Identification of SUMO conjugation sites in the budding yeast proteome

Authors:

Miguel Esteras1, I-Chun Liu1, Ambrosius P. Snijders2, Adam Jarmuz1 and Luis Aragon1

doi: 10.15698/mic2017.10.593
Volume 4, pp. 331 to 341, published 02/10/2017.

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Affiliations:

1 Cell Cycle Group, MRC London Institute of Medical Sciences, Du Cane Road, London W12 0NN, UK.

2 Protein Analysis and Proteomics Platform, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.

Keywords: 

SUMO, proteome, budding yeast, mass spectrometry, site-specific SUMOylation.

Corresponding Author(s):

Luis Aragon, Cell Cycle Group, MRC London Institute of Medical Sciences, Du Cane Road, London W12 0NN, UK; luis.aragon@csc.mrc.ac.uk

Conflict of interest statement:

The authors declared that there is no conflict of interest arising from this work.

Please cite this article as:

Miguel Esteras, I-Chun Liu, Ambrosius P. Snijders, Adam Jarmuz & Luis Aragon (2017). Identification of SUMO conjugation sites in the budding yeast proteome. Microbial Cell 4(10): 331-341. doi: 10.15698/mic2017.10.593

© 2017 Esteras et al. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.

Abstract:

Post-translational modification by the small ubiquitin-like modifier (SUMO) is an important mechanism regulating protein function. Identification of SUMO conjugation sites on substrates is a challenging task. Here we employed a proteomic method to map SUMO acceptor lysines in budding yeast proteins. We report the identification of 257 lysine residues where SUMO is potentially attached. Amongst the hits, we identified already known SUMO substrates and sites, confirming the success of the approach. In addition, we tested several of the novel substrates using SUMO immunoprecipitation analysis and confirmed that the SUMO acceptor lysines identified in these proteins are indeed bona fide SUMOylation sites. We believe that the collection of SUMO sites presented here is an important resource for future functional studies of SUMOylation in yeast.