Branimir Bertoša, a researcher from the Chemistry Department, and Sanja Škulj, a recent researcher from the Chemistry Department, in collaboration with researchers from the University of Nottingham (Rebecca J. Lever, Emily Simmons, Rebecca Gamble-Milner, Ryan J. Buckley, Catherine Harrison, Ashley J. Parkes, Laura Mitchell, Jacob A. Gausden, Edward L. Bolt, and Thorsten Allers) have published the scientific publication: Archaeal Hel308 suppresses recombination through a catalytic switch that controls DNA annealing. The paper was published in the prestigious journal Nucleic Acid Research (IF = 19.160).
Hel308 helicases promote genome stability in archaea and their helicase mechanism is well characterised. However, collaborators form University of Nottingham have surprisingly discovered that a single amino acid substitution results in hyper-active DNA helicase Hel308. Molecular dynamics simulations conducted at the Chemistry Department of Faculty of Science at University of Zagreb provided a molecular basis for experimentally observed differences between Phe295Ala mutant and wild type Hel308. Helicase activity starts with the DNA binding between the two protein domains that are connected through π-π interactions. Therefore, DNA binding requires the interruption of these π-π interactions. In case of Phe295Ala mutant, the mentioned network of π-π interactions cannot be formed and Hel308 is always in conformation which is available for DNA binding. Consequently, hyper-active DNA helicase activity of Hel308 is observed. The results were validated computationally and experimentally.
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