ArticleNature communications2022
A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Ribonucleotide reductase repression: a mutational study of NrdR-binding motifs.Journal of bacteriology · 2026Article
- How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity.Science advances · 2025Article
- FleQ-Dependent regulation of the ribonucleotide reductase repressor NrdR in Pseudomonas aeruginosa during biofilm growth and infection.Scientific reports · 2025Article
- Bacterial transcriptional repressor NrdR - a flexible multifactorial nucleotide sensor.The FEBS journal · 2025Article
- NrdR in Streptococcus and Listeria spp.: DNA Helix Phase Dependence of the Bacterial Ribonucleotide Reductase Repressor.Molecular microbiology · 2025Article
- Structural insights into CDF1 accumulation on the CONSTANS promoter via a plant-specific DNA-binding domain.Nature plants · 2025Article
- The phage protein paratox is a multifunctional metabolic regulator of Streptococcus.Nucleic acids research · 2025Article
- How ATP and dATP Act as Molecular Switches to Regulate Enzymatic Activity in the Prototypical Bacterial Class Ia Ribonucleotide Reductase.Biochemistry · 2024Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribonucleotide reductase (RNR) is an essential enzyme that catalyzes the synthesis of DNA building blocks in virtually all living cells. NrdR, an RNR-specific repressor, controls the transcription of RNR genes and, often, its own, in most bacteria and some archaea. NrdR senses the concentration of nucleotides through its ATP-cone, an evolutionarily mobile domain that also regulates the enzymatic activity of many RNRs, while a Zn-ribbon domain mediates binding to NrdR boxes upstream of and overlapping the transcription start site of RNR genes. Here, we combine biochemical and cryo-EM studies of NrdR from Streptomyces coelicolor to show, at atomic resolution, how NrdR binds to DNA. The suggested mechanism involves an initial dodecamer loaded with two ATP molecules that cannot bind to DNA. When dATP concentrations increase, an octamer forms that is loaded with one molecule each of dATP and ATP per monomer. A tetramer derived from this octamer then binds to DNA and represses transcription of RNR. In many bacteria - including well-known pathogens such as Mycobacterium tuberculosis - NrdR simultaneously controls multiple RNRs and hence DNA synthesis, making it an excellent target for novel antibiotics development.
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