A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization
Thioredoxins, with a dithiol/disulfide active site (CGPC) are major highly conserved and ubiquitous proteins that are involved in protecting organisms against various oxidative stresses. In the present study, a novel thioredoxin gene was identified in antarctic microcrustacean, Euphausia superba (de...
Published in: | Fish & Shellfish Immunology |
---|---|
Main Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2017
|
Subjects: | |
Online Access: | http://ir.qdio.ac.cn/handle/337002/136724 https://doi.org/10.1016/j.fsi.2017.02.035 |
id |
ftchinacasciocas:oai:ir.qdio.ac.cn:337002/136724 |
---|---|
record_format |
openpolar |
spelling |
ftchinacasciocas:oai:ir.qdio.ac.cn:337002/136724 2023-05-15T14:03:36+02:00 A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization Li, Fengmei Ma, Liyan Zhang, Huan Xu, Li Zhu, Qianqian 2017-04-01 http://ir.qdio.ac.cn/handle/337002/136724 https://doi.org/10.1016/j.fsi.2017.02.035 英语 eng FISH & SHELLFISH IMMUNOLOGY Li, Fengmei,Ma, Liyan,Zhang, Huan,et al. A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization[J]. FISH & SHELLFISH IMMUNOLOGY,2017,63:376-383. http://ir.qdio.ac.cn/handle/337002/136724 doi:10.1016/j.fsi.2017.02.035 Antioxidant Enzyme Thioredoxin Euphausia Superba Microcrustacean Oxidative Stress Article 期刊论文 2017 ftchinacasciocas https://doi.org/10.1016/j.fsi.2017.02.035 2022-06-27T05:38:01Z Thioredoxins, with a dithiol/disulfide active site (CGPC) are major highly conserved and ubiquitous proteins that are involved in protecting organisms against various oxidative stresses. In the present study, a novel thioredoxin gene was identified in antarctic microcrustacean, Euphausia superba (designated as EsTrx1). The full-length cDNA sequences of EsTrx1 was of 621 bp, containing a 5' untranslated region (UTR) of 45 bp, a 3' UTR of 276 bp and an open reading frame (ORF) of 303 bp encoding a putative protein of 100 amino acids. The predicted molecular weight of EsTrx1 was 11.08 kDa and the theoretical isoelectric point was 4.51. Multiple sequence alignment indicated that the EsTrx1 possessed conserved CGPC redox-active site. EsTrx1 shared 68.6% similarity with the Chinese mitten crab (Eriocheir sinensis) Trx1. The predicted three-dimensional structure of EsTrx1 consisted of a central core of a four-stranded beta-sheet and four flanking alpha-helices. The high similarity of EsTrx1 with Trxls from other animals together with the phylogenetic analysis indicated that EsTrx1 could be a novel member of Trx1 sub-family. In order to elucidate its biological functions, the recombinant EsTrx1 was constructed and expressed in Escherichia coli BL21 (DE3). Experiments demonstrated that the rEsTrx1 fusion protein possessed the expected redox activity in enzymatic analysis, and be more potent than GSH in antioxidant capacity. These results together indicated that EsTrx1 could be involved in the oxidative stress response of E. superba. (C) 2017 Elsevier Ltd. All rights reserved. Article in Journal/Newspaper Antarc* Antarctic Euphausia superba Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Antarctic Fish & Shellfish Immunology 63 376 383 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
Antioxidant Enzyme Thioredoxin Euphausia Superba Microcrustacean Oxidative Stress |
spellingShingle |
Antioxidant Enzyme Thioredoxin Euphausia Superba Microcrustacean Oxidative Stress Li, Fengmei Ma, Liyan Zhang, Huan Xu, Li Zhu, Qianqian A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization |
topic_facet |
Antioxidant Enzyme Thioredoxin Euphausia Superba Microcrustacean Oxidative Stress |
description |
Thioredoxins, with a dithiol/disulfide active site (CGPC) are major highly conserved and ubiquitous proteins that are involved in protecting organisms against various oxidative stresses. In the present study, a novel thioredoxin gene was identified in antarctic microcrustacean, Euphausia superba (designated as EsTrx1). The full-length cDNA sequences of EsTrx1 was of 621 bp, containing a 5' untranslated region (UTR) of 45 bp, a 3' UTR of 276 bp and an open reading frame (ORF) of 303 bp encoding a putative protein of 100 amino acids. The predicted molecular weight of EsTrx1 was 11.08 kDa and the theoretical isoelectric point was 4.51. Multiple sequence alignment indicated that the EsTrx1 possessed conserved CGPC redox-active site. EsTrx1 shared 68.6% similarity with the Chinese mitten crab (Eriocheir sinensis) Trx1. The predicted three-dimensional structure of EsTrx1 consisted of a central core of a four-stranded beta-sheet and four flanking alpha-helices. The high similarity of EsTrx1 with Trxls from other animals together with the phylogenetic analysis indicated that EsTrx1 could be a novel member of Trx1 sub-family. In order to elucidate its biological functions, the recombinant EsTrx1 was constructed and expressed in Escherichia coli BL21 (DE3). Experiments demonstrated that the rEsTrx1 fusion protein possessed the expected redox activity in enzymatic analysis, and be more potent than GSH in antioxidant capacity. These results together indicated that EsTrx1 could be involved in the oxidative stress response of E. superba. (C) 2017 Elsevier Ltd. All rights reserved. |
format |
Article in Journal/Newspaper |
author |
Li, Fengmei Ma, Liyan Zhang, Huan Xu, Li Zhu, Qianqian |
author_facet |
Li, Fengmei Ma, Liyan Zhang, Huan Xu, Li Zhu, Qianqian |
author_sort |
Li, Fengmei |
title |
A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization |
title_short |
A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization |
title_full |
A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization |
title_fullStr |
A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization |
title_full_unstemmed |
A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization |
title_sort |
thioredoxin from antarctic microcrustacean (euphausia superba): cloning and functional characterization |
publishDate |
2017 |
url |
http://ir.qdio.ac.cn/handle/337002/136724 https://doi.org/10.1016/j.fsi.2017.02.035 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Euphausia superba |
genre_facet |
Antarc* Antarctic Euphausia superba |
op_relation |
FISH & SHELLFISH IMMUNOLOGY Li, Fengmei,Ma, Liyan,Zhang, Huan,et al. A thioredoxin from antarctic microcrustacean (Euphausia superba): Cloning and functional characterization[J]. FISH & SHELLFISH IMMUNOLOGY,2017,63:376-383. http://ir.qdio.ac.cn/handle/337002/136724 doi:10.1016/j.fsi.2017.02.035 |
op_doi |
https://doi.org/10.1016/j.fsi.2017.02.035 |
container_title |
Fish & Shellfish Immunology |
container_volume |
63 |
container_start_page |
376 |
op_container_end_page |
383 |
_version_ |
1766274310145572864 |