Lysine and Arginine Protein Post-translational Modifications by Enhanced DIA Libraries: Quantification in Murine Liver Disease
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 count...
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| Veröffentlicht in: | Journal of proteome research 2020-10, Vol.19 (10), p.4163-4178 |
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| container_title | Journal of proteome research |
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| creator | Robinson, Aaron E Binek, Aleksandra Venkatraman, Vidya Searle, Brian C Holewinski, Ronald J Rosenberger, George Parker, Sarah J Basisty, Nathan Xie, Xueshu Lund, Peder J Saxena, Gautam Mato, José M Garcia, Benjamin A Schilling, Birgit Lu, Shelly C Van Eyk, Jennifer E |
| description | 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. |
| doi_str_mv | 10.1021/acs.jproteome.0c00685 |
| format | Article |
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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. 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| subjects | Acetylation Animals Arginine Biochemical Research Methods Biochemistry & Molecular Biology Life Sciences & Biomedicine Liver Diseases Lysine - metabolism Mice Protein Processing, Post-Translational Proteomics Science & Technology |
| title | Lysine and Arginine Protein Post-translational Modifications by Enhanced DIA Libraries: Quantification in Murine Liver Disease |
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