TY - JOUR
T1 - Quantitative analysis and discovery of lysine and arginine modifications
AU - Galligan, James J.
AU - Kingsley, Philip J.
AU - Wauchope, Orrette R.
AU - Mitchener, Michelle M.
AU - Camarillo, Jeannie M.
AU - Wepy, James A.
AU - Harris, Peter S.
AU - Fritz, Kristofer S.
AU - Marnett, Lawrence J.
N1 - Funding Information:
We would like to thank Carol A. Rouzer for help in scientific discussion and preparation of the manuscript. This work was supported by the following grants from the U.S. National Institutes of Health: Grant T32 ES007028 to J.J.G.; Grants R37 CA087819 and S10OD017997 to L.J.M.; and Grant AA022146 to K.S.F.
Publisher Copyright:
© 2016 American Chemical Society.
PY - 2017/1/17
Y1 - 2017/1/17
N2 - Post-translational modifications (PTMs) affect protein function, localization, and stability, yet very little is known about the ratios of these modifications. Here, we describe a novel method to quantitate and assess the relative stoichiometry of Lys and Arg modifications (QuARKMod) in complex biological settings. We demonstrate the versatility of this platform in monitoring recombinant protein modification of peptide substrates, PTMs of individual histones, and the relative abundance of these PTMs as a function of subcellular location. Lastly, we describe a product ion scanning technique that offers the potential to discover unexpected and possibly novel Lys and Arg modifications. In summary, this approach yields accurate quantitation and discovery of protein PTMs in complex biological systems without the requirement of high mass accuracy instrumentation.
AB - Post-translational modifications (PTMs) affect protein function, localization, and stability, yet very little is known about the ratios of these modifications. Here, we describe a novel method to quantitate and assess the relative stoichiometry of Lys and Arg modifications (QuARKMod) in complex biological settings. We demonstrate the versatility of this platform in monitoring recombinant protein modification of peptide substrates, PTMs of individual histones, and the relative abundance of these PTMs as a function of subcellular location. Lastly, we describe a product ion scanning technique that offers the potential to discover unexpected and possibly novel Lys and Arg modifications. In summary, this approach yields accurate quantitation and discovery of protein PTMs in complex biological systems without the requirement of high mass accuracy instrumentation.
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U2 - 10.1021/acs.analchem.6b04105
DO - 10.1021/acs.analchem.6b04105
M3 - Article
C2 - 27982582
AN - SCOPUS:85035110637
VL - 89
SP - 1299
EP - 1306
JO - Analytical Chemistry
JF - Analytical Chemistry
SN - 0003-2700
IS - 2
ER -