TY - JOUR
T1 - Regulation of TG accumulation and lipid droplet morphology by the novel TLDP1 in Aurantiochytrium limacinum F26-b
AU - Watanabe, Takashi
AU - Sakiyama, Ryo
AU - Iimi, Yuya
AU - Sekine, Satomi
AU - Abe, Eriko
AU - Nomura, Kazuko H.
AU - Nomura, Kazuya
AU - Ishibashi, Yohei
AU - Okino, Nozomu
AU - Hayashi, Masahiro
AU - Ito, Makoto
N1 - Funding Information:
This work was supported in part by Science and Technology Research Promotion Program Grant 26050A for Agriculture, Forestry, Fisheries, and Food Industry, Japan and Japanese Ministry of Education, Culture, Science, and Technology Basic Research B Grant 15H04488. The authors declare no competing financial interests. Manuscript received 9 August 2017 and in revised form 3 October 2017. Published, JLR Papers in Press, October 12, 2017 DOI https://doi.org/10.1194/jlr.M079897
Funding Information:
This work was supported in part by Science and Technology Research Promotion Program Grant 26050A for Agriculture, Forestry, Fisheries, and Food Industry, Japan and Japanese Ministry of Education, Culture, Science, and Technology Basic Research B Grant 15H04488. The authors declare no competing financial interests.
Publisher Copyright:
Copyright © 2017 by the American Society for Biochemistry and Molecular Biology, Inc.
PY - 2017
Y1 - 2017
N2 - 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.
AB - 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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U2 - 10.1194/jlr.M079897
DO - 10.1194/jlr.M079897
M3 - Article
C2 - 29025869
AN - SCOPUS:85036513472
SN - 0022-2275
VL - 58
SP - 2334
EP - 2347
JO - Journal of Lipid Research
JF - Journal of Lipid Research
IS - 12
ER -
