Translational control of protein folding by elongation kinetics (B14*)

Many proteins begin to fold as they emerge from translating ribosomes. The interplay between synonymous codon choice and matching tRNA supply can promote folding by modulating local translation rates, but the underlying regulatory principles are largely unknown. In this project, we will combine ribosome profiling with limited proteolysis mass spectrometry (LiP MS) to define how changes in tRNA or co translational chaperone availability impact translation and protein conformation landscapes in yeast. This global approach will identify proteins with folding trajectories potentially modulated by elongation kinetics in vivo and help uncover underlying mRNA sequence and protein structure patterns. We will explore the nature and origins of conformational changes stemming from altered translation rates for a subset of proteins with biophysical methods.

DFG Programme Collaborative Research Centres

Subproject of SFB 1035:  Control of Protein Function by Conformational Switching

Applicant Institution Technische Universität München (TUM)

Project Head Professorin Dr. Danny Nedialkova