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Dynamics of the Lipid Droplet Proteome of the Oleaginous Yeast Rhodosporidium toruloides
Zhu, Zhiwei1; Ding, Yunfeng2; Gong, Zhiwei1; Yang, Li2; Zhang, Sufang1,3; Zhang, Congyan2; Lin, Xinping1; Shen, Hongwei1,3; Zou, Hanfa1; Xie, Zhensheng2; Yang, Fuquan2; Zhao, Xudong2; Liu, Pingsheng2; Zhao, Zongbao K.1,3
Source PublicationEUKARYOTIC CELL
2015-03-01
DOI10.1128/EC.00141-14
Volume14Issue:3Pages:252-264
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectMicrobiology ; Mycology
WOS Research AreaMicrobiology ; Mycology
WOS KeywordSACCHAROMYCES-CEREVISIAE ; ASPERGILLUS-NIDULANS ; BIODIESEL PRODUCTION ; HIGH CONFIDENCE ; BODY PROTEIN ; FAT STORAGE ; REVEALS ; IDENTIFICATION ; LOCALIZATION ; ACCUMULATION
AbstractLipid droplets (LDs) are ubiquitous organelles that serve as a neutral lipid reservoir and a hub for lipid metabolism. Manipulating LD formation, evolution, and mobilization in oleaginous species may lead to the production of fatty acid-derived biofuels and chemicals. However, key factors regulating LD dynamics remain poorly characterized. Here we purified the LDs and identified LD-associated proteins from cells of the lipid-producing yeast Rhodosporidium toruloides cultured under nutrient-rich, nitrogen-limited, and phosphorus-limited conditions. The LD proteome consisted of 226 proteins, many of which are involved in lipid metabolism and LD formation and evolution. Further analysis of our previous comparative transcriptome and proteome data sets indicated that the transcription level of 85 genes and protein abundance of 77 proteins changed under nutrient-limited conditions. Such changes were highly relevant to lipid accumulation and partially confirmed by reverse transcription-quantitative PCR. We demonstrated that the major LD structure protein Ldp1 is an LD marker protein being upregulated in lipid-rich cells. When overexpressed in Saccharomyces cerevisiae, Ldp1 localized on the LD surface and facilitated giant LD formation, suggesting that Ldp1 plays an important role in controlling LD dynamics. Our results significantly advance the understanding of the molecular basis of lipid overproduction and storage in oleaginous yeasts and will be valuable for the development of superior lipid producers.
Language英语
WOS IDWOS:000350666000006
Citation statistics
Cited Times:32[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/146069
Collection中国科学院大连化学物理研究所
Affiliation1.Chinese Acad Sci, Dalian Inst Chem Phys, Div Biotechnol, Dalian, Peoples R China
2.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing, Peoples R China
3.Chinese Acad Sci, Dalian Inst Chem Phys, Dalian Natl Lab Clean Energy, Dalian, Peoples R China
Recommended Citation
GB/T 7714
Zhu, Zhiwei,Ding, Yunfeng,Gong, Zhiwei,et al. Dynamics of the Lipid Droplet Proteome of the Oleaginous Yeast Rhodosporidium toruloides[J]. EUKARYOTIC CELL,2015,14(3):252-264.
APA Zhu, Zhiwei.,Ding, Yunfeng.,Gong, Zhiwei.,Yang, Li.,Zhang, Sufang.,...&Zhao, Zongbao K..(2015).Dynamics of the Lipid Droplet Proteome of the Oleaginous Yeast Rhodosporidium toruloides.EUKARYOTIC CELL,14(3),252-264.
MLA Zhu, Zhiwei,et al."Dynamics of the Lipid Droplet Proteome of the Oleaginous Yeast Rhodosporidium toruloides".EUKARYOTIC CELL 14.3(2015):252-264.
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