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Review
.2013 Dec;12(12):3532-42.
doi: 10.1074/mcp.M113.031310. Epub 2013 Jul 25.

Proteolytic post-translational modification of proteins: proteomic tools and methodology

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Review

Proteolytic post-translational modification of proteins: proteomic tools and methodology

Lindsay D Rogers et al. Mol Cell Proteomics.2013 Dec.

Abstract

Proteolytic processing is a ubiquitous and irreversible post-translational modification involving limited and highly specific hydrolysis of peptide and isopeptide bonds of a protein by a protease. Cleavage generates shorter protein chains displaying neo-N and -C termini, often with new or modified biological activities. Within the past decade, degradomics and terminomics have emerged as significant proteomics subfields dedicated to characterizing proteolysis products as well as natural protein N and C termini. Here we provide an overview of contemporary proteomics-based methods, including specific quantitation, data analysis, and curation considerations, and highlight exciting new and emerging applications within these fields enabling in vivo analysis of proteolytic events.

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Figures

Fig. 1.
Fig. 1.
Representation of select N- and C-terminal peptide enrichment strategies. COFRADIC is shown as a combination of two variations of the method employing either 2,4,6-trinitrobenzenesulfonic acid (TNBS) treatment for enrichment of N-terminal peptides or N-Hydroxysuccinimidyl-butyrate treatment for separation of N- and C-terminal peptides. Refer to the main text for a description of each method.
Fig. 2.
Fig. 2.
Quantitation and terminomics data.A, flow diagram representing quantitation of terminal peptides between a control and protease-treated condition.B, schematic showing quantifiable N-terminal peptides following stable-isotope labeling methods targeting primary amines. X represents any amino acid except lysine; red diamonds represent an amine modification such as acetylation.
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