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Nat Methods. 2015 Jan;12(1):55-8. doi: 10.1038/nmeth.3177. Epub 2014 Nov 24.

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

Author information

1
1] 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.
2
1] 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.
3
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
4
Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Spanish Research Council, Barcelona, Spain.

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.

PMID:
25419962
DOI:
10.1038/nmeth.3177
[Indexed for MEDLINE]

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