More than 30 research groups are active at the Department of Biochemistry and Biophysics. The research projects span across a broad range of topics covering various aspects of structure and function of biological systems. A majority of these topics is centered on biological membranes. Science for Life Laboratory, where many of our researchers are based, is also closely linked to the Department.
In a new study published in Nature Communications, researchers from Stockholm University show for the first time how NrdR binds to DNA to inhibit RNR. The novel mechanism could help scientists design better antibiotics by targeting a pathogen’s ability to reproduce.
Ribonucleotide reductase (RNR) is an essential enzyme that catalyzes the synthesis of DNA building blocks. In a new study from Britt-Marie Sjöberg’s and Pål Stenmark’s groups at DBB, they present several cryo-EM structures and the mechanism of action of NrdR. NrdR is the RNR-specific repressor, that controls transcription of RNR genes in bacteria. The repressor uses an unprecedented nucleotide-sensing oligomerization mechanism to control NrdR-dependent transcription of ribonucleotide reductases.