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Article Abstract
The combination of random mutagenesis and high-throughput screening is an effective strategy for optimizing protein secretion in . However, this strategy is often limited by reliance on activity-dependent screening. Here, we developed a CATCHFIRE (chemically assisted tethering of chimera by fluorogenic-induced recognition) system-based screening method for the quantification of secreted protein, in which the small peptide tag (11 amino acids) was fused to the C-terminus of a target protein, and the secretion of this protein could be detected via fluorescence after addition of the mate (114 amino acids) and the fluorogenic inducer compound match. The feasibility of this method was demonstrated by monitoring the secretion of five proteins and optimizing the secretion of a nanobody via screening of a signal peptide library and a random mutagenesis library. Together, this study offers a versatile and high-throughput screening method for optimizing target protein secretion in .
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