NrdR in Streptococcus and Listeria spp.: DNA Helix Phase Dependence of the Bacterial Ribonucleotide Reductase Repressor.

ABSTRACT: NrdR is a universal transcriptional repressor of bacterial genes coding for ribonucleotide reductases (RNRs), essential enzymes that provide DNA building blocks in all living cells. Despite its bacterial prevalence, the NrdR mechanism has been scarcely studied. We report the biochemical, biophysical, and bioinformatical characterization of NrdR and its binding sites from two major bacterial pathogens of the phylum Bacillota Listeria monocytogenes and Streptococcus pneumoniae. NrdR consists of a Zn-ribbon domain followed by an ATP-cone domain. We show that it forms tetramers that bind to DNA when loaded with ATP and dATP, but if loaded with only ATP, NrdR forms various oligomeric complexes unable to bind DNA. The DNA-binding site in L. monocytogenes is a pair of NrdR boxes separated by 15-1

SUBMITTER: Shahid S 

PROVIDER: S-EPMC12051234 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature