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- W4367054582 abstract "Abstract Surface display co-opts yeast’s innate ability to embellish its cell wall with mannoproteins, thus converting the yeast’s outer surface into a growing and self-sustaining catalyst. However, the efficient toolbox for converting the enzyme of interest into its surface-displayed isoform is currently lacking, especially if the isoform needs to be anchored to the cell wall near the isoform’s N-terminus. Aiming to advance such N-terminally anchored surface display, we employed in silico and machine-learning strategies to study the 3D structure, function, genomic organisation, and evolution of the Pir protein family, whose members evolved to covalently attach themselves near their N-terminus to the β-1,3-glucan of the cell wall. Through the newly-gained insights, we rationally engineered 14 S. cerevisiae Hsp150 (Pir2)-based fusion proteins. We quantified their performance, uncovering guidelines for efficient yeast surface display while developing a construct that promoted a 2.5-fold more efficient display than the full-length Hsp150 and a Pir-tag, i.e., a peptide spanning only 4.5 kDa but promoting as efficient surface display as the full-length Hsp150. These constructs fortify the existing surface display toolbox, allowing for a prompt and routine refitting of any protein into its N-terminally anchored isoform. Graphical abstract" @default.
- W4367054582 created "2023-04-27" @default.
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- W4367054582 date "2023-04-25" @default.
- W4367054582 modified "2023-10-15" @default.
- W4367054582 title "Boosting N-terminally anchored yeast surface display via structural insights into<i>S. cerevisiae</i>Pir proteins" @default.
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- W4367054582 doi "https://doi.org/10.1101/2023.04.25.538238" @default.
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