Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L
Chlamydomonas sp. ICE-L, which can thrive in extreme environments of the Antarctic, could represent a promising alternative for polyunsaturated fatty acid (PUFA) production. A new Δ(12)-fatty acid desaturase (FAD)-encoding gene (Δ(12)CiFAD), 1269 bp in size, was cloned from Chlamydomonas sp. ICE-L....
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ftpubmed:oai:pubmedcentral.nih.gov:6689313 2023-05-15T14:04:46+02:00 Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L He, Yingying Zheng, Zhou An, Meiling Chen, Hao Qu, Changfeng Liu, Fangming Wang, Yibin Miao, Jinlai Hou, Xuguang 2019-08-10 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6689313/ http://www.ncbi.nlm.nih.gov/pubmed/31406650 https://doi.org/10.1007/s13205-019-1858-6 en eng Springer International Publishing http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6689313/ http://www.ncbi.nlm.nih.gov/pubmed/31406650 http://dx.doi.org/10.1007/s13205-019-1858-6 © King Abdulaziz City for Science and Technology 2019 3 Biotech Original Article Text 2019 ftpubmed https://doi.org/10.1007/s13205-019-1858-6 2020-09-06T00:17:26Z Chlamydomonas sp. ICE-L, which can thrive in extreme environments of the Antarctic, could represent a promising alternative for polyunsaturated fatty acid (PUFA) production. A new Δ(12)-fatty acid desaturase (FAD)-encoding gene (Δ(12)CiFAD), 1269 bp in size, was cloned from Chlamydomonas sp. ICE-L. Bioinformatics analysis showed that Δ(12)CiFAD-encoded protein was homologous to known FADs with conserved histidine motifs, and localized to the chloroplast. Functional analysis of Δ(12)CiFAD indicated that recombinant Synechococcus 6803 expressing Δ(12)CiFAD could accumulate C18:2, whereas recombinant Saccharomyces cerevisiae expressing this enzyme could not accumulate C18:2 or any other new fatty acids. These results indicate that Δ(12)CiFAD is a functional enzyme in the chloroplast that can adjust Chlamydomonas sp. ICE-L cell membrane fluidity to adapt to Antarctic extreme low-temperature environments, which give us insights into the frigostable and cold-resistant mechanisms of hypothermic organisms. Text Antarc* Antarctic PubMed Central (PMC) Antarctic The Antarctic 3 Biotech 9 9 |
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Original Article |
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Original Article He, Yingying Zheng, Zhou An, Meiling Chen, Hao Qu, Changfeng Liu, Fangming Wang, Yibin Miao, Jinlai Hou, Xuguang Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L |
topic_facet |
Original Article |
description |
Chlamydomonas sp. ICE-L, which can thrive in extreme environments of the Antarctic, could represent a promising alternative for polyunsaturated fatty acid (PUFA) production. A new Δ(12)-fatty acid desaturase (FAD)-encoding gene (Δ(12)CiFAD), 1269 bp in size, was cloned from Chlamydomonas sp. ICE-L. Bioinformatics analysis showed that Δ(12)CiFAD-encoded protein was homologous to known FADs with conserved histidine motifs, and localized to the chloroplast. Functional analysis of Δ(12)CiFAD indicated that recombinant Synechococcus 6803 expressing Δ(12)CiFAD could accumulate C18:2, whereas recombinant Saccharomyces cerevisiae expressing this enzyme could not accumulate C18:2 or any other new fatty acids. These results indicate that Δ(12)CiFAD is a functional enzyme in the chloroplast that can adjust Chlamydomonas sp. ICE-L cell membrane fluidity to adapt to Antarctic extreme low-temperature environments, which give us insights into the frigostable and cold-resistant mechanisms of hypothermic organisms. |
format |
Text |
author |
He, Yingying Zheng, Zhou An, Meiling Chen, Hao Qu, Changfeng Liu, Fangming Wang, Yibin Miao, Jinlai Hou, Xuguang |
author_facet |
He, Yingying Zheng, Zhou An, Meiling Chen, Hao Qu, Changfeng Liu, Fangming Wang, Yibin Miao, Jinlai Hou, Xuguang |
author_sort |
He, Yingying |
title |
Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L |
title_short |
Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L |
title_full |
Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L |
title_fullStr |
Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L |
title_full_unstemmed |
Molecular cloning and functional analysis of a Δ(12)-fatty acid desaturase from the Antarctic microalga Chlamydomonas sp. ICE-L |
title_sort |
molecular cloning and functional analysis of a δ(12)-fatty acid desaturase from the antarctic microalga chlamydomonas sp. ice-l |
publisher |
Springer International Publishing |
publishDate |
2019 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6689313/ http://www.ncbi.nlm.nih.gov/pubmed/31406650 https://doi.org/10.1007/s13205-019-1858-6 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
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Antarc* Antarctic |
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Antarc* Antarctic |
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3 Biotech |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6689313/ http://www.ncbi.nlm.nih.gov/pubmed/31406650 http://dx.doi.org/10.1007/s13205-019-1858-6 |
op_rights |
© King Abdulaziz City for Science and Technology 2019 |
op_doi |
https://doi.org/10.1007/s13205-019-1858-6 |
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3 Biotech |
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9 |
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9 |
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1766276070607159296 |