Branimir Bertoša, a researcher from the Chemistry Department, in collaboration with researchers from the Ruđer Bošković Institute (Andrea Hloušek-Kasun, Petra Mikolčević, Marija Matković, Andreja Mikoč) and the University of Oxford (Johannes Gregor Matthias Rack, Callum Tromans-Coia, Marion Schuller, Gytis Jankevicius, Ivan Ahel) has published the scientific publication Streptomyces coelicolor macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA. The paper was published in the prestigious journal Computational and Structural Biotechnology Journal (IF = 7.271).
ADP-ribosylation is an ancient, highly conserved, and reversible covalent modification in which ADPr from NAD+ is transferred onto the target (macro)molecule. The system consists of ADPr-transferases which catalyse the transfer of ADPr, while the ADPr-hydrolases ensure reversibility. ADP-ribosylation controls important cellular processes, conserved from bacteria to humans. Protein SCO6735 from Streptomyces coelicolor is a homologue to human protein TARG1, whose mutation causes neurodegenerative disease. A combination of computational and experimental research revealed a novel catalytic mechanism of DNA-(ADP-ribose) hydrolysis characteristic for this subgroup of SCO6735-related proteins.
The results presented in the paper are obtained in the frame of doctoral thesis of Andrea Hloušek-Kasun which is supervised by Andreja Mikoč i Branimir Bertoša.
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