ArticleThe Journal of biological chemistry2015
Diversity in Overall Activity Regulation of Ribonucleotide Reductase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Substrate Specificity of B12-Depedent Ribonucleotide Reductases: Biotechnology and Metabolic Implications.Chembiochem : a European journal of chemical biology · 2026Article
- How ATP and dATP reposition class III ribonucleotide reductase cone domains to regulate enzyme activity.Science advances · 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
- Article
- Analysis of insertions and extensions in the functional evolution of the ribonucleotide reductase family.Protein science : a publication of the Protein Society · 2022Article
- Structural and Biochemical Investigation of Class I Ribonucleotide Reductase from the HyperthermophileBiochemistry · 2022Article
- Article
- Still no Rest for the Reductases: Ribonucleotide Reductase (RNR) Structure and Function: An Update.Sub-cellular biochemistry · 2022Review
- Radicals in Biology: Your Life Is in Their Hands.Journal of the American Chemical Society · 2021Article
- Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase FromFrontiers in molecular biosciences · 2021Article
- A ribonucleotide reductase fromThe Journal of biological chemistry · 2020Article
- The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.The Journal of biological chemistry · 2020Article
- Proteomics of Sentinel Lymph Nodes in Early Breast Cancer for Identification of Thymidylate Synthase as a Potential Biomarker to Flag Metastasis: A Preliminary Study.Cancer management and research · 2020Article
- Convergent allostery in ribonucleotide reductase.Nature communications · 2019Article
- Structures of Class Id Ribonucleotide Reductase Catalytic Subunits Reveal a Minimal Architecture for Deoxynucleotide Biosynthesis.Biochemistry · 2019Article
- Reannotation of the Ribonucleotide Reductase in a Cyanophage Reveals Life History Strategies Within the Virioplankton.Frontiers in microbiology · 2019Article
- A glutaredoxin domain fused to the radical-generating subunit of ribonucleotide reductase (RNR) functions as an efficient RNR reductant.The Journal of biological chemistry · 2018Article
- Disruption of an oligomeric interface prevents allosteric inhibition ofThe Journal of biological chemistry · 2018Article
- An endogenous dAMP ligand inProceedings of the National Academy of Sciences of the United States of America · 2018Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribonucleotide reductase (RNR) catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, which are used as building blocks for DNA replication and repair. This process is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. There are three classes of RNRs, and class I RNRs consist of different combinations of α and β subunits. In eukaryotic and Escherichia coli class I RNRs, dATP inhibits enzyme activity through the formation of inactive α6 and α4β4 complexes, respectively. Here we show that the Pseudomonas aeruginosa class I RNR has a duplicated ATP cone domain and represents a third mechanism of overall activity regulation. Each α polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an α4 complex, which can interact with β2 to form a non-productive α4β2 complex. Other allosteric effectors induce a mixture of α2 and α4 forms, with the former being able to interact with β2 to form active α2β2 complexes. The unique features of the P. aeruginosa RNR are interesting both from evolutionary and drug discovery perspectives.
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