Open AccessIdentification of a Chlamydomonas plastidial 2‐lysophosphatidic acid acyltransferase and its use to engineer microalgae with increased oil content
Author(s) -
Yamaoka Yasuyo,
Achard Dorine,
Jang Sunghoon,
Legéret Bertrand,
Kamisuki Shogo,
Ko Donghwi,
SchulzRaffelt Miriam,
Kim Yeongho,
Song WonYong,
Nishida Ikuo,
LiBeisson Yonghua,
Lee Youngsook
Publication year - 2016
Publication title -
plant biotechnology journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.525
H-Index - 115
eISSN - 1467-7652
pISSN - 1467-7644
DOI - 10.1111/pbi.12572
Subject(s) - chlamydomonas reinhardtii , plastid , lysophosphatidic acid , biology , acyltransferase , biochemistry , phosphatidic acid , biosynthesis , chlamydomonas , enzyme , gene , chloroplast , membrane , mutant , phospholipid , receptor
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 (Cr LPAAT 1) 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 Cr LPAAT 1 prefers 16:0‐CoA to 18:1‐CoA as an acyl donor. Fluorescent protein‐tagged Cr LPAAT 1 was localized to the plastid membrane in C. reinhardtii cells. Furthermore, expression of Cr LPAAT 1 in plastids led to a > 20% increase in oil content under nitrogen‐deficient conditions. Taken together, these results demonstrate that Cr LPAAT 1 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.