Back to Search
Start Over
Identification and Molecular Characterization of Parkin in Clonorchis sinensis
- Source :
- The Korean Journal of Parasitology
- Publication Year :
- 2015
- Publisher :
- The Korean Society for Parasitology and Tropical Medicine, 2015.
-
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.
- Subjects :
- Models, Molecular
Clonorchis sinensis
DNA, Complementary
Sequence Homology, Amino Acid
Protein Conformation
Gene Expression Profiling
Ubiquitin-Protein Ligases
ubiquitin ligase
platyhelminth
Mitochondria
mtabolism
Molecular Weight
Animals
Cluster Analysis
Original Article
parkin
Amino Acid Sequence
Energy Metabolism
Conserved Sequence
Phylogeny
Subjects
Details
- Language :
- English
- ISSN :
- 17380006 and 00234001
- Volume :
- 53
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- The Korean Journal of Parasitology
- Accession number :
- edsair.pmid..........08646257f3c38858f9d9ddf7adc9b76d