@article{oai:tsukuba.repo.nii.ac.jp:00049112,
 author = {吉田, 昌樹 and YOSHIDA, Masaki and 鈴木, 石根 and SUZUKI, Iwane and Yoneda, Kohei and Watanabe, Makoto M.},
 issue = {5},
 journal = {Journal of Applied Phycology},
 month = {Oct},
 note = {Lipid droplets are ubiquitous cellular compartments that store neutral lipids and specific proteins localize on their surface. These proteins work as a scaffold in maintaining the lipid droplet structure or as regulators of lipogenesis or lipolysis. Previously, the most abundant lipid droplet protein, namely stramenopile-type lipid droplet protein (StLDP), was identified in the marine diatom Phaeodactylum tricornutum; however, its function remains unclear because StLDP does not reveal homology with known lipid droplet proteins and lacks a predictable domain. In this study, P. tricornutum was transformed to express a homologous StLDP gene under an fcpA promoter in order to determine its function. StLDP expression was strongly enhanced in the mutant (H8), especially in nitrogen-sufficient conditions; however, it was attenuated in nitrogen-deficient conditions. Despite the strong expression, no significant difference was observed in the lipid composition between the wild type (WT) and H8 under nitrogen-sufficient conditions. After cultivation in nitrogen-free medium for 6 days, neutral lipid content significantly increased in H8 than in WT. After 2 days of cultivation in nitrogen-free medium, 97.0% of single cells in WT formed one or two lipid droplets, whereas in H8, this proportion decreased to 78.8%, and the proportion of cells forming three or four lipid droplets increased. Thus, the function of StLDP was speculated to sequester triacylglycerol on the initial lipid droplet formation.},
 pages = {2793--2802},
 title = {Homologous expression of lipid droplet protein-enhanced neutral lipid accumulation in the marine diatom Phaeodactylum tricornutum},
 volume = {30},
 year = {2018},
 yomi = {ヨシダ, マサキ and スズキ, イワネ}
}