信号肽
蛋白质组
酵母
计算生物学
生物
信号(编程语言)
酿酒酵母
蛋白质分选信号
功能(生物学)
肽
生物化学
细胞生物学
肽序列
基因
计算机科学
程序设计语言
作者
Patrick V. Holec,Karen V. Camacho,Kathryn C. Breuckman,Jody Mou,Michael E. Birnbaum
标识
DOI:10.1021/acssynbio.2c00101
摘要
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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