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