ArticleProceedings of the National Academy of Sciences of the United States of America2000
Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 94 citations in OpenAlex.
- The C-terminal domain of Hsp70 is responsible for paralog-specific regulation of ribonucleotide reductase.PLoS genetics · 2022Article
- Review
- Enhanced production of poly(3-hydroxybutyrate-co-3-hydroxyvalerate) biopolymer by recombinant Bacillus megaterium in fed-batch bioreactors.Bioprocess and biosystems engineering · 2021Article
- Mechanistic insights on the mode of action of an antiproliferative thiosemicarbazone-nickel complex revealed by an integrated chemogenomic profiling study.Scientific reports · 2020Article
- Class Id ribonucleotide reductase utilizes a MnJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Functional link between mitochondria and Rnr3, the minor catalytic subunit of yeast ribonucleotide reductase.Microbial cell (Graz, Austria) · 2019Article
- Novel insights into molecular chaperone regulation of ribonucleotide reductase.Current genetics · 2019Review
- The Hsp70 co-chaperone Ydj1/HDJ2 regulates ribonucleotide reductase activity.PLoS genetics · 2018Article
- Unique molecular mechanisms for maintenance and alteration of genetic information in the budding yeastGenes and environment : the official journal of the Japanese Environmental Mutagen Society · 2017Review
- Inhibition of yeast ribonucleotide reductase by Sml1 depends on the allosteric state of the enzyme.FEBS letters · 2016Article
- Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Small Subunit Localization in Response to Iron Deficiency.The Journal of biological chemistry · 2016Article
- dNTP pool levels modulate mutator phenotypes of error-prone DNA polymerase ε variants.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Checkpoint-dependent RNR induction promotes fork restart after replicative stress.Scientific reports · 2015Article
- White spot syndrome virus protein kinase 1 defeats the host cell's iron-withholding defense mechanism by interacting with host ferritin.Journal of virology · 2015Article
- Quantitative proteomics of the yeast Hsp70/Hsp90 interactomes during DNA damage reveal chaperone-dependent regulation of ribonucleotide reductase.Journal of proteomics · 2015Article
- Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit.Nucleic acids research · 2014Article
- Choosing the right metal: case studies of class I ribonucleotide reductases.The Journal of biological chemistry · 2014Review
- Telomere length kinetics assay (TELKA) sorts the telomere length maintenance (tlm) mutants into functional groups.Nucleic acids research · 2014Article
- The conserved Lys-95 charged residue cluster is critical for the homodimerization and enzyme activity of human ribonucleotide reductase small subunit M2.The Journal of biological chemistry · 2014Article
- Investigation of in vivo roles of the C-terminal tails of the small subunit (ββ') of Saccharomyces cerevisiae ribonucleotide reductase: contribution to cofactor formation and intersubunit association within the active holoenzyme.The Journal of biological chemistry · 2013Article
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7 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Ribonucleotide reductase (RNR) catalyzes the de novo synthesis of deoxyribonucleotides. Eukaryotes have an alpha(2)beta(2) form of RNR consisting of two homodimeric subunits, proteins R1 (alpha(2)) and R2 (beta(2)). The R1 protein is the business end of the enzyme containing the active site and the binding sites for allosteric effectors. The R2 protein is a radical storage device containing an iron center-generated tyrosyl free radical. Previous work has identified an RNR protein in yeast, Rnr4p, which is homologous to other R2 proteins but lacks a number of conserved amino acid residues involved in iron binding. Using highly purified recombinant yeast RNR proteins, we demonstrate that the crucial role of Rnr4p (beta') is to fold correctly and stabilize the radical-storing Rnr2p by forming a stable 1:1 Rnr2p/Rnr4p complex. This complex sediments at 5.6 S as a betabeta' heterodimer in a sucrose gradient. In the presence of Rnr1p, both polypeptides of the Rnr2p/Rnr4p heterodimer cosediment at 9.7 S as expected for an alpha(2)betabeta' heterotetramer, where Rnr4p plays an important role in the interaction between the alpha(2) and the betabeta ' subunits. The specific activity of the Rnr2p complexed with Rnr4p is 2,250 nmol deoxycytidine 5'-diphosphate formed per min per mg, whereas the homodimer of Rnr2p shows no activity. This difference in activity may be a consequence of the different conformations of the inactive homodimeric Rnr2p and the active Rnr4p-bound form, as shown by CD spectroscopy. Taken together, our results show that the Rnr2p/Rnr4p heterodimer is the active form of the yeast RNR small subunit.
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