Project Details
Projekt
Unnatural amino acids to study protein ubiquitylation (B03)
Subject Area
Biochemistry
Term
from 2012 to 2023
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 189682160
Modification of proteins by ubiquitin alters their biochemical/biological properties. Notably, ubiquitin is not only a "modifier", but is itself subject to posttranslational modification including phosphorylation and acetylation. Similarly, the lysine residues of proteins, which are ubiquitylated, are frequently also subject to acetylation, indicating a competitive crosstalk between the two modification systems. To address how these different modifications affect the activities/properties of ubiquitin and other selected proteins, we are employing unnatural amino acids in combination with recombinant protein expression and orthogonal chemistry. Comparative functional and structural characterization of the differently modified proteins will provide intimate insights into the consequences of the different modifications and their potential physiological relevance.
DFG Programme
Collaborative Research Centres
Applicant Institution
Universität Konstanz
Project Heads
Professor Dr. Andreas Marx; Professor Dr. Martin Scheffner
