Journal
MOLECULAR & CELLULAR PROTEOMICS
Volume 16, Issue 5, Pages 717-727Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/mcp.M116.062125
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Funding
- Ministry of Science and Technology of China [2016YFA0502500]
- National Program on Key Basic Research Project [2014CBA02000, 2013CB910802]
- National International Cooperation Grant [2014DFB30010, 2014DFB30020, 2012DFB30080, CPRIT RP11 0784]
- National High-tech R&D Program of China [2015AA020 108, 2014AA020201]
- Chinese State Key Project Specialized for Infectious Diseases [2012ZX10002012-006]
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SUMOylation is a reversible post-translational modification involved in various critical biological processes. To date, there is limited approach for endogenous wild-type SUMO-modified peptides enrichment and SUMOylation sites identification. In this study, we generated a high-affinity SUMO1 antibody to facilitate the enrichment of endogenous SUMO1-modified peptides from Trypsin/Lys-C protease digestion. Following secondary Glu-C protease digestion, we identified 53 high-confidence SUMO1-modified sites from mouse testis by using high-resolution mass spectrometry. Bioinformatics analyses showed that SUMO1-modified proteins were enriched in transcription regulation and DNA repair. Nab1 was validated to be an authentic SUMOylated protein and Lys(479) was identified to be the major SUMOylation site. The SUMOylation of Nab1 enhanced its interaction with HDAC2 and maintained its inhibitory effect on EGR1 transcriptional activity. Therefore, we provided a novel approach to investigating endogenous SUMOylation sites in tissue samples.
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