Evidence map›Paper›PMID 9315671›Full record

ArticleMolecular and cellular biology1997

Rnr4p, a novel ribonucleotide reductase small-subunit protein.

P J Wang, A Chabes, R Casagrande, X C Tian, L Thelander, T C Huffaker

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

59 citing papers in PubMed, 120 citations in OpenAlex.

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  9. Genes · 2021
    Review
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  11. Ribonucleotides incorporated by the yeast mitochondrial DNA polymerase are not repaired.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. 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 · 2017
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

P J WangSection of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA.
A Chabes
R Casagrande
X C Tian
L Thelander
T C Huffaker
Cornell University · USUmeå University · SE

Funding

MOLECULAR ANALYSIS OF MICROTUBULE FUNCTION IN YEASTR01GM040479 · NIGMS · CORNELL UNIVERSITY ITHACA · PI HUFFAKER, TIM C · 1988 to 2010
$2.6M
NIGMS NIH HHS GM40479NIGMS NIH HHS R01 GM040479
6 · The paper itself

Abstract

Ribonucleotide reductases catalyze the formation of deoxyribonucleotides by the reduction of the corresponding ribonucleotides. Eukaryotic ribonucleotide reductases are alpha2beta2 tetramers; each of the larger, alpha subunits possesses binding sites for substrate and allosteric effectors, and each of the smaller, beta subunits contains a binuclear iron complex. The iron complex interacts with a specific tyrosine residue to form a tyrosyl free radical which is essential for activity. Previous work has identified two genes in the yeast Saccharomyces cerevisiae, RNR1 and RNR3, that encode alpha subunits and one gene, RNR2, that encodes a beta subunit. Here we report the identification of a second gene from this yeast, RNR4, that encodes a protein with significant similarity to the beta-subunit proteins. The phenotype of rnr4 mutants is consistent with that expected for a defect in ribonucleotide reductase; rnr4 mutants are supersensitive to the ribonucleotide reductase inhibitor hydroxyurea and display an S-phase arrest at their restrictive temperature. rnr4 mutant extracts are deficient in ribonucleotide reductase activity, and this deficiency can be remedied by the addition of exogenous Rnr4p. As is the case for the other RNR genes, RNR4 is induced by agents that damage DNA. However, Rnr4p lacks a number of sequence elements thought to be essential for iron binding, and mutation of the critical tyrosine residue does not affect Rnr4p function. These results suggest that Rnr4p is catalytically inactive but, nonetheless, does play a role in the ribonucleotide reductase complex.

Indexed as

Amino Acid SequenceCloning, MolecularCold TemperatureEnzyme InhibitorsGene DosageGene Expression Regulation, FungalGenes, FungalHydroxyureaMethyl MethanesulfonateMolecular Sequence DataMutagensMutationPhenotypeRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesRNA, FungalEnzyme InhibitorsHydroxyureaMethyl MethanesulfonateMutagensRibonucleoside Diphosphate ReductaseRibonucleotide ReductasesRNA, FungalRNA, MessengerRnr4 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID9315671
PMCPMC232461
OpenAlexW2143472729

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.