Biomolecular Structures and Interactions (BioMolStruct)

Stress granules (SG) are one type of membraneless organelles that assemble transiently in the cytosol upon acute stress, causing the arrest of mRNA translation in response to generic stress stimuli. According to a current view, SG set mature mRNAs on hold for translation during stress, and rapidly dissociate afterwards, thereby releasing bound mRNA for appropriate processing. The RNA-binding protein TIA-1 (T-cell restricted intracellular antigen-1) translocates, under stress, to the cytosol where it reversibly incorporates into SG. TIA-1, together with SERF1a, drives the prion-like assembly of SGs. We will investigate the roles of TIA-1 and SERF1a in SG formation, by studying their interactions.

NMR spectroscopy is perfectly suited for studies on intrinsically disordered proteins. However, the spectra of IDPs are typically poorly resolved due to low spectra dispersion. Pure shift NMR is a technique, which has been partly developed in our lab and is capable to significantly enhance the resolution of proton-detected NMR spectra. In this project we develop novel approaches of high resolution pure shift techniques. They will be applied in the study of intrinsically disordered proteins (IDPs) involved in the formation of stress granules (SG).

Principle investigator

Klaus Zangger 
Department of Chemistry, University of Graz
T: +43 316 380 8673