Protein and RNA structural biology group
Team leader: dr Katarzyna Bandyra
Team leader’s e-mail address: k.bandyra@uw.edu.pl
Brief description of the research topic:
We are broadly interested in understanding the structure–function relationships of proteins and protein–nucleic acid complexes. To explore these relationships, we use a combination of biochemical, biophysical, and structural biology methods. Our work spans from in vitro studies on isolated protein-RNA complexes, to functional assays in human cells, allowing us to bridge detailed molecular insight with cellular context. A central approach in our lab is the use of cryogenic electron microscopy (cryo-EM) to determine high-resolution structures of macromolecular complexes. These structural models help us uncover the molecular mechanisms underlying complex processes, particularly those involved in RNA metabolism within human mitochondria.
Currently, our research focuses on two key mitochondrial protein systems that are critical for mitochondrial homeostasis. The first is human polynucleotide phosphorylase (hPNPase), an evolutionarily conserved exoribonuclease found in organisms ranging from bacteria to humans. In human mitochondria, hPNPase degrades RNA in complex with the helicase Suv3. However, studies in bacteria have shown that PNPase can also act as an RNA chaperone depending on its molecular context. Our aim is to investigate whether human PNPase similarly adopts dual functions, both degradative and protective, and to explore its broader roles beyond RNA decay.
We are also investigating the FASTK protein family, which includes six human mitochondrial proteins believed to contain a novel RNA-binding fold. These proteins are involved in various aspects of mitochondrial RNA metabolism, but their precise molecular functions, RNA targets, structural features, and interaction partners remain largely unknown. Given their essential roles in mitochondrial gene expression and human health, our goal is to elucidate the functions of FASTK proteins by studying their structure, RNA substrates, and protein–protein interactions.