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

Takashi Watanabe, Ryo Sakiyama, Yuya Iimi, Satomi Sekine, Eriko Abe, Kazuko H. Nomura, Kazuya Nomura, Yohei Ishibashi, Nozomu Okino, Masahiro Hayashi, Makoto Ito

研究成果: ジャーナルへの寄稿記事

3 引用 (Scopus)

抄録

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 Aurantiochytrium limacinum 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 tldp1 gene decreased the content of TG and number of LDs per cell; however, irregular and unusually large LDs were generated in tldp1-deficient mutants. Although the level of TG synthesis was unchanged by the disruption of tldp1, the level of TG degradation was higher in tldp1-deficient mutants than in the WT. These phenotypic abnormalities in tldp1-deficient mutants were restored by the expression of tldp1. These results indicate that TLDP1 is a thraustochytrid-specific LD protein and regulates the TG accumulation and LD morphology in A. limacinum F26-b.—Watanabe, T., R. Sakiyama, Y. Iimi, S. Sekine, E. Abe, K. H. Nomura, K. Nomura, Y. Ishibashi, N. Okino, M. Hayashi, and M. Ito. Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b.

元の言語英語
ページ(範囲)2334-2347
ページ数14
ジャーナルJournal of Lipid Research
58
発行部数12
DOI
出版物ステータス出版済み - 1 1 2017

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Triglycerides
Lipids
Proteins
Plant Proteins
Electrophoresis, Gel, Two-Dimensional
Lipid Droplets
Electrophoresis
Lipid Droplet Associated Proteins
Genes
Gels
Degradation

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology
  • Cell Biology

これを引用

Watanabe, T., Sakiyama, R., Iimi, Y., Sekine, S., Abe, E., Nomura, K. H., ... Ito, M. (2017). Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b. Journal of Lipid Research, 58(12), 2334-2347. https://doi.org/10.1194/jlr.M079897

Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b. / Watanabe, Takashi; Sakiyama, Ryo; Iimi, Yuya; Sekine, Satomi; Abe, Eriko; Nomura, Kazuko H.; Nomura, Kazuya; Ishibashi, Yohei; Okino, Nozomu; Hayashi, Masahiro; Ito, Makoto.

:: Journal of Lipid Research, 巻 58, 番号 12, 01.01.2017, p. 2334-2347.

研究成果: ジャーナルへの寄稿記事

Watanabe, T, Sakiyama, R, Iimi, Y, Sekine, S, Abe, E, Nomura, KH, Nomura, K, Ishibashi, Y, Okino, N, Hayashi, M & Ito, M 2017, 'Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b', Journal of Lipid Research, 巻. 58, 番号 12, pp. 2334-2347. https://doi.org/10.1194/jlr.M079897
Watanabe, Takashi ; Sakiyama, Ryo ; Iimi, Yuya ; Sekine, Satomi ; Abe, Eriko ; Nomura, Kazuko H. ; Nomura, Kazuya ; Ishibashi, Yohei ; Okino, Nozomu ; Hayashi, Masahiro ; Ito, Makoto. / Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b. :: Journal of Lipid Research. 2017 ; 巻 58, 番号 12. pp. 2334-2347.
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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 Aurantiochytrium limacinum 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 tldp1 gene decreased the content of TG and number of LDs per cell; however, irregular and unusually large LDs were generated in tldp1-deficient mutants. Although the level of TG synthesis was unchanged by the disruption of tldp1, the level of TG degradation was higher in tldp1-deficient mutants than in the WT. These phenotypic abnormalities in tldp1-deficient mutants were restored by the expression of tldp1. These results indicate that TLDP1 is a thraustochytrid-specific LD protein and regulates the TG accumulation and LD morphology in A. limacinum F26-b.—Watanabe, T., R. Sakiyama, Y. Iimi, S. Sekine, E. Abe, K. H. Nomura, K. Nomura, Y. Ishibashi, N. Okino, M. Hayashi, and M. Ito. Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b.",
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AU - Sekine, Satomi

AU - Abe, Eriko

AU - Nomura, Kazuko H.

AU - Nomura, Kazuya

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AU - Ito, Makoto

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