LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification

Pitter F Huesgen, Philip F Lange, Lindsay D Rogers, Nestor Solis, Ulrich Eckhardt, Oded Kleifeld, Theodoros Goulas, F Xavier Xavier Gomis-Ruth, Christopher M Overall

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126 Citations (Scopus)


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 degrees 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.
Original languageEnglish
Pages (from-to)55 - 58
Number of pages4
JournalNature Methods
Issue number1
Publication statusPublished - 2015

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