Role of Ubiquitin and SUMO in Genome Biology
Department
Cell Dynamics and Signaling
Research group
Ubiquitin (-like) signaling and Proteomics
Project code
Description
Our genome is formed by several molecules of DNA that are scaffolded onto proteic structures conforming the chromatin. The most elemental chromatin unit is the nucleosome, where 146 base pairs of DNA wrap a histone core consisting of two units of histone H3, H4, H2A and H2B types.
Another histone type, linker Histone H1, is present in compacted areas of our genome.
Apart from chemical modifications on the DNA molecule, Post Translational Modifications (PTMs) on the histones represent the main source of epigenetic information. The variety of PTMs over histones ranges from small chemical modifications such as phosphorylations, acetylations or methylations to the covalent attachment of small proteins such as Ubiquitin or Small Ubiquitin-like MOdifiers (SUMOs). Modification by SUMOs have been reported over every histone type on different residues. Although SUMOylation is essential for cell proliferation and different SUMO waves are crucial in lineage differentiation and development, we are greatly limited in our knowledge about what the function and relevance of histone sumoylation in genome biology is, main because of the lack of specific tools enabling such research.
We have developed a new approach, termed PLAMSseq, which enables the Proteogenomic characterization of chromatin-asociated (ubiquitin-like modified) proteins, including histones. We have successfully applied this approach to study histone H1 SUMOylation. Now, we want to apply this approach to study the SUMOylation of the core histones and also to investigate the dynamics of histone H1 sumoylation through development.
Moreover, we intend to investigate the role of a novel ubiquitin E3 enzyme involved in genome replication
Project investigators
- Román González Prieto – Principal Investigator
- Carmen Espejo Serrano
- Lourdes González Vinceiro
- Emily Esperanza Soto Hidalgo
Funding entities
Proyecto de investigación PID2024-159761NB-I00 financiado por MICIU/AEI/10.13039/501100011033 y por FEDER, UE
