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

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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)55-58
Number of pages4
JournalNature Methods
Volume12
Issue number1
DOIs
StatePublished - 1 Jan 2014
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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