Published: 25 June 2025
Researchers at the BZH have uncovered how a key RNA processing and repair enzyme from fungi, Trl1, recognizes and joins broken RNA strands. Using high-resolution X-ray crystallography at the European Synchrotron Radiation Facility (ESRF), the
team led by Jirka Peschek captured the enzyme in action—bound to its RNA substrate in a catalytically active state. The structure reveals how Trl1 precisely positions RNA ends for repair and highlights a dynamic domain that clamps onto the RNA to ensure proper alignment. These findings shed light on how cells process and splice RNA during stress responses and tRNA maturation, and offer broader insights into the evolution of RNA ligases. The study was carried out in collaboration with the BZH crystallization platform and the Bujnicki lab in Warsaw, Poland.
The study was published in Nature Structural & Molecular Biology:
Köhler, S. et al. Structure of fungal tRNA ligase Trl1 with RNA reveals conserved substrate-binding principles.
https://doi.org/10.1038/s41594-025-01589-3
Read more in the ESRF Spotlight on Science:
https://www.esrf.fr/home/news/spotlight/content-news/spotlight/x-ray-crystallography-shows-how-fungal-trna-ligase-coordinates-non-conventional-splicing.html