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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Bibliographic Details
Published in:3 Biotech
Main Authors: He, Yingying, Zheng, Zhou, An, Meiling, Chen, Hao, Qu, Changfeng, Liu, Fangming, Wang, Yibin, Miao, Jinlai, Hou, Xuguang
Format: Text
Language:English
Published: Springer International Publishing 2019
Subjects:
Original Article
Antarctic
The Antarctic
Antarc*
Online Access: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
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Summary: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.

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