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  Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS)

Fischer, M., Joppe, M., Mulinacci, B., Vollrath, R., Konstantinidis, K., Koetter, P., et al. (2020). Analysis of the co-translational assembly of the fungal fatty acid synthase (FAS). SCIENTIFIC REPORTS, 10: 895. doi:10.1038/s41598-020-57418-8.

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 Creators:
Fischer, Manuel1, Author
Joppe, Mirko1, Author
Mulinacci, Barbara2, Author              
Vollrath, Ronnald2, Author              
Konstantinidis, Kosta2, Author              
Koetter, Peter1, Author
Ciccarelli, Luciano1, Author
Vonck, Janet1, Author
Oesterhelt, Dieter2, Author              
Grininger, Martin2, Author              
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1external, ou_persistent22              
2Oesterhelt, Dieter / Membrane Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565164              

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Free keywords: PROTEIN; EVOLUTION; BIOLOGY; ALPHA
 Abstract: The yeast fatty acid synthase (FAS) is a barrel-shaped 2.6 MDa complex. Upon barrel-formation, two multidomain subunits, each more than 200kDa large, intertwine to form a heterododecameric complex that buries 170,000 angstrom (2) of protein surface. In spite of the rich knowledge about yeast FAS in structure and function, its assembly remained elusive until recently, when co-translational interaction of the beta -subunit with the nascent alpha -subunit was found to initiate assembly. Here, we characterize the co-translational assembly of yeast FAS at a molecular level. We show that the co-translationally formed interface is sensitive to subtle perturbations, so that the exchange of two amino acids located in the emerging interface can prevent assembly. On the other hand, assembly can also be initiated via the co-translational interaction of the subunits at other sites, which implies that this process is not strictly site or sequence specific. We further highlight additional steps in the biogenesis of yeast FAS, as the formation of a dimeric subunit that orchestrates complex formation and acts as platform for post-translational phosphopantetheinylation. The presented data supports the understanding of the recently discovered prevalence of eukaryotic complexes for co-translational assembly, and is valuable for further harnessing FAS in the biotechnological production of aliphatic compounds.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: 13
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: SCIENTIFIC REPORTS
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 10 Sequence Number: 895 Start / End Page: - Identifier: ISSN: 2045-2322