Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS

	Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS
	Fischer, Manuel 1; Rhinow, Daniel 2; Zhu, Zhiwei 3; Mills, Deryck J.2; Zhao, Zongbao K.3,4; Vonck, Janet 2; Grininger, Martin 1
刊名	protein science
	2015-06-01
卷号	24 期号:6 页码:987-995
关键词	mega-enzyme multifunctional proteins protein assembly acyl carrier protein biofuel
英文摘要	fungal fatty acid synthases type i (fas i) are up to 2.7 mda large molecular machines composed of large multifunctional polypeptides. half of the amino acids in fungal fas i are involved in structural elements that are responsible for scaffolding the elaborate barrel-shaped architecture and turning fungal fas i into highly efficient de novo producers of fatty acids. rhodosporidium toruloides is an oleaginous fungal species and renowned for its robust conversion of carbohydrates into lipids to over 70% of its dry cell weight. here, we use cryo-em to determine a 7.8-angstrom reconstruction of its fas i that reveals unexpected features; its novel form of splitting the multifunctional polypeptide chain into the two subunits and , and its duplicated acp domains. we show that the specific distribution into and occurs by splitting at one of many possible sites that can be accepted by fungal fas i. while, therefore, the specific distribution in and chains in r. toruloides fas i is not correlated to increased protein activities, we also show that the duplication of acp is an evolutionary late event and argue that duplication is beneficial for the lipid overproduction phenotype.
WOS标题词	science & technology ; life sciences & biomedicine
类目[WOS]	biochemistry & molecular biology
研究领域[WOS]	biochemistry & molecular biology
关键词[WOS]	acyl-carrier protein ; particle electron cryomicroscopy ; multienzyme complex ; rhodotorula-glutinis ; polyketide synthases ; crystal-structure ; yeast ; substrate ; resolution ; biosynthesis
收录类别	SCI
语种	英语
WOS记录号	WOS:000355151200007
公开日期	2016-05-09
内容类型	期刊论文
源URL	[http://cas-ir.dicp.ac.cn/handle/321008/146287]
专题	大连化学物理研究所_中国科学院大连化学物理研究所
作者单位	1.Goethe Univ Frankfurt, Cluster Excellence Macromol Complexes, Buchmann Inst Mol Life Sci, Inst Organ Chem & Chem Biol, D-60438 Frankfurt, Germany 2.Max Planck Inst Biophys, Dept Biol Struct, D-60438 Frankfurt, Germany 3.Chinese Acad Sci, Div Biotechnol, Dalian Inst Chem Phys, Dalian 116023, Peoples R China 4.Chinese Acad Sci, Dalian Natl Lab Clean Energy, Dalian Inst Chem Phys, Dalian 116023, Peoples R China
推荐引用方式 GB/T 7714	Fischer, Manuel,Rhinow, Daniel,Zhu, Zhiwei,et al. Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS[J]. protein science,2015,24(6):987-995.
APA	Fischer, Manuel.,Rhinow, Daniel.,Zhu, Zhiwei.,Mills, Deryck J..,Zhao, Zongbao K..,...&Grininger, Martin.(2015).Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS.protein science,24(6),987-995.
MLA	Fischer, Manuel,et al."Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS".protein science 24.6(2015):987-995.