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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Huesgen, Pitter F. Lange, Philipp F. Rogers, Lindsay D. Solis, Nestor Eckhard, Ulrich Kleifeld, Oded Goulas, Theodoros Gomis-Rüth, F. Xavier Overall, Christopher M.
Description	Author Affiliation: Huesgen PF ( 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); Lange PF ( 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); Rogers LD ( 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); Solis N ( 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); Eckhard U ( 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); Kleifeld O ( Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.); Goulas T ( Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Spanish Research Council, Barcelona, Spain.); Gomis-Rüth FX ( Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Spanish Research Council, Barcelona, Spain.); Overall CM ( 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)
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.
File Format	HTM / HTML
ISSN	15487091
Issue Number	1
Volume Number	12
e-ISSN	15487105
Journal	Nature Methods
Language	English
Publisher	Nature Publishing Group
Publisher Date	2015-01-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Clinical Laboratory Techniques Metalloproteases Metabolism Proteomics Methods Amino Acid Sequence Methanosarcina Enzymology Methylation Protein Processing, Post-translational Proteome Substrate Specificity Trypsin Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology Biotechnology

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