New exciting publication in Nature Communications from fruitful collaboration with colleagues from the University of Ljubljana and Vrije Universiteit Brussels

We are pleased to present the study focused on the newfound function of the intrinsically disordered domain of antitoxin protein HigA2 from Vibrio cholerae. The main function of HigA2 is binding and neutralization of HigB2 toxin through high-affinity folding‑upon‑binding interaction. Our new study reveals that the disordered domain also mediates fuzzy interactions between HigA2 and its operator sequence, further strengthening the binding of the C-terminal structured domain of HigA2 to DNA. Matic Kovačič and Janez Plavec from our lab contributed to the characterization of the HigA2 protein by performing NMR experiments for the assignment of HigA2 backbone signals, which was followed by NMR titration experiments of HigA2 with the operator dsDNA to reinforce the results of the complementary methods on the HigA2-DNA binding mechanism.

Link to the Nature Communications paper is available here

As an additional honor, the article was chosen to be featured in the Editor’s Highlights webpage of recent research called “Structural biology, biochemistry and biophysics”.
Link to the dedicated Editors’ Highlights page is available here

18. 4. 2024

Invitation to apply for the 54th Krka prizes

We encourage all eligible researchers to apply for the 54th Krka Prizes. The application process is now open and will close on July 5 ,2024.

Find more information here (in Slovene).

14. 2. 2024