Identification of the major functional proteins of prokaryotic lipid droplets

Yunfeng Ding, Li Yang, Shuyan Zhang, Yang Wang, Yalan Du, Jing Pu, Gong Peng, Yong Chen, Huina Zhang, Jinhai Yu, Haiying Hang, Peng Wu, Fuquan Yang, Hongyuan Yang, Alexander Steinbuc̈hel, Pingsheng Liu

Research output: Contribution to journalArticlepeer-review

96 Scopus citations

Abstract

Storage of cellular triacylglycerols (TAGs) in lipid droplets (LDs) has been linked to the progression of many metabolic diseases in humans, and to the development of biofuels from plants and microorganisms. However, the biogenesis and dynamics of LDs are poorly understood. Compared with other organisms, bacteria seem to be a better model system for studying LD biology, because they are relatively simple and are highly efficient in converting biomass to TAG. We obtained highly purified LDs from Rhodococcus sp. RHA1, a bacterium that can produce TAG from many carbon sources, and then comprehensively characterized the LD proteome. Of the 228 LD-associated proteins identified, two major proteins, ro02104 and PspA, constituted about 15% of the total LD protein. The structure predicted for ro02104 resembles that of apolipoproteins, the structural proteins of plasma lipoproteins in mammals. Deletion of ro02104 resulted in the formation of supersized LDs, indicating that ro02104 plays a critical role in cellular LD dynamics. The putative α helix of the ro02104 LD-targeting domain (amino acids 83-146) is also similar to that of apolipoproteins. We report the identification of 228 proteins in the proteome of prokaryotic LDs, identify a putative structural protein of this organelle, and suggest that apolipoproteins may have an evolutionarily conserved role in the storage and trafficking of neutral lipids.

Original languageEnglish (US)
Pages (from-to)399-411
Number of pages13
JournalJournal of Lipid Research
Volume53
Issue number3
DOIs
StatePublished - Mar 2012
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology
  • Cell Biology

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