ArticleProceedings of the National Academy of Sciences of the United States of America2006
Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. 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, 46 citations in OpenAlex.
- Identification of different classes of genome instability suppressor genes through analysis of DNA damage response markers.G3 (Bethesda, Md.) · 2024Article
- Tolerance to replication stress requires Dun1p kinase and activation of the electron transport chain.Biochimica et biophysica acta. Molecular cell research · 2023Article
- DNA damage response activates respiration and thereby enlarges dNTP pools to promote cell survival in budding yeast.The Journal of biological chemistry · 2019Article
- Engineered SUMO/protease system identifies Pdr6 as a bidirectional nuclear transport receptor.The Journal of cell biology · 2019Article
- Structural basis for the nuclear import and export functions of the biportin Pdr6/Kap122.The Journal of cell biology · 2019Article
- Clb6-Cdc28 Promotes Ribonucleotide Reductase Subcellular Redistribution during S Phase.Molecular and cellular biology · 2018Article
- Regulation of Small Mitochondrial DNA Replicative Advantage by Ribonucleotide Reductase inG3 (Bethesda, Md.) · 2017Article
- 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
- Identification of TaWD40D, a wheat WD40 repeat-containing protein that is associated with plant tolerance to abiotic stresses.Plant cell reports · 2015Article
- Yeast Dun1 kinase regulates ribonucleotide reductase inhibitor Sml1 in response to iron deficiency.Molecular and cellular biology · 2014Article
- Conserved electron donor complex Dre2-Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Genome-wide single-cell-level screen for protein abundance and localization changes in response to DNA damage in S. cerevisiae.Nucleic acids research · 2013Article
- Regulation of ribonucleotide reductase during iron limitation.Molecular cell · 2011Article
- Regulation of ribonucleotide reductase in response to iron deficiency.Molecular cell · 2011Article
- Targeting the Large Subunit of Human Ribonucleotide Reductase for Cancer Chemotherapy.Pharmaceuticals (Basel, Switzerland) · 2011Article
- Nuclear import by karyopherin-βs: recognition and inhibition.Biochimica et biophysica acta · 2011Review
- Ribosome synthesis-unrelated functions of the preribosomal factor Rrp12 in cell cycle progression and the DNA damage response.Molecular and cellular biology · 2011Article
- Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization.Nature structural & molecular biology · 2011Article
- Mechanisms of dNTP supply that play an essential role in maintaining genome integrity in eukaryotic cells.Cancer science · 2010Review
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Ribonucleotide reductase (RNR) catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides and is an essential enzyme for DNA replication and repair. Cells have evolved intricate mechanisms to regulate RNR activity to ensure high fidelity of DNA replication during normal cell-cycle progression and of DNA repair upon genotoxic stress. The RNR holoenzyme is composed of a large subunit R1 (alpha, oligomeric state unknown) and a small subunit R2 (beta(2)). R1 binds substrates and allosteric effectors; R2 contains a diferric-tyrosyl radical [(Fe)(2)-Y.] cofactor that is required for catalysis. In Saccharomyces cerevisiae, R1 is predominantly localized in the cytoplasm, whereas R2, which is a heterodimer (betabeta'), is predominantly in the nucleus. When cells encounter DNA damage or stress during replication, betabeta' is redistributed from the nucleus to the cytoplasm in a checkpoint-dependent manner, resulting in the colocalization of R1 and R2. We have identified two proteins that have an important role in betabeta' nuclear localization: the importin beta homolog Kap122 and the WD40 repeat protein Wtm1. Deletion of either WTM1 or KAP122 leads to loss of betabeta' nuclear localization. Wtm1 and its paralog Wtm2 are both nuclear proteins that are in the same protein complex with betabeta'. Wtm1 also interacts with Kap122 in vivo and requires Kap122 for its nuclear localization. Our results suggest that Wtm1 acts either as an adaptor to facilitate nuclear import of betabeta' by Kap122 or as an anchor to retain betabeta' in the nucleus.
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