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000143329 0247_ $$2doi$$a10.1007/s13361-019-02176-9
000143329 0247_ $$2pmid$$apmid:30915654
000143329 0247_ $$2ISSN$$a1044-0305
000143329 0247_ $$2ISSN$$a1879-1123
000143329 0247_ $$2altmetric$$aaltmetric:57825006
000143329 037__ $$aDKFZ-2019-00919
000143329 041__ $$aeng
000143329 082__ $$a530
000143329 1001_ $$aKatsanovskaja, Ksenia$$b0
000143329 245__ $$aNegative Ion Mode Collision-Induced Dissociation for Analysis of Protein Arginine Methylation.
000143329 260__ $$aNew York [u.a.]$$bSpringer$$c2019
000143329 3367_ $$2DRIVER$$aarticle
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000143329 520__ $$aArginine methylation is a common protein post-translational modification (PTM) that plays a key role in eukaryotic cells. Three distinct types of this modification are found in mammals: asymmetric Nη1Nη1-dimethylarginine (aDMA), symmetric Nη1Nη2-dimethylarginine (sDMA), and an intermediate Nη1-monomethylarginine (MMA). Elucidation of regulatory mechanisms of arginine methylation in living organisms requires precise information on both the type of the modified residues and their location inside the protein amino acid sequences. Despite mass spectrometry (MS) being the method of choice for analysis of multiple protein PTMs, unambiguous characterization of protein arginine methylation may not be always straightforward. Indeed, frequent internal basic residues of Arg methylated tryptic peptides hamper their sequencing under positive ion mode collision-induced dissociation (CID), the standardly used tandem mass spectrometry method, while the relative stability of the aDMA and sDMA side chains under alternative non-ergodic electron-based fragmentation techniques, electron-capture and electron transfer dissociations (ECD and ETD), may impede differentiation between the isobaric residues. Here, for the first time, we demonstrate the potential of the negative ion mode collision-induced dissociation MS for analysis of protein arginine methylation and present data revealing that the negative polarity approach can deliver both an unambiguous identification of the arginine methylation type and extensive information on the modified peptide sequences.
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000143329 7001_ $$aDriver, Taran$$b1
000143329 7001_ $$0P:(DE-HGF)0$$aPipkorn, Rüdiger$$b2
000143329 7001_ $$aEdelson-Averbukh, Marina$$b3
000143329 773__ $$0PERI:(DE-600)2019911-9$$a10.1007/s13361-019-02176-9$$n7$$p1229-1241$$tJournal of the American Society for Mass Spectrometry$$v30$$x1879-1123$$y2019
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000143329 9141_ $$y2019
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