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

By Pitter Huesgen, Philipp F Lange, Lindsay D Rogers, Nestor Solis, Ulrich Eckhard, Oded Kleifeld, Theodoros Goulas, F Xavier Gomis-Rüth and Christopher M Overall

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

Topics: info:eu-repo/classification/ddc/570
Publisher: Nature Publishing Group
Year: 2015
DOI identifier: 10.1038/nmeth.3177
OAI identifier: oai:juser.fz-juelich.de:185849
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