ArticlePloS one2015
A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- UBA2: the gatekeeper of the sumoylation pathway and its multifaceted roles in human diseases and therapeutic prospects.Clinical and experimental medicine · 2026Review
- Dynamic sumoylation is essential in yeast for suppressing stress-induced gene expression in non-stress conditions.Nucleic acids research · 2026Article
- Article
- 1,10-phenanthroline inhibits sumoylation and reveals that yeast SUMO modifications are highly transient.EMBO reports · 2024Article
- Sumoylation is Largely Dispensable for Normal Growth but Facilitates Heat Tolerance in Yeast.Molecular and cellular biology · 2023Article
- Yeast ORC sumoylation status fine-tunes origin licensing.Genes & development · 2022Article
- Dynamic sumoylation of promoter-bound general transcription factors facilitates transcription by RNA polymerase II.PLoS genetics · 2021Article
- SUMO is a pervasive regulator of meiosis.eLife · 2021Article
- Binding to small ubiquitin-like modifier and the nucleolar protein Csm1 regulates substrate specificity of the Ulp2 protease.The Journal of biological chemistry · 2018Article
- Identification of SUMO conjugation sites in the budding yeast proteome.Microbial cell (Graz, Austria) · 2017Article
- Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity.Genes & development · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed by E1, E2, and E3 enzymes. A major barrier to understanding the diverse regulatory roles of SUMO has been a lack of suitable methods to identify protein sumoylation sites. Here we developed a mass-spectrometry (MS) based approach combining chemical and enzymatic modifications to identify sumoylation sites. We applied this method to analyze the auto-sumoylation of the E1 enzyme in vitro and compared it to the GG-remnant method using Smt3-I96R as a substrate. We further examined the effect of smt3-I96R mutation in vivo and performed a proteome-wide analysis of protein sumoylation sites in Saccharomyces cerevisiae. To validate these findings, we confirmed several sumoylation sites of Aos1 and Uba2 in vivo. Together, these results demonstrate that our chemical and enzymatic method for identifying protein sumoylation sites provides a useful tool and that a combination of methods allows a detailed analysis of protein sumoylation sites.
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Registered trials
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