RNR1 ribonucleotide-diphosphate reductase subunit RNR1 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: RNR1
Official Full Name: ribonucleotide-diphosphate reductase subunit RNR1
Primary source: SGD:S000000872
Locus tag: YER070W
See related: AllianceGenome:SGD:S000000872; FungiDB:YER070W; VEuPathDB:YER070W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as: CRT7; RIR1; SDS12
Summary: Enables nucleotide binding activity. Contributes to ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor. Involved in deoxyribonucleotide biosynthetic process. Located in cytoplasm. Part of ribonucleoside-diphosphate reductase complex. Human ortholog(s) of this gene implicated in chronic progressive external ophthalmoplegia. Orthologous to human RRM1 (ribonucleotide reductase catalytic subunit M1). [provided by Alliance of Genome Resources, Jul 2025]
Orthologs: all
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Genomic context

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See RNR1 in Genome Data Viewer

Location:: chromosome: V

Exon count:: 1

Sequence:: Chromosome: V; NC_001137.3 (298950..301616)

Chromosome V - NC_001137.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001137.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency.
Title: The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency.
We identified 24 rnr1 mutant alleles resulting in diverse mutator phenotypes linked in most cases to imbalanced dNTPs. Among the identified rnr1 alleles the strongest mutators presented a dNTP imbalance in which three out of the four dNTPs were elevated (dCTP, dTTP and dGTP), particularly if dGTP levels were highly increased.
Title: A genetic screen pinpoints ribonucleotide reductase residues that sustain dNTP homeostasis and specifies a highly mutagenic type of dNTP imbalance.
Fhl1p regulates RNR1 gene transcription to maintain dNTP levels, thus modulating longevity by protection against replication stress
Title: The forkhead-like transcription factor (Fhl1p) maintains yeast replicative lifespan by regulating ribonucleotide reductase 1 (RNR1) gene transcription.
Multiple turnover kinetics show that Sml1 inhibition of dGTP/ADP- and ATP/CDP-bound ScRR follows a mixed inhibition mechanism. However, Sml1 cooperatively binds to the ES complex in the dGTP/ADP form, whereas with ATP/CDP, Sml1 binds weakly and noncooperatively
Title: Inhibition of yeast ribonucleotide reductase by Sml1 depends on the allosteric state of the enzyme.
there is a directed orientation of the RNR beta and beta' C-terminal tails relative to alpha within the holoenzyme consistent with a docking model of the two subunits and argue against RT across the beta beta' interface
Title: 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 data reveaedl that the arginine 293 and glutamine 288 residues of ribonucleotide reductase 1 are crucial in facilitating ADP and CDP substrate selection.
Title: Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase.
defects in autophagy result in an increase in soluble Rnr1 protein levels and a DNA damage phenotype.
Title: Autophagy-dependent regulation of the DNA damage response protein ribonucleotide reductase 1.
Data show that Rnr1 transcription requires protein bound to a particular site and either five different sites or one additional sites.
Title: Reverse engineering the yeast RNR1 transcriptional control system.
x-ray structures upon binding to gemcitabine diphosphate
Title: Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly.
The structures of the apo-, AMPPNP only-, AMPPNP-CDP-, AMPPNP-UDP-, dGTP-ADP- and TTP-GDP-bound complexes give insight into substrate and effector binding and specificity cross-talk.
Title: Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation.

Submit: New GeneRIF Correction See all GeneRIFs (11)

Pathways from PubChem

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

NCBI Orthologs

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables ATP binding	IBA Inferred from Biological aspect of Ancestor more info
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables catalytic activity	IEA Inferred from Electronic Annotation more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables nucleotide binding	IDA Inferred from Direct Assay more info	PubMed
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables oxidoreductase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IBA Inferred from Biological aspect of Ancestor more info
contributes_to ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IDA Inferred from Direct Assay more info	PubMed
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IDA Inferred from Direct Assay more info	PubMed
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IEA Inferred from Electronic Annotation more info
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IMP Inferred from Mutant Phenotype more info	PubMed
enables ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in deoxyribonucleotide biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in deoxyribonucleotide biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in deoxyribonucleotide biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in deoxyribonucleotide biosynthetic process	ISS Inferred from Sequence or Structural Similarity more info

Component	Evidence Code	Pubs
located_in cytoplasm	HDA more info	PubMed
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	IEA Inferred from Electronic Annotation more info
located_in cytoplasm	NAS Non-traceable Author Statement more info	PubMed
located_in nucleus	HDA more info	PubMed
part_of ribonucleoside-diphosphate reductase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonucleoside-diphosphate reductase complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: ribonucleotide-diphosphate reductase subunit RNR1

NP_010993.1

EC 1.17.4.1

Major isoform of large subunit of ribonucleotide-diphosphate reductase; the RNR complex catalyzes rate-limiting step in dNTP synthesis, regulated by DNA replication and DNA damage checkpoint pathways via localization of small subunits; relative distribution to the nucleus increases upon DNA replication stress; RNR1 has a paralog, RNR3, that arose from the whole genome duplication

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_001137.3 Reference assembly

Range

298950..301616

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178961.1 → NP_010993.1 ribonucleotide-diphosphate reductase subunit RNR1

See identical proteins and their annotated locations for NP_010993.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D3DLX5, P21524

UniProtKB/TrEMBL

A6ZR24, B3LRI7, C7GRQ2, C8Z778, N1PA44

Conserved Domains (1) summary

PLN02437
Location:1 → 758

PLN02437; ribonucleoside--diphosphate reductase large subunit