A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers

Archives of Biochemistry and Biophysics
Tianwei LiP Boon Chock

Abstract

Ubiquitin-like modifiers (UBLs) contain ubiquitin homology domains and can covalently modify target proteins in a manner similar to ubiquitylation. In this study, we revealed a general proteomic approach to elucidate the enzymatic pathways and identify target proteins for three UBLs: SUMO-2, SUMO-3, and NEDD8. Expression plasmids containing the cDNAs of Myc/6xHis doubly-tagged processed or non-conjugatable forms of these UBLs were constructed. The constructed vectors were then used to transfect HEK 293 Tet-On cells, and stable cell lines expressing these UBLs and their mutants were established. The epitope-tagged proteins were purified by immunoprecipitation under native conditions or by affinity chromatography on nickel resin under denaturing conditions. Purified proteins were analyzed using liquid chromatography coupled with mass spectrometry (LC-MS/MS). Most of the E1-like activating enzymes, E2-like conjugating enzymes and the majorities of the known target as well as some previously unreported proteins for SUMO-2, SUMO-3, and NEDD8 pathways were identified.

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Citations

Feb 6, 2008·Journal of Proteome Research·Jeffrey JonesLan Huang
Feb 16, 2008·EMBO Reports·Dimitris P XirodimasRonald T Hay
Oct 24, 2006·Biochimica Et Biophysica Acta·Ping Xu, Junmin Peng
Oct 19, 2011·The Biochemical Journal·Roland HjerpeThimo Kurz
Apr 7, 2015·Pancreatology : Official Journal of the International Association of Pancreatology (IAP) ... [et Al.]·David Fernández-Ramos, María L Martínez-Chantar
Apr 9, 2014·Frontiers in Plant Science·Julia Mergner, Claus Schwechheimer
Feb 20, 2008·Expert Review of Proteomics·Van G Wilson, Phillip R Heaton
Sep 17, 2008·Biochemical Society Transactions·Dimitris P Xirodimas
Oct 3, 2006·The Journal of Biological Chemistry·Tianwei LiP Boon Chock

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