MMS4 Mms4p [Saccharomyces cerevisiae S288C] - Gene

Summary

Go to the top of the page Help

Official Symbol: MMS4
Official Full Name: Mms4p
Primary source: SGD:S000000302
Locus tag: YBR098W
See related: AllianceGenome:SGD:S000000302; FungiDB:YBR098W; VEuPathDB:YBR098W
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: SLX2; YBR100W
Summary: Contributes to crossover junction endodeoxyribonuclease activity. Involved in DNA metabolic process and regulation of reciprocal meiotic recombination. Part of Holliday junction resolvase complex. Orthologous to human EME1 (essential meiotic structure-specific endonuclease 1). [provided by Alliance of Genome Resources, Apr 2022]
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

See MMS4 in Genome Data Viewer

Location:: chromosome: II

Exon count:: 1

Sequence:: Chromosome: II; NC_001134.8 (441515..443590)

Chromosome II - NC_001134.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_001134.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

The cruciform DNA-binding protein Crp1 stimulates the endonuclease activity of Mus81-Mms4 in Saccharomyces cerevisiae.
Title: The cruciform DNA-binding protein Crp1 stimulates the endonuclease activity of Mus81-Mms4 in Saccharomyces cerevisiae.
Mus81-Mms4 endonuclease is an Esc2-STUbL-Cullin8 mitotic substrate impacting on genome integrity.
Title: Mus81-Mms4 endonuclease is an Esc2-STUbL-Cullin8 mitotic substrate impacting on genome integrity.
Study presents evidence that yeast Mus81-Mms4 endonuclease contributes to cell viability in the absence of functional telomerase. This involvement is not through recombination-mediated telomere lengthening as proposed in humans, but rather through an indirect role involving replication stress.
Title: Saccharomyces cerevisiae Mus81-Mms4 prevents accelerated senescence in telomerase-deficient cells.
These results strongly support the notion that Rad52 and Mus81-Mms4 collaborate and work jointly in processing of homologous recombination intermediates.
Title: Saccharomyces cerevisiae Mus81-Mms4 and Rad52 can cooperate in the resolution of recombination intermediates.
Identification of new interacting partners and modulators of Mus81-Mms4 nuclease, RFC, and PCNA imply the cooperation of these factors in resolution of stalled replication forks and branched DNA structures emanating from the restarted replication forks under conditions of replication stress.
Title: Role of PCNA and RFC in promoting Mus81-complex activity.
The scaffold protein Rtt107, which binds the Mus81-Mms4 complex, interacts with Cdc7 and thereby targets Cdc7-Dbf4 and Cdc5 to the complex enabling full Mus81 activation.
Title: Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis.
Our data suggest that Srs2 and Mus81-Mms4 have critical roles in preventing the formation of (or in resolving) toxic inter-homolog joint molecules, which could otherwise interfere with chromosome segregation and lead to genetic instability.
Title: Srs2 and Mus81-Mms4 Prevent Accumulation of Toxic Inter-Homolog Recombination Intermediates.
The role of Mms4 in crossover formation during meiotic recombinational repair
Title: Controlling meiotic recombinational repair - specifying the roles of ZMMs, Sgs1 and Mus81/Mms4 in crossover formation.
Unresolved recombination intermediates are a source of mitotic sister chromatid bridges, and Mus81-Mms4 and Yen1 play a central role in their resolution in vivo.
Title: Mus81-Mms4 and Yen1 resolve a novel anaphase bridge formed by noncanonical Holliday junctions.
data point to a coordinated role of Mus81-Mms4 and Srs2 in processing of recombination as well as replication intermediates
Title: Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates.

Submit: New GeneRIF Correction See all GeneRIFs (19)

Pathways from PubChem

Go to the top of the page

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables DNA binding	IEA Inferred from Electronic Annotation more info
contributes_to DNA endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
contributes_to crossover junction DNA endonuclease activity	IBA Inferred from Biological aspect of Ancestor more info
contributes_to crossover junction DNA endonuclease activity	IDA Inferred from Direct Assay more info	PubMed
enables endonuclease activity	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 damage response	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in DNA recombination	IEA Inferred from Electronic Annotation more info
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 DNA topological change	IGI Inferred from Genetic Interaction more info	PubMed
involved_in double-strand break repair	IBA Inferred from Biological aspect of Ancestor more info
involved_in meiotic cell cycle	IEA Inferred from Electronic Annotation more info
involved_in mitotic intra-S DNA damage checkpoint signaling	IBA Inferred from Biological aspect of Ancestor more info
involved_in reciprocal meiotic recombination	IGI Inferred from Genetic Interaction more info	PubMed
involved_in reciprocal meiotic recombination	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in regulation of reciprocal meiotic recombination	IGI Inferred from Genetic Interaction more info	PubMed
involved_in replication fork processing	IBA Inferred from Biological aspect of Ancestor more info
involved_in resolution of meiotic recombination intermediates	IBA Inferred from Biological aspect of Ancestor more info
involved_in resolution of meiotic recombination intermediates	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
part_of Holliday junction resolvase complex	IBA Inferred from Biological aspect of Ancestor more info
part_of Holliday junction resolvase complex	IDA Inferred from Direct Assay more info	PubMed
part_of Holliday junction resolvase complex	IEA Inferred from Electronic Annotation more info
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: Mms4p

NP_009656.2

Subunit of structure-specific Mms4p-Mus81p endonuclease; cleaves branched DNA; involved in recombination, DNA repair, and joint molecule formation/resolution during meiotic recombination; phosphorylation of the non-catalytic subunit Mms4p by Cdc28p and Cdc5p during mitotic cell cycle activates the function of Mms4p-Mus81p

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

Genome Annotation

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

Reference assembly

Genomic

NC_001134.8 Reference assembly

Range

441515..443590

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001178446.1 → NP_009656.2 TPA: Mms4p [Saccharomyces cerevisiae S288C]

See identical proteins and their annotated locations for NP_009656.2

Status: REVIEWED

UniProtKB/Swiss-Prot

D6VQ99, P38257, P38259, Q6B1Z9, Q9URQ2

UniProtKB/TrEMBL

D3UEJ3, G2W9A5, N1P9F9

Conserved Domains (1) summary

cd20080
Location:397 → 599

XPF_nuclease_EME-like; XPF-like nuclease domain of the family of Essential Meiotic Endonucleases (EMEs) and similar proteins