真菌脂肪酸合酶（FAS）的共翻译组装分析。,Scientific Reports

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真菌脂肪酸合酶（FAS）的共翻译组装分析。
Scientific Reports ( IF 3.8 ) Pub Date : 2020-01-21 , DOI: 10.1038/s41598-020-57418-8
Manuel Fischer ₁ , Mirko Joppe ₁ , Barbara Mulinacci ₂ , Ronnald Vollrath ₂ , Kosta Konstantinidis ₂ , Peter Kötter ₃ , Luciano Ciccarelli ₄ , Janet Vonck ₄ , Dieter Oesterhelt ₂ , Martin Grininger _{1,

2}

Affiliation

酵母脂肪酸合酶（FAS）是桶形的2.6 MDa复合物。桶形形成后，两个多域亚基相互缠绕，形成一个杂二聚体复合物，每个复合物都大于200 kDa，该复合物掩埋了170,000Å2的蛋白质表面。尽管对酵母FAS具有丰富的结构和功能方面的知识，但直到最近，当发现β亚基与新生α亚基的共翻译相互作用才开始组装时，其组装仍然难以捉摸。在这里，我们在分子水平上表征酵母FAS的共翻译组装。我们表明，共翻译形成的界面对微妙的扰动敏感，因此位于新兴界面的两个氨基酸的交换可以防止组装。另一方面，还可以通过亚单位在其他位点的共翻译相互作用来启动装配，这意味着该过程并非严格地是位点或序列特异性的。我们进一步强调了酵母FAS的生物合成中的其他步骤，因为这种二聚体亚基的形成协调了复合物的形成并充当了翻译后磷酸泛素化的平台。呈现的数据支持对最近发现的真核复合体普遍存在的共翻译组装的理解，并且对于在脂肪族化合物的生物技术生产中进一步利用FAS有价值。如二聚体亚单位的形成，其协调复合物的形成并充当翻译后磷酸泛素化的平台。呈现的数据支持对最近发现的真核复合体普遍存在的共翻译组装的理解，并且对于在脂肪族化合物的生物技术生产中进一步利用FAS有价值。如二聚体亚基的形成，其协调复合物的形成并充当翻译后磷酸泛素化的平台。所提供的数据支持对最近发现的真核复合体普遍存在的共翻译组装的理解，并且对于在脂肪族化合物的生物技术生产中进一步利用FAS有价值。

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

The yeast fatty acid synthase (FAS) is a barrel-shaped 2.6 MDa complex. Upon barrel-formation, two multidomain subunits, each more than 200 kDa large, intertwine to form a heterododecameric complex that buries 170,000 Å2 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 β-subunit with the nascent α-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.

更新日期：2020-01-22

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