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Review
, 12 (12), 3532-42

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.

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.

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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