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题名: Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS
作者: Fischer, Manuel1;  Rhinow, Daniel2;  Zhu, Zhiwei3;  Mills, Deryck J.2;  Zhao, Zongbao K.3, 4;  Vonck, Janet2;  Grininger, Martin1
关键词: mega-enzyme ;  multifunctional proteins ;  protein assembly ;  acyl carrier protein ;  biofuel
刊名: PROTEIN SCIENCE
发表日期: 2015-06-01
DOI: 10.1002/pro.2678
卷: 24, 期:6, 页:987-995
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biochemistry & Molecular Biology
研究领域[WOS]: Biochemistry & Molecular Biology
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.
关键词[WOS]: ACYL-CARRIER PROTEIN ;  PARTICLE ELECTRON CRYOMICROSCOPY ;  MULTIENZYME COMPLEX ;  RHODOTORULA-GLUTINIS ;  POLYKETIDE SYNTHASES ;  CRYSTAL-STRUCTURE ;  YEAST ;  SUBSTRATE ;  RESOLUTION ;  BIOSYNTHESIS
语种: 英语
WOS记录号: WOS:000355151200007
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/146287
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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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

Recommended Citation:
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.
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