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Identification and molecular characterization of Parkin in Clonorchis sinensis.

Bai X, Kim TI, Lee JY, Dai F, Hong SJ - Korean J. Parasitol. (2015)

Bottom Line: CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae.Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells.From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

View Article: PubMed Central - PubMed

Affiliation: Department of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul 156-756, Korea.

ABSTRACT
Clonorchis sinensis habitating in the bile duct of mammals causes clonorchiasis endemic in East Asian countries. Parkin is a RING-between-RING protein and has E3-ubiquitin ligase activity catalyzing ubiquitination and degradation of substrate proteins. A cDNA clone of C. sinensis was predicted to encode a polypeptide homologous to parkin (CsParkin) including 5 domains (Ubl, RING0, RING1, IBR, and RING2). The cysteine and histidine residues binding to Zn(2+) were all conserved and participated in formation of tertiary structural RINGs. Conserved residues were also an E2-binding site in RING1 domain and a catalytic cysteine residue in the RING2 domain. Native CsParkin was determined to have an estimated molecular weight of 45.7 kDa from C. sinensis adults by immunoblotting. CsParkin revealed E3-ubiquitin ligase activity and higher expression in metacercariae than in adults. CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae. Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells. From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

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A phylogenetic tree of CsParkin with homolog of other animals. Number at each node denotes bootstrap value (in percentage) generated using by Neighbor-Joining method (1,000 replicates). Parkin is labeled each with its species name. A phylogenetic tree was drawn with 24 parkin homologs of vertebrate and invertebrate animals retrieved from GenBank using MEGA5.0.
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f3-kjp-53-1-65: A phylogenetic tree of CsParkin with homolog of other animals. Number at each node denotes bootstrap value (in percentage) generated using by Neighbor-Joining method (1,000 replicates). Parkin is labeled each with its species name. A phylogenetic tree was drawn with 24 parkin homologs of vertebrate and invertebrate animals retrieved from GenBank using MEGA5.0.

Mentions: A predicted tertiary structure of CsParkin showed a very similar conformation to the crystal structure of the parkin of human and rat [26,31]. IBR was conformationally adjacent to RING1, while RING0 was adjacent to RING2. The E2-binding site in RING1 was occupied by REP near the Ubl binding site (Fig. 2). A phylogenetic tree showed CsParkin grouped with a homolog of blood fluke, Schistosoma mansoni. Parkin has not been reported from other trematodes and Platyhelminthes yet. Parkins of the mammalian animals formed a branch appearing as a major clade, followed by clades of fish and the insects (Fig. 3).


Identification and molecular characterization of Parkin in Clonorchis sinensis.

Bai X, Kim TI, Lee JY, Dai F, Hong SJ - Korean J. Parasitol. (2015)

A phylogenetic tree of CsParkin with homolog of other animals. Number at each node denotes bootstrap value (in percentage) generated using by Neighbor-Joining method (1,000 replicates). Parkin is labeled each with its species name. A phylogenetic tree was drawn with 24 parkin homologs of vertebrate and invertebrate animals retrieved from GenBank using MEGA5.0.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4384794&req=5

f3-kjp-53-1-65: A phylogenetic tree of CsParkin with homolog of other animals. Number at each node denotes bootstrap value (in percentage) generated using by Neighbor-Joining method (1,000 replicates). Parkin is labeled each with its species name. A phylogenetic tree was drawn with 24 parkin homologs of vertebrate and invertebrate animals retrieved from GenBank using MEGA5.0.
Mentions: A predicted tertiary structure of CsParkin showed a very similar conformation to the crystal structure of the parkin of human and rat [26,31]. IBR was conformationally adjacent to RING1, while RING0 was adjacent to RING2. The E2-binding site in RING1 was occupied by REP near the Ubl binding site (Fig. 2). A phylogenetic tree showed CsParkin grouped with a homolog of blood fluke, Schistosoma mansoni. Parkin has not been reported from other trematodes and Platyhelminthes yet. Parkins of the mammalian animals formed a branch appearing as a major clade, followed by clades of fish and the insects (Fig. 3).

Bottom Line: CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae.Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells.From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

View Article: PubMed Central - PubMed

Affiliation: Department of Medical Environmental Biology, Chung-Ang University College of Medicine, Seoul 156-756, Korea.

ABSTRACT
Clonorchis sinensis habitating in the bile duct of mammals causes clonorchiasis endemic in East Asian countries. Parkin is a RING-between-RING protein and has E3-ubiquitin ligase activity catalyzing ubiquitination and degradation of substrate proteins. A cDNA clone of C. sinensis was predicted to encode a polypeptide homologous to parkin (CsParkin) including 5 domains (Ubl, RING0, RING1, IBR, and RING2). The cysteine and histidine residues binding to Zn(2+) were all conserved and participated in formation of tertiary structural RINGs. Conserved residues were also an E2-binding site in RING1 domain and a catalytic cysteine residue in the RING2 domain. Native CsParkin was determined to have an estimated molecular weight of 45.7 kDa from C. sinensis adults by immunoblotting. CsParkin revealed E3-ubiquitin ligase activity and higher expression in metacercariae than in adults. CsParkin was localized in the locomotive and male reproductive organs of C. sinensis adults, and extensively in metacercariae. Parkin has been found to participate in regulating mitochondrial function and energy metabolism in mammalian cells. From these results, it is suggested that CsParkin play roles in energy metabolism of the locomotive organs, and possibly in protein metabolism of the reproductive organs of C. sinensis.

Show MeSH
Related in: MedlinePlus