ArticleMethods in molecular biology (Clifton, N.J.)2022
Profiling Sequence Specificity of Proteolytic Activities Using Proteome-Derived Peptide Libraries.
Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Processing and release of the maize phytocytokine Zip1.Plant physiology · 2026Article
- Thermostable neutral metalloprotease from Geobacillus sp. EA1 does not share thermolysin's preference for substrates with leucine at the P1' position.FEBS letters · 2025Article
- Bioengineering secreted proteases converts divergent Rcr3 orthologs and paralogs into extracellular immune co-receptors.The Plant cell · 2024Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
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Abstract
Substrate sequence specificity is a fundamental characteristic of proteolytic enzymes. Hundreds of proteases are encoded in plant genomes, but the vast majority of them have not been characterized and their distinct specificity remains largely unknown. Here we present our current protocol for profiling sequence specificity of plant proteases using Proteomic Identification of Cleavage Sites (PICS). This simple, cost-effective protocol is suited for detailed, time-resolved specificity profiling of purified or enriched proteases. The isolated active protease or fraction with enriched protease activity together with a suitable control are incubated with split aliquots of proteome-derived peptide libraries, followed by identification of specifically cleaved peptides using quantitative mass spectrometry. Detailed specificity profiles are obtained by alignment of many individual cleavage sites. The chapter covers preparation of complementary peptide libraries from heterologous sources, the cleavage assay itself, as well as mass spectrometry data analysis.
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