Abstract:
:Proteoforms containing post-translational modifications (PTMs) represent a degree of functional diversity only harnessed through analytically precise simultaneous quantification of multiple PTMs. Here we present a method to accurately differentiate an unmodified peptide from its PTM-containing counterpart through data-independent acquisition-mass spectrometry, leveraging small precursor mass windows to physically separate modified peptidoforms from each other during MS2 acquisition. We utilize a lysine and arginine PTM-enriched peptide assay library and site localization algorithm to simultaneously localize and quantify seven PTMs including mono-, di-, and trimethylation, acetylation, and succinylation in addition to total protein quantification in a single MS run without the need to enrich experimental samples. To evaluate biological relevance, this method was applied to liver lysate from differentially methylated nonalcoholic steatohepatitis (NASH) mouse models. We report that altered methylation and acetylation together with total protein changes drive the novel hypothesis of a regulatory function of PTMs in protein synthesis and mRNA stability in NASH.
journal_name
J Proteome Resjournal_title
Journal of proteome researchauthors
Robinson AE,Binek A,Venkatraman V,Searle BC,Holewinski RJ,Rosenberger G,Parker SJ,Basisty N,Xie X,Lund PJ,Saxena G,Mato JM,Garcia BA,Schilling B,Lu SC,Van Eyk JEdoi
10.1021/acs.jproteome.0c00685subject
Has Abstractpub_date
2020-10-02 00:00:00pages
4163-4178issue
10eissn
1535-3893issn
1535-3907journal_volume
19pub_type
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