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The University of Southampton
Biological Sciences

Understanding the functions of the N-end rule pathway of targeted protein degradation using genetics and proteomics Event

Time:
13:00 - 14:00
Date:
3 February 2016
Venue:
Life Sciences Building 85, Room 2207, University of Southampton, Highfield Campus

For more information regarding this event, please telephone Kim Lipscombe on 02380597747 or email K.R.Lipscombe@soton.ac.uk .

Event details

This talk is part of the Centre for Biological Sciences Invited Speaker Series. Open to all.

The N-end rule pathway of targeted protein degradation links the half-life of a protein to the identity of its amino (N-) terminal residue. In Arabidopsis, proteins with basic and aromatic N-termini are targeted for degradation by the PROTEOLYSIS6 (PRT6) and PROTEOLYSIS1 (PRT1) E3 ligases, respectively. Proteins with acidic N-termini may also become substrates for PRT6 following post-translational arginylation, which is catalysed by arginyltransferase (ATE) enzymes. This arginine sub-branch of the N-end rule plays roles in the control of germination, seed oil mobilisation, hormone signalling, leaf development and senescence. The pathway also functions as a sensor of oxygen and NO in animals and plants. Despite the importance of protein degradation by the N-end rule, to date the only confirmed substrates of ATE and PRT6 are selected proteins initiating with Met-Cys which enter the pathway following N-terminal Met excision and arginylation. However, proteins can also potentially become N-end rule substrates following cleavage by endopeptidases. In this talk I will discuss the use of quantitative proteomics, N-terminal peptide enrichment and affinity purification to identify substrates and interacting proteins of N-end rule components in plants and our efforts to unravel the downstream targets of the pathway using genetics.

Speaker information

Dr. Frederica Theodoulou,Rothamsted Research,Principal Investigator

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