About our group
Protein translation is the final step of gene expression, and its fidelity is essential for the accurate production of functional proteins. Yet ribosomes make errors, generating mistranslated proteoforms whose amino-acid sequences differ from the genetically encoded template. Recent proteome-wide studies have shown that such variants are widespread across bacteria, yeast, and human cells, but their biological significance remains largely unknown. We hypothesize that mistranslation is not merely molecular noise, but a regulated source of proteome diversity that can alter protein function and, in some contexts, confer adaptive advantages. Our group studies non-genetic protein variants as a potential reservoir of previously overlooked biological functions. We focus on detecting translation errors and characterizing their causes and consequences for protein function and organismal fitness. The aim is to establish a new mechanistic perspective on how transient, non-genetic sequence variation shapes cellular phenotype and biological success.
