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Cryo-EM structure of fatty acid synthase (FAS) from Rhodosporidium toruloides provides insights into the evolutionary development of fungal FAS
Fischer, Manuel1; Rhinow, Daniel2; Zhu, Zhiwei3; Mills, Deryck J.2; Zhao, Zongbao K.3,4; Vonck, Janet2; Grininger, Martin1
KeywordMega-enzyme Multifunctional Proteins Protein Assembly Acyl Carrier Protein Biofuel
Source PublicationPROTEIN SCIENCE
2015-06-01
DOI10.1002/pro.2678
Volume24Issue:6Pages:987-995
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemistry & Molecular Biology
WOS Research AreaBiochemistry & Molecular Biology
WOS KeywordACYL-CARRIER PROTEIN ; PARTICLE ELECTRON CRYOMICROSCOPY ; MULTIENZYME COMPLEX ; RHODOTORULA-GLUTINIS ; POLYKETIDE SYNTHASES ; CRYSTAL-STRUCTURE ; YEAST ; SUBSTRATE ; RESOLUTION ; BIOSYNTHESIS
AbstractFungal 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.
Language英语
WOS IDWOS:000355151200007
Citation statistics
Cited Times:8[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/146287
Collection中国科学院大连化学物理研究所
Affiliation1.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
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.
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