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Updated: Apr 20, 2026
A Mass Spectrometry-Based Proteomics Approach for Global and High-Confidence Protein R-Methylation Analysis
Published on: April 28, 2022
LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification
Pitter F Huesgen1, Philipp F Lange2, Lindsay D Rogers2
11] Centre for Blood Research, University of British Columbia, Vancouver, British Columbia, Canada. [2] Department of Oral Biological and Medical Sciences, University of British Columbia, Vancouver, British Columbia, Canada. [3] Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada. [4] Zentralinstitut für Engineering, Elektronik und Analytik, ZEA-3: Analytik, Forschungszentrum Jülich, Jülich, Germany.
Abstract:
To improve proteome coverage and protein C-terminal identification, we characterized the Methanosarcina acetivorans thermophilic proteinase LysargiNase, which cleaves before lysine and arginine up to 55 °C. Unlike trypsin, LysargiNase-generated peptides had N-terminal lysine or arginine residues and fragmented with b ion-dominated spectra. This improved protein C terminal-peptide identification and several arginine-rich phosphosite assignments. Notably, cleavage also occurred at methylated or dimethylated lysine and arginine, facilitating detection of these epigenetic modifications.
