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Molecular cloning and characterization of omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea: Biochemical comparison with theta class glutathione S-transferase (GST-T)

Title
Molecular cloning and characterization of omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea: Biochemical comparison with theta class glutathione S-transferase (GST-T)
Author
신경훈
Keywords
polychaete; Neanthes succinea; glutathione S-transferases; antioxidant defense; biomarker
Issue Date
2007-11
Publisher
ELSEVIER SCIENCE INC
Citation
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY, v. 146, No. 4, Page. 471-477
Abstract
We cloned and sequenced a full-length cDNA of an omega class glutathione S-transferase (GST-O) from the polychaete Neanthes succinea (ns-GST-O). The full-length cDNA of ns-GST-O was 1562 bp in length, containing an open reading frame (OR) of 732 bp that encoded a 244 amino acid protein. The deduced amino acid sequence of ns-GST-O showed a low similarity with the theta class N. suucinea GST (ns-GST-T). As GSTs play a significant role in antioxidant defense, we checked the expression pattern of ns-GST-0 in N. succinea after exposure to copper (CUCl2 12 to 72 mu g/L), which is an oxidative stress-inducing agent. After exposure to CUCl2, ns-GST-O gene was dramatically up-regulated and when compared with ns-GST-T the expression pattern was more pronounced at all the concentrations of copper. Even the basal transcription levels of ns-GST-O were higher than those of ns-GST-T To further characterize the catalytic properties of ns-GST-O, we constructed a recombinant ns-GST-O plasmid with a 6x His-Tag at the N-terminal of the full-length ns-GST-O cDNA. Recombinant ns-GST-O protein was highly expressed in transformed Escherichia coli. The effect of pH, temperature and chemical inhibitors on the enzyme activity of ns-GST-O was also studied and compared with the reported effect of these factors on recombinant ns-GST-T protein. These results suggest that, like other types of GSTs, ns-GST-O protein plays a conserved antioxidant role in the polychacte N. succinea. (C) 2007 Elsevier Inc. All rights reserved.
URI
https://www.sciencedirect.com/science/article/pii/S153204560700138Xhttps://repository.hanyang.ac.kr/handle/20.500.11754/107395
ISSN
1532-0456; 1878-1659
DOI
10.1016/j.cbpc.2007.05.003
Appears in Collections:
COLLEGE OF SCIENCE AND CONVERGENCE TECHNOLOGY[E](과학기술융합대학) > MARINE SCIENCE AND CONVERGENCE ENGINEERING(해양융합공학과) > Articles
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