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MSc by Research Programme: How are SUMO substrates selected for modification

  • Full or part time
    Prof R Hay
  • Application Deadline
    Thursday, July 16, 2020
  • Self-Funded PhD Students Only
    Self-Funded PhD Students Only

About This PhD Project

Project Description

This course allows you to work alongside our world renowned experts from the School of Life Sciences and gain a ’real research’ experience. You will have the opportunity to select a research project from a variety of thematic areas of research.

You will be part of our collaborative working environment and have access to outstanding shared facilities such as microscopy and proteomics. Throughout your year, you will develop an advanced level of knowledge on your topic of interest as well as the ability to perform independent research in the topic area. Alongside basic science training in experimental design, data handling and research ethics, we will help you to develop skills in critical assessment and communication. This will be supported by workshops in scientific writing, presentation skills, ethics, laboratory safety, statistics, public engagement and optional applied bioinformatics.

The period of study is one year full-time or two years part-time research, which includes two months to write up the thesis. Please apply via the UCAS postgraduate application form: https://digital.ucas.com/courses/details?coursePrimaryId=c735d826-42b6-ca1f-50db-2a3ac6f68718

SUMO has diverse roles in cellular physiology that inmost cases are mediated by its ability to interact non-covalently with hydrophobic patches of low sequence complexity known as SUMO Interaction Motifs (SIMs). Extensive proteomic analysis has documented the co-ordinate SUMO modification of many componentsof large nucleoprotein complexes.An emerging mode of action of SUMO is that multiple members of large protein complexes, rather than single proteins, are targeted for modification by the limited number of SUMO E3 ligases. Although the modification of components of the complexes may be sub-stoichiometric this still allows them to interact non-covalently with the more abundant SIM sequences. This serves to increase the stability of the complex such that it attains or retains biological activity. In this situation SUMO modification is acting as a relatively unspecific biological glue.

The aim of the project is to determine the molecular basis for the recognition of the nucleoprotein complexes and the SUMO modification of their protein components.

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