ArticleACS synthetic biology2022
Proteome-Scale Screening to Identify High-Expression Signal Peptides with Minimal N-Terminus Biases via Yeast Display.
Article in ACS synthetic biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Integrating fab phage and yeast display through seamless transfer of paired heavy- and light-chain libraries for efficient antibody discovery.Antibody therapeutics · 2026Article
- High-throughput screening for class I peptide MHC binding via yeast surface display.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Uncoupling protein production from growth: different strategies for intracellular and secreted proteins in yeast.Microbial cell factories · 2025Article
- YTK Display-and-Secrete: Screening for Optimal Protein Secretion Elements inACS synthetic biology · 2025Article
- A facile yeast-display approach for antibody mask discovery.Protein engineering, design & selection : PEDS · 2025Article
- A Yeast Modular Cloning (MoClo) Toolkit Expansion for Optimization of Heterologous Protein Secretion and Surface Display inACS synthetic biology · 2024Article
- Genome-wide identification and expression analysis of xyloglucan endotransglucosylase/hydrolase genes family in Salicaceae during grafting.BMC genomics · 2023Article
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5 authors.
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Abstract
Signal peptides are critical for the efficient expression and routing of extracellular and secreted proteins. Most protein production and screening technologies rely upon a relatively small set of signal peptides. Despite their central role in biotechnology, there are limited studies comprehensively examining the interplay between signal peptides and expressed protein sequences. Here, we describe a high-throughput method to screen novel signal peptides that maintain a high degree of surface expression across a range of protein scaffolds with highly variable N-termini. We find that the canonical signal peptide used in yeast surface display, derived from Aga2p, fails to achieve high surface expression for 42.5% of constructs containing diverse N-termini. To circumvent this, we have identified two novel signal peptides derived from endogenous yeast proteins, SRL1 and KISH, which are highly tolerant to diverse N-terminal sequences. This pipeline can be used to expand our understanding of signal peptide function, identify improved signal peptides for protein expression, and refine the computational tools used for signal peptide prediction.
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