Characterization of Echinostoma cinetorchis endoribonuclease, RNase H.
10.3347/kjp.2017.55.4.451
- Author:
Sung Bin LIM
1
;
Seok Ho CHA
;
Seung JEGAL
;
Hojong JUN
;
Seo Hye PARK
;
Bo Young JEON
;
Jhang Ho PAK
;
Young Yil BAKH
;
Tong Soo KIM
;
Hyeong Woo LEE
Author Information
1. Department of Tropical Medicine and Parasitology, Inha University School of Medicine, Incheon 22212, Korea. tongsookim@inha.ac.kr
- Publication Type:Brief Communication
- Keywords:
Echinostoma cinetorchis;
endoribonuclease;
recombinant protein;
localization;
RNase H
- MeSH:
Amino Acids;
Catalytic Domain;
DNA, Complementary;
Echinostoma*;
Endoribonucleases;
Escherichia coli;
Intestine, Small;
Oligonucleotides, Antisense;
Parasites;
Ribonuclease H*;
Ribonucleases*;
RNA;
Trematoda
- From:The Korean Journal of Parasitology
2017;55(4):451-455
- CountryRepublic of Korea
- Language:English
-
Abstract:
Echinostoma cinetorchis is an oriental intestinal fluke causing significant pathological damage to the small intestine. The aim of this study was to determine a full-length cDNA sequence of E. cinetorchis endoribonuclease (RNase H; EcRNH) and to elucidate its molecular biological characters. EcRNH consisted of 308 amino acids and showed low similarity to endoribonucleases of other parasites (<40%). EcRNH had an active site centered on a putative DDEED motif instead of DEDD conserved in other species. A recombinant EcRNH produced as a soluble form in Escherichia coli showed enzymatic activity to cleave the 3′-O-P bond of RNA in a DNA-RNA duplex, producing 3′-hydroxyl and 5′-phosphate. These findings may contribute to develop antisense oligonucleotides which could damage echinostomes and other flukes.
