Identification of SUMOylated proteins in proximity to a protein o | 31242
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

Identification of SUMOylated proteins in proximity to a protein of interest

6th International Conference & Expo on Proteomics

March 29-31, 2016 Atlanta, USA

Arman Kulyyassov, Chloe Robin, Undine Mechold, Anamarija Jurisic, Yerlan Ramanculov and Vasily Ogryzko

National Center for Biotechnology, Kazakhstan
Institut de Canc�?©rologie Gustave Roussy, France
Institut Pasteur, France

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

Small ubiquitin like modifier (SUMO) proteins are a group of small proteins that are covalently linked to and disconnected from other proteins in cells to modify their function. SUMOylation is a post translational modification involved in various cellular processes, such as transcriptional regulation, sub cellular localization, DNA repair, apoptosis, response to stress and progression through the cell cycle. In order to study SUMO dependent signalling and regulation, we have developed a systematic proteomics based approach based on Proximity Utilizing Biotinylation (PUB). The co expression of a protein of interest, fused to BirAligase with the fusion of a SUMO with BAP (Biotin Acceptor Peptide, specifically biotinylated by BirA) leads to Biotinylated of SUMO modified proteins interacting with (orelse in proximity to) the BirA fusion. Accordingly, we decided to identify SUMOylated proteins in proximity with emerin, nucleolin and HP1�?³nuclear proteins that are distinctly localized in the nucleus. For proteomic analysis, the Biotinylated proteins were purified with streptavidin agarose and analyzed by Gel-LC-MS/MS. In addition to the many proteins, found in common in all biotinylated samples, we identified proteins that were either unique or significantly enriched in a particular sample. Consistent with its known localization, the emerin specific sample was enriched in RANGAP1, known to require SUMOylation for its targeting to the nuclear envelope. The SUMOylated nucleolin associated proteins were represented by the nucleoli proteins nucleophosmin and nucleolar protein 58. Finally, we found several proteins in the HP1�?³ sample, already known as HP1 interaction partners (KAP1, hnrpU, Ncor1).

Biography :