MRE11 MRX complex nuclease subunit [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: MRE11
Official Full Name: MRX complex nuclease subunit
Primary source: SGD:S000004837
Locus tag: YMR224C
See related: AllianceGenome:SGD:S000004837; FungiDB:YMR224C; VEuPathDB:YMR224C
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: NGS1; RAD58; XRS4
Summary: Enables DNA binding activity; molecular adaptor activity; and nuclease activity. Contributes to adenylate kinase activity. Involved in DNA metabolic process; ascospore formation; and regulation of transcription by RNA polymerase II. Located in nucleus. Part of Mre11 complex. Used to study breast cancer; intestinal cancer; liver cancer; ovarian cancer; and skin cancer. Human ortholog(s) of this gene implicated in several diseases, including Lynch syndrome; ataxia-telangiectasia-like disorder-1; endometrial cancer; gastrointestinal system cancer (multiple); and urinary bladder cancer. Orthologous to human MRE11 (MRE11 homolog, double strand break repair nuclease). [provided by Alliance of Genome Resources, Dec 2024]
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Genomic context

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See MRE11 in Genome Data Viewer

Location:: chromosome: XIII

Exon count:: 1

Sequence:: Chromosome: XIII; NC_001145.3 (718575..720653, complement)

Chromosome XIII - NC_001145.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001145.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Physical interaction with Spo11 mediates the localisation of Mre11 to chromatin in meiosis and promotes its nuclease activity.
Title: Physical interaction with Spo11 mediates the localisation of Mre11 to chromatin in meiosis and promotes its nuclease activity.
Xrs2/NBS1 promote end-bridging activity of the MRE11-RAD50 complex.
Title: Xrs2/NBS1 promote end-bridging activity of the MRE11-RAD50 complex.
Yeast-based screening of cancer mutations in the DNA damage response protein Mre11 demonstrates importance of conserved capping domain residues.
Title: Yeast-based screening of cancer mutations in the DNA damage response protein Mre11 demonstrates importance of conserved capping domain residues.
The 9-1-1 Complex Controls Mre11 Nuclease and Checkpoint Activation during Short-Range Resection of DNA Double-Strand Breaks.
Title: The 9-1-1 Complex Controls Mre11 Nuclease and Checkpoint Activation during Short-Range Resection of DNA Double-Strand Breaks.
Inhibition of MRN activity by a telomere protein motif.
Title: Inhibition of MRN activity by a telomere protein motif.
A Role for the Mre11-Rad50-Xrs2 Complex in Gene Expression and Chromosome Organization.
Title: A Role for the Mre11-Rad50-Xrs2 Complex in Gene Expression and Chromosome Organization.
Effect of BRCA1 missense variants on gene reversion in DNA double-strand break repair mutants and cell cycle-arrested cells of Saccharomyces cerevisiae.
Title: Effect of BRCA1 missense variants on gene reversion in DNA double-strand break repair mutants and cell cycle-arrested cells of Saccharomyces cerevisiae.
Here we describe two separation-of-functions alleles, mre11-S499P and rad50-A78T, which we show to specifically affect Tel1 activation without impairing MRX functions in DSB repair. Both Mre11-S499P and Rad50-A78T reduce Tel1-MRX interaction leading to poor Tel1 association at DSBs and consequent loss of Tel1 activation
Title: The ATP-bound conformation of the Mre11-Rad50 complex is essential for Tel1/ATM activation.
Data show that ssDNA endodeoxyribonuclease SAE2 (Sae2) cooperates with the Mre11-Rad50-Xrs2 (MRX) complex to initiate resection of DNA double-strand breaks (DSBs) and to maintain the DSB ends in close proximity to allow their repair.
Title: Structurally distinct Mre11 domains mediate MRX functions in resection, end-tethering and DNA damage resistance.
A harmless head-on replication-transcription clash resolution requires the fine-tuning of origin firing and coordination among Sen1, Exo1, Mre11 and Mrc1-Ctf4 complexes.
Title: Dormant origins and fork protection mechanisms rescue sister forks arrested by transcription.

Submit: New GeneRIF Correction See all GeneRIFs (63)

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 3'-5' exonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables 3'-5'-DNA exonuclease activity	IEA Inferred from Electronic Annotation more info
enables DNA endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA endonuclease activity	IEA Inferred from Electronic Annotation more info
enables G-quadruplex DNA binding	IDA Inferred from Direct Assay more info	PubMed
contributes_to adenylate kinase activity	IDA Inferred from Direct Assay more info	PubMed
enables double-stranded telomeric DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables endonuclease activity	IEA Inferred from Electronic Annotation more info
enables exonuclease activity	IEA Inferred from Electronic Annotation more info
enables manganese ion binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables molecular adaptor activity	IGI Inferred from Genetic Interaction more info	PubMed
enables molecular adaptor activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables single-stranded DNA endodeoxyribonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
enables single-stranded telomeric DNA binding	IDA Inferred from Direct Assay more info	PubMed
enables telomeric DNA binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA double-strand break processing involved in repair via synthesis-dependent strand annealing	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in DNA repair	IEA Inferred from Electronic Annotation more info
involved_in DNA repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in ascospore formation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in base-excision repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in double-strand break repair	IEA Inferred from Electronic Annotation more info
involved_in double-strand break repair via break-induced replication	IGI Inferred from Genetic Interaction more info	PubMed
involved_in double-strand break repair via break-induced replication	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in double-strand break repair via homologous recombination	IBA Inferred from Biological aspect of Ancestor more info
involved_in double-strand break repair via nonhomologous end joining	IBA Inferred from Biological aspect of Ancestor more info
involved_in double-strand break repair via nonhomologous end joining	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in maintenance of DNA trinucleotide repeats	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in meiotic DNA double-strand break formation	IBA Inferred from Biological aspect of Ancestor more info
involved_in meiotic cell cycle	IEA Inferred from Electronic Annotation more info
involved_in meiotic cell cycle	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitochondrial double-strand break repair via homologous recombination	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitochondrial double-strand break repair via homologous recombination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mitotic G2 DNA damage checkpoint signaling	IBA Inferred from Biological aspect of Ancestor more info
involved_in mitotic intra-S DNA damage checkpoint signaling	IBA Inferred from Biological aspect of Ancestor more info
involved_in nucleoside monophosphate phosphorylation	IEA Inferred from Electronic Annotation more info
involved_in reciprocal meiotic recombination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of transcription by RNA polymerase II	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in telomere maintenance	IBA Inferred from Biological aspect of Ancestor more info
involved_in telomere maintenance	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
part_of Mre11 complex	IBA Inferred from Biological aspect of Ancestor more info
part_of Mre11 complex	IEA Inferred from Electronic Annotation more info
part_of Mre11 complex	IPI Inferred from Physical Interaction more info	PubMed
located_in chromosome	IEA Inferred from Electronic Annotation more info
located_in chromosome, telomeric region	IEA Inferred from Electronic Annotation more info
located_in mitochondrion	HDA more info	PubMed
located_in nucleus	HDA more info	PubMed
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info
is_active_in site of double-strand break	IBA Inferred from Biological aspect of Ancestor more info

General protein information

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Preferred Names: MRX complex nuclease subunit

NP_013951.1

Nuclease subunit of the MRX complex with Rad50p and Xrs2p; complex functions in repair of DNA double-strand breaks and in telomere stability; Mre11p associates with Ser/Thr-rich ORFs in premeiotic phase; nuclease activity required for MRX function; widely conserved; forms nuclear foci upon DNA replication stress

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_001145.3 Reference assembly

Range

718575..720653 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001182731.1 → NP_013951.1 TPA: MRX complex nuclease subunit [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_013951.1

Status: REVIEWED

UniProtKB/Swiss-Prot

D6W049, P32829, P87289, Q07173

UniProtKB/TrEMBL

G2WKT1, N1NYN0

Conserved Domains (1) summary

TIGR00583
Location:6 → 413

mre11; DNA repair protein (mre11)