LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification.
basic_science · Level V
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- Record sourced from PubMed, PMID 25419962.
- Also identified by DOI 10.1038/nmeth.3177.
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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.
Medical subject headings
- Metalloproteases
- Proteomics