Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity
Abstract Taurine has been reported high amounts in marine animals to maintain osmotic balance between osmoformers and sea water. Approximately 80% of the total amino-acid content is taurine in Pacific oyster Crassostrea gigas, an intertidal and euryhaline species. In this study, we cloned the two co...
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ftdoajarticles:oai:doaj.org/article:a1dc3a69c8d344aba6922f2348f9503a 2023-05-15T15:58:00+02:00 Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity Xuelin Zhao Qi Li Qian Meng Chenyang Yue Chengxun Xu 2017-07-01T00:00:00Z https://doi.org/10.1038/s41598-017-05852-6 https://doaj.org/article/a1dc3a69c8d344aba6922f2348f9503a EN eng Nature Portfolio https://doi.org/10.1038/s41598-017-05852-6 https://doaj.org/toc/2045-2322 doi:10.1038/s41598-017-05852-6 2045-2322 https://doaj.org/article/a1dc3a69c8d344aba6922f2348f9503a Scientific Reports, Vol 7, Iss 1, Pp 1-10 (2017) Medicine R Science Q article 2017 ftdoajarticles https://doi.org/10.1038/s41598-017-05852-6 2022-12-31T07:10:11Z Abstract Taurine has been reported high amounts in marine animals to maintain osmotic balance between osmoformers and sea water. Approximately 80% of the total amino-acid content is taurine in Pacific oyster Crassostrea gigas, an intertidal and euryhaline species. In this study, we cloned the two copies of cysteine sulfinate decarboxylase (CSAD), the key enzyme in taurine biosynthesis pathway, screened in oyster genome data. Sequentially, we compared the expression patterns of CgCSAD1 and CgCSAD2 under low salinity treatment (8‰ and 15‰) using different families from two populations. There was no correlation between the expression of CSAD and the different population. Notably, CgCSAD1 increased significantly in treated groups for 24 h, but CgCSAD2 had no significant differentiation. Moreover, the results of CgCSAD1 interference provided the evidence of the positive correlation between CgCSAD1 expressions and taurine contents. The zinc finger domain showed in multi-alignment results may be the important character of CgCSAD1 as the key enzyme in taurine biosynthesis to regulate taurine pool in response to low salinity. This study provides a new evidence for the important role of taurine in adaptation to low salinity in oyster. In addition, it is a good model to discuss the function and evolution of the duplication in mollusks. Article in Journal/Newspaper Crassostrea gigas Pacific oyster Directory of Open Access Journals: DOAJ Articles Pacific Scientific Reports 7 1 |
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Medicine R Science Q |
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Medicine R Science Q Xuelin Zhao Qi Li Qian Meng Chenyang Yue Chengxun Xu Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity |
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Medicine R Science Q |
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Abstract Taurine has been reported high amounts in marine animals to maintain osmotic balance between osmoformers and sea water. Approximately 80% of the total amino-acid content is taurine in Pacific oyster Crassostrea gigas, an intertidal and euryhaline species. In this study, we cloned the two copies of cysteine sulfinate decarboxylase (CSAD), the key enzyme in taurine biosynthesis pathway, screened in oyster genome data. Sequentially, we compared the expression patterns of CgCSAD1 and CgCSAD2 under low salinity treatment (8‰ and 15‰) using different families from two populations. There was no correlation between the expression of CSAD and the different population. Notably, CgCSAD1 increased significantly in treated groups for 24 h, but CgCSAD2 had no significant differentiation. Moreover, the results of CgCSAD1 interference provided the evidence of the positive correlation between CgCSAD1 expressions and taurine contents. The zinc finger domain showed in multi-alignment results may be the important character of CgCSAD1 as the key enzyme in taurine biosynthesis to regulate taurine pool in response to low salinity. This study provides a new evidence for the important role of taurine in adaptation to low salinity in oyster. In addition, it is a good model to discuss the function and evolution of the duplication in mollusks. |
format |
Article in Journal/Newspaper |
author |
Xuelin Zhao Qi Li Qian Meng Chenyang Yue Chengxun Xu |
author_facet |
Xuelin Zhao Qi Li Qian Meng Chenyang Yue Chengxun Xu |
author_sort |
Xuelin Zhao |
title |
Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity |
title_short |
Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity |
title_full |
Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity |
title_fullStr |
Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity |
title_full_unstemmed |
Identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in Crassostrea gigas in response to low salinity |
title_sort |
identification and expression of cysteine sulfinate decarboxylase, possible regulation of taurine biosynthesis in crassostrea gigas in response to low salinity |
publisher |
Nature Portfolio |
publishDate |
2017 |
url |
https://doi.org/10.1038/s41598-017-05852-6 https://doaj.org/article/a1dc3a69c8d344aba6922f2348f9503a |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_source |
Scientific Reports, Vol 7, Iss 1, Pp 1-10 (2017) |
op_relation |
https://doi.org/10.1038/s41598-017-05852-6 https://doaj.org/toc/2045-2322 doi:10.1038/s41598-017-05852-6 2045-2322 https://doaj.org/article/a1dc3a69c8d344aba6922f2348f9503a |
op_doi |
https://doi.org/10.1038/s41598-017-05852-6 |
container_title |
Scientific Reports |
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7 |
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1 |
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1766393727217041408 |