期刊
NATURE METHODS
卷 12, 期 1, 页码 55-58出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nmeth.3177
关键词
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资金
- German Academic Exchange Service (DAAD)
- Michael Smith Foundation for Health Research (MSFHR)
- Alexander von Humboldt Foundation
- Breast Cancer Society of Canada
- MSFHR
- Canadian Institutes for Health Research (CIHR)
- Canada Research Chair in Metalloproteinase Proteomics and Systems Biology
- CIHR [111055]
- Canada Foundations for Innovation
- European Union
- Consotider Program of the Spanish Ministry of Science and Technology
- State Plan for Research in Science, Technology and Innovation of the Spanish Ministry of Economy and Competitiveness
To improve proteome coverage and protein C-terminal identification, we characterized the Methanosardna 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.
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