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新型 TLDP1 调控 F26-b 细胞中 TG 蓄积和脂滴形态

Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in F26-b.

机构信息

Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka, Japan.

Department of Biological Sciences, Faculty of Sciences, Kyushu University, Fukuoka, Japan.

出版信息

J Lipid Res. 2017 Dec;58(12):2334-2347. doi: 10.1194/jlr.M079897. Epub 2017 Oct 12.

DOI:10.1194/jlr.M079897
PMID:29025869
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5711496/
Abstract

Thraustochytrids are marine single-cell protists that produce large amounts of PUFAs, such as DHA. They accumulate PUFAs in lipid droplets (LDs), mainly as constituent(s) of triacylglycerol (TG). We identified a novel protein in the LD fraction of F26-b using 2D-difference gel electrophoresis. The protein clustered with orthologs of thraustochytrids; however, the cluster was evolutionally different from known PAT family proteins or plant LD protein; thus, we named it thraustochytrid-specific LD protein 1 (TLDP1). TLDP1 surrounded LDs when expressed as a GFP-tagged form. Disruption of the gene decreased the content of TG and number of LDs per cell; however, irregular and unusually large LDs were generated in -deficient mutants. Although the level of TG synthesis was unchanged by the disruption of , the level of TG degradation was higher in -deficient mutants than in the WT. These phenotypic abnormalities in -deficient mutants were restored by the expression of These results indicate that TLDP1 is a thraustochytrid-specific LD protein and regulates the TG accumulation and LD morphology in F26-b.

摘要

裂殖壶菌是一种海洋单细胞原生生物,能够大量生产多不饱和脂肪酸(PUFAs),如二十二碳六烯酸(DHA)。它们将 PUFAs 积累在脂滴(LDs)中,主要作为三酰基甘油(TG)的组成部分。我们使用二维差异凝胶电泳在 F26-b 的 LD 部分鉴定到一种新型蛋白质。该蛋白与裂殖壶菌的同源蛋白聚类;然而,该聚类在进化上与已知的 PAT 家族蛋白或植物 LD 蛋白不同;因此,我们将其命名为裂殖壶菌特异性 LD 蛋白 1(TLDP1)。TLDP1 以 GFP 标记形式表达时会围绕 LD。 基因的破坏会降低 TG 的含量和每个细胞中的 LD 数量;然而,在缺陷突变体中会产生不规则且异常大的 LD。尽管 基因的破坏对 TG 合成水平没有影响,但在缺陷突变体中,TG 的降解水平高于 WT。WT 中表达 可以恢复缺陷突变体中的这些表型异常。这些结果表明 TLDP1 是一种裂殖壶菌特异性 LD 蛋白,可调节 F26-b 中的 TG 积累和 LD 形态。

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