Identification of the major functional proteins of prokaryotic lipid droplets
Identification of the major functional proteins of prokaryotic lipid droplets
复制标题
原核脂滴主要功能蛋白的鉴定
DOI：
10.1194/jlr.m021899
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发表时间：
2012-03-01
影响因子：
6.5
通讯作者：
Liu, Pingsheng
中科院分区：
文献类型：
--
作者：
Ding, Yunfeng;Yang, Li;Liu, Pingsheng
细胞内甘油三酯（TAG）在脂滴（LDs）中的储存与人类许多代谢性疾病的进展以及植物和微生物生物燃料的开发有关。然而，人们对LDs的生物成因和动力学了解甚少。与其他生物相比，细菌似乎是研究LD生物学的一个更好的模型系统，因为它们相对简单，并且能够高效地将生物量转化为TAG。我们从Rhodococcus sp. RHA 1（一种能从多种碳源产生TAG的细菌）中获得了高纯度的LD，并对LD蛋白质组进行了全面的表征。在鉴定的228个LD相关蛋白中，两个主要蛋白ro 02104和PspA约占总LD蛋白的15%。ro 02104的预测结构与哺乳动物血浆脂蛋白的结构蛋白--载脂蛋白相似。ro 02104的缺失导致了超大LD的形成，这表明ro 02104在细胞LD动力学中起着关键作用。ro 02104 LD靶向结构域（氨基酸83-146）的推定α螺旋也与载脂蛋白的α螺旋相似。我们报道了在原核LDs的蛋白质组中鉴定出的228种蛋白质，鉴定了该细胞器的一种推定结构蛋白，并提示载脂蛋白可能在中性脂质的储存和运输中具有进化上的保守作用。丁，Y.，L. Yang，S. Zhang， Y. Wang，Y. Du，J. Pu，G.彭，Y. Chen，H. Zhang，Ju，H. Hang，P. Wu，F. Yang，H. Yang，杨树A. Steinbuchel和P.刘。原核生物脂滴主要功能蛋白的鉴定。《脂类研究杂志》，2012年。第五十三章，第399-411节。
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 alpha 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.-Ding, Y., L. Yang, S. Zhang, Y. Wang, Y. Du, J. Pu, G. Peng, Y. Chen, H. Zhang, J. Yu, H. Hang, P. Wu, F. Yang, H. Yang, A. Steinbuchel, and P. Liu. Identification of the major functional proteins of prokaryotic lipid droplets. J. Lipid Res. 2012. 53: 399-411.