Identification of a Chlamydomonas plastidial 2‐lysophosphatidic acid acyltransferase and its use to engineer microalgae with increased oil content

Summary Despite a strong interest in microalgal oil production, our understanding of the biosynthetic pathways that produce algal lipids and the genes involved in the biosynthetic processes remains incomplete. Here, we report that Chlamydomonas reinhardtii Cre09.g398289 encodes a plastid‐targeted 2‐...

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Bibliographic Details
Published in:Plant biotechnology journal 2016-11, Vol.14 (11), p.2158-2167
Main Authors: Yamaoka, Yasuyo, Achard, Dorine, Jang, Sunghoon, Legéret, Bertrand, Kamisuki, Shogo, Ko, Donghwi, Schulz‐Raffelt, Miriam, Kim, Yeongho, Song, Won‐Yong, Nishida, Ikuo, Li‐Beisson, Yonghua, Lee, Youngsook
Format: Article
Language:English
Subjects:
acyl specificity
Acyltransferase
Acyltransferases - genetics
Algae
Amino acids
Biosynthesis
Chlamydomonas
Chlamydomonas - enzymology
Chlamydomonas reinhardtii
Deoxyribonucleic acid
DNA
Enzymes
Fatty acids
Flowers & plants
Fluorescence
Genomes
Glycerol
Life Sciences
Lipids
Lysophosphatidic acid
lysophosphatidic acid acyltransferase
Microalgae
Microalgae - chemistry
Microalgae - genetics
Microalgae - metabolism
oil content
Petroleum engineering
Petroleum industry
Phosphatidic acid
Phylogenetics
Plant Oils - metabolism
plastid transformation
Plastids
Plastids - enzymology
Proteins
Ribosomal DNA
triacylglycerols
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Summary:Summary Despite a strong interest in microalgal oil production, our understanding of the biosynthetic pathways that produce algal lipids and the genes involved in the biosynthetic processes remains incomplete. Here, we report that Chlamydomonas reinhardtii Cre09.g398289 encodes a plastid‐targeted 2‐lysophosphatidic acid acyltransferase (CrLPAAT1) that acylates the sn‐2 position of a 2‐lysophosphatidic acid to form phosphatidic acid, the first common precursor of membrane and storage lipids. In vitro enzyme assays showed that CrLPAAT1 prefers 16:0‐CoA to 18:1‐CoA as an acyl donor. Fluorescent protein‐tagged CrLPAAT1 was localized to the plastid membrane in C. reinhardtii cells. Furthermore, expression of CrLPAAT1 in plastids led to a > 20% increase in oil content under nitrogen‐deficient conditions. Taken together, these results demonstrate that CrLPAAT1 is an authentic plastid‐targeted LPAAT in C. reinhardtii, and that it may be used as a molecular tool to genetically increase oil content in microalgae.
ISSN:1467-7644
1467-7652
DOI:10.1111/pbi.12572