Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Ribonucleotide reductases.

Pär Nordlund1, Peter Reichard

  • 1Division of Biophysics and 2Division of Biochemistry, Medical Nobel Institute, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm, Sweden. par.nordlund@mbb.ki.se

Annual Review of Biochemistry
|June 8, 2006
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Pleiotropic effects of BET inhibition broadly boost tumor immunogenicity to CD8<sup><b>+</b></sup> T cells.

Oncoimmunology·2026
Same author

Correction to "Intracellular Binding of Novel Fluorinated Compounds to Carbonic Anhydrase Isoforms Explored by In-Cell <sup>19</sup>F NMR".

Journal of medicinal chemistry·2025
Same author

Intracellular Binding of Novel Fluorinated Compounds to Carbonic Anhydrase Isoforms Explored by In-Cell <sup>19</sup>F NMR.

Journal of medicinal chemistry·2025
Same author

VHL restoration in clear cell renal cell carcinoma improves NK cell infiltration and function.

Cancer immunology, immunotherapy : CII·2025
Same author

MS CETSA deep functional proteomics uncovers DNA repair programs leading to gemcitabine resistance.

Nature communications·2025
Same author

Hybrid Model Design For Protein Function Prediction.

Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual International Conference·2025
Same journal

Lactate as a Chemical Modification on Proteins and Metabolites.

Annual review of biochemistry·2026
Same journal

Nucleocytoplasmic Transport.

Annual review of biochemistry·2026
Same journal

Packaging of Single-Stranded RNA in Viruses and Virus-Like Particles.

Annual review of biochemistry·2026
Same journal

Shaping of the Infant Gut Microbiome by Milk Oligosaccharides.

Annual review of biochemistry·2026
Same journal

Proteostasis Deregulation by Metabolism Drives the Hallmarks of Cancer.

Annual review of biochemistry·2026
Same journal

JoAnne Stubbe's Radical Path: A Story of Passion, Curiosity, and Persistence.

Annual review of biochemistry·2026
See all related articles

Ribonucleotide reductases (RNRs) are crucial enzymes that convert RNA to DNA building blocks. This review highlights how RNR regulation at molecular and cellular levels ensures proper DNA synthesis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Ribonucleotide reductases (RNRs) are essential enzymes for DNA synthesis.
  • RNRs catalyze the conversion of ribonucleotides to deoxyribonucleotides, a critical step for DNA replication and repair.
  • Three distinct classes of RNRs exist, each utilizing unique mechanisms for radical generation.

Purpose of the Study:

  • To review the regulation of Ribonucleotide reductases (RNRs) at molecular and cellular levels.
  • To elucidate the mechanisms of RNR allosteric regulation by nucleoside triphosphates.
  • To explore the structural similarities and evolutionary origins of the three RNR classes.

Main Methods:

  • Review of recent structural studies on RNRs from all three classes.

Related Experiment Videos

  • Analysis of molecular and cellular regulatory mechanisms.
  • Examination of allosteric regulation by nucleoside triphosphates.

    • Main Results:

    • Structural studies have deepened the understanding of RNR catalytic mechanisms and allosteric regulation.
    • Nucleotide binding induces conformational changes that regulate substrate specificity.
    • Complex interplay of gene activation, enzyme inhibition, and protein degradation controls RNR activity.

    Conclusions:

    • RNR regulation is intricate, involving allosteric effects, gene control, and protein turnover.
    • Appropriate deoxynucleotide levels for DNA replication and repair are maintained through precise RNR regulation.
    • Despite sequence diversity, conserved structural features suggest a common evolutionary origin for RNR classes.