RAD27 multifunctional nuclease RAD27 [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: RAD27
Official Full Name: multifunctional nuclease RAD27
Primary source: SGD:S000001596
Locus tag: YKL113C
See related: AllianceGenome:SGD:S000001596; FungiDB:YKL113C; VEuPathDB:YKL113C
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: ERC11; FEN1; RTH1
Summary: Enables 5'-3' exonuclease activity and 5'-flap endonuclease activity. Involved in DNA metabolic process. Located in cytosol and mitochondrion. Is active in nucleus. Used to study cancer. Orthologous to human FEN1 (flap structure-specific endonuclease 1). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

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See RAD27 in Genome Data Viewer

Location:: chromosome: XI

Exon count:: 1

Sequence:: Chromosome: XI; NC_001143.9 (224727..225875, complement)

Chromosome XI - NC_001143.9 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001143.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Flap endonuclease Rad27 cleaves the RNA of R-loop structures to suppress telomere recombination.
Title: Flap endonuclease Rad27 cleaves the RNA of R-loop structures to suppress telomere recombination.
Rad27 and Exo1 function in different excision pathways for mismatch repair in Saccharomyces cerevisiae.
Title: Rad27 and Exo1 function in different excision pathways for mismatch repair in Saccharomyces cerevisiae.
Cross-Species Complementation of Nonessential Yeast Genes Establishes Platforms for Testing Inhibitors of Human Proteins.
Title: Cross-Species Complementation of Nonessential Yeast Genes Establishes Platforms for Testing Inhibitors of Human Proteins.
By conditionally depleting lagging-strand nucleases and directly analyzing Okazaki fragments synthesized in vivo in Saccharomyces cerevisiae, we conduct a systematic evaluation of the impact of Rad27, Dna2 and Exo1 on lagging-strand synthesis. We find that Rad27 processes the majority of lagging-strand flaps, with a significant additional contribution from Exo1 but not from Dna2.
Title: Processing of eukaryotic Okazaki fragments by redundant nucleases can be uncoupled from ongoing DNA replication in vivo.
Overexpression of RAD27 impairs DNA replication leading to S phase delay, DNA damage and mutation in a manner that is dependent on its interaction with PCNA.
Title: Flap endonuclease overexpression drives genome instability and DNA damage hypersensitivity in a PCNA-dependent manner.
Data show that unlike short-flap substrates, which are bound, bent and cleaved within the first encounter between Flap Endonuclease 1 (FEN1) and DNA, long-flap substrates can escape cleavage even after DNA binding and bending.
Title: Missed cleavage opportunities by FEN1 lead to Okazaki fragment maturation via the long-flap pathway.
Rad2 and rad27 overexpression increases genomic instability in yeast. Rad2 and Rad27 causes DNA breaks that are processed by different repair functions.
Title: Differential effect of the overexpression of Rad2/XPG family endonucleases on genome integrity in yeast and human cells.
Data show that wild-type Rad27 proteins are more stably associated with chromatin than tailless Rad27.
Title: Physical and functional interactions between nucleosomes and Rad27, a critical component of DNA processing during DNA metabolism.
our findings underscore the importance of Rad27p in the maintenance of mtDNA, and demonstrate that it participates in multiple DNA repair pathways in mitochondria, unlinked to nuclear phenotypes.
Title: Roles for the Rad27 Flap Endonuclease in Mitochondrial Mutagenesis and Double-Strand Break Repair in Saccharomyces cerevisiae.
findings indicate that the N-terminal region of Mus81 acts as a landing pad to interact with Rad27 and that Mus81 and Rad27 work conjointly for efficient removal of various aberrant DNA structures
Title: A physiological significance of the functional interaction between Mus81 and Rad27 in homologous recombination repair.

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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

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables 5'-3' exonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables 5'-3' exonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables 5'-3' exonuclease activity	IEA Inferred from Electronic Annotation more info
enables 5'-flap endonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables 5'-flap endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables 5'-flap endonuclease activity	IEA Inferred from Electronic Annotation more info
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA nuclease activity	IEA Inferred from Electronic Annotation more info
enables endonuclease activity	IEA Inferred from Electronic Annotation more info
enables exonuclease activity	IEA Inferred from Electronic Annotation more info
enables magnesium ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nuclease activity	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in DNA replication, removal of RNA primer	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA replication, removal of RNA primer	IEA Inferred from Electronic Annotation more info
involved_in base-excision repair	IEA Inferred from Electronic Annotation more info
involved_in double-strand break repair via nonhomologous end joining	IDA Inferred from Direct Assay more info	PubMed
involved_in gene conversion at mating-type locus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in maintenance of DNA trinucleotide repeats	IGI Inferred from Genetic Interaction more info	PubMed
involved_in maintenance of DNA trinucleotide repeats	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IEA Inferred from Electronic Annotation more info
located_in nucleolus	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleus	HDA more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
is_active_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: multifunctional nuclease RAD27

NP_012809.1

5' to 3' exonuclease, 5' flap endonuclease; required for Okazaki fragment processing and maturation, for long-patch base-excision repair and large loop repair (LLR), ribonucleotide excision repair; cleaves off RNA flap in a RNA:DNA hybrid intermediate during processing of DNA lagging strand; relocalizes to the cytosol in response to hypoxia; member of the S. pombe RAD2/FEN1 family

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_001143.9 Reference assembly

Range

224727..225875 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001179679.1 → NP_012809.1 TPA: multifunctional nuclease RAD27 [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_012809.1

Status: REVIEWED

UniProtKB/Swiss-Prot

A6ZZK4, B3LQY3, C7GVJ8, C8ZC62, D6VXH5, P26793

UniProtKB/TrEMBL

G2WHS1, N1P312

Conserved Domains (1) summary

PTZ00217
Location:1 → 364

PTZ00217; flap endonuclease-1; Provisional