MUS81_SCHPO
ID MUS81_SCHPO Reviewed; 608 AA.
AC P87231; Q2EEM1;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Crossover junction endonuclease mus81;
DE EC=3.1.22.-;
GN Name=mus81; ORFNames=SPCC4G3.05c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH CDS1, AND PHOSPHORYLATION.
RX PubMed=11073977; DOI=10.1128/mcb.20.23.8758-8766.2000;
RA Boddy M.N., Lopez-Girona A., Shanahan P., Interthal H., Heyer W.-D.,
RA Russell P.;
RT "Damage tolerance protein Mus81 associates with the FHA1 domain of
RT checkpoint kinase Cds1.";
RL Mol. Cell. Biol. 20:8758-8766(2000).
RN [3]
RP FUNCTION, COFACTOR, INTERACTION WITH EME1, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 395-ASP-ASP-396.
RX PubMed=11719193; DOI=10.1016/s0092-8674(01)00536-0;
RA Boddy M.N., Gaillard P.-H.L., McDonald W.H., Shanahan P., Yates J.R. III,
RA Russell P.;
RT "Mus81-Eme1 are essential components of a Holliday junction resolvase.";
RL Cell 107:537-548(2001).
RN [4]
RP FUNCTION, AND INTERACTION WITH EME1.
RX PubMed=12084712; DOI=10.1074/jbc.m202120200;
RA Doe C.L., Ahn J.S., Dixon J., Whitby M.C.;
RT "Mus81-Eme1 and Rqh1 involvement in processing stalled and collapsed
RT replication forks.";
RL J. Biol. Chem. 277:32753-32759(2002).
RN [5]
RP FUNCTION.
RX PubMed=14704204; DOI=10.1093/genetics/165.4.2289;
RA Smith G.R., Boddy M.N., Shanahan P., Russell P.;
RT "Fission yeast Mus81.Eme1 Holliday junction resolvase is required for
RT meiotic crossing over but not for gene conversion.";
RL Genetics 165:2289-2293(2003).
RN [6]
RP FUNCTION.
RX PubMed=12473680; DOI=10.1074/jbc.m210006200;
RA Whitby M.C., Osman F., Dixon J.;
RT "Cleavage of model replication forks by fission yeast Mus81-Eme1 and
RT budding yeast Mus81-Mms4.";
RL J. Biol. Chem. 278:6928-6935(2003).
RN [7]
RP FUNCTION, AND CHARACTERIZATION OF MUTANT 395-ALA-ALA-396.
RX PubMed=14527419; DOI=10.1016/s1097-2765(03)00342-3;
RA Gaillard P.-H.L., Noguchi E., Shanahan P., Russell P.;
RT "The endogenous Mus81-Eme1 complex resolves Holliday junctions by a nick
RT and counternick mechanism.";
RL Mol. Cell 12:747-759(2003).
RN [8]
RP FUNCTION.
RX PubMed=14527420; DOI=10.1016/s1097-2765(03)00343-5;
RA Osman F., Dixon J., Doe C.L., Whitby M.C.;
RT "Generating crossovers by resolution of nicked Holliday junctions: a role
RT for Mus81-Eme1 in meiosis.";
RL Mol. Cell 12:761-774(2003).
RN [9]
RP FUNCTION.
RX PubMed=15486206; DOI=10.1093/nar/gkh853;
RA Doe C.L., Osman F., Dixon J., Whitby M.C.;
RT "DNA repair by a Rad22-Mus81-dependent pathway that is independent of
RT Rhp51.";
RL Nucleic Acids Res. 32:5570-5581(2004).
RN [10]
RP FUNCTION, INTERACTION WITH CDS1, ASSOCIATION WITH CHROMATIN,
RP PHOSPHORYLATION, MUTAGENESIS OF THR-275, AND CHARACTERIZATION OF MUTANT
RP 395-ALA-ALA-396.
RX PubMed=15805465; DOI=10.1101/gad.1304305;
RA Kai M., Boddy M.N., Russell P., Wang T.S.-F.;
RT "Replication checkpoint kinase Cds1 regulates Mus81 to preserve genome
RT integrity during replication stress.";
RL Genes Dev. 19:919-932(2005).
CC -!- FUNCTION: Interacts with eme1 to form a DNA structure-specific
CC endonuclease with substrate preference for branched DNA structures with
CC a 5'-end at the branch nick. Typical substrates include 3'-flap
CC structures, D-loops, replication forks and nicked Holliday junctions.
CC May be required in mitosis for the processing of stalled or collapsed
CC replication fork intermediates. May be required in meiosis for the
CC repair of meiosis-specific double strand breaks subsequent to single-
CC end invasion (SEI). {ECO:0000269|PubMed:11073977,
CC ECO:0000269|PubMed:11719193, ECO:0000269|PubMed:12084712,
CC ECO:0000269|PubMed:12473680, ECO:0000269|PubMed:14527419,
CC ECO:0000269|PubMed:14527420, ECO:0000269|PubMed:14704204,
CC ECO:0000269|PubMed:15486206, ECO:0000269|PubMed:15805465}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11719193};
CC -!- SUBUNIT: Interacts with eme1. Associates with chromatin. Interacts with
CC the FHA domain of cds1, and this may require prior phosphorylation of
CC Thr-275. {ECO:0000269|PubMed:11073977, ECO:0000269|PubMed:11719193,
CC ECO:0000269|PubMed:12084712, ECO:0000269|PubMed:15805465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11719193}.
CC -!- PTM: Phosphorylated in a cds1-dependent manner in response to
CC hydroxyurea (HU) treatment. This phosphorylation promotes dissociation
CC of mus81 from chromatin which may prevent cleavage of intact stalled
CC replication forks. {ECO:0000269|PubMed:11073977,
CC ECO:0000269|PubMed:15805465}.
CC -!- MISCELLANEOUS: S.pombe appears to be critically dependent on the mus81-
CC eme1 endonuclease for the resolution of meiotic crossovers. This may be
CC due to the absence of an alternate pathway for crossover resolution
CC such as the MSH4-MSH5 pathway which exists in S.cerevisiae and other
CC eukaryotes.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
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DR EMBL; CU329672; CAJ77393.1; -; Genomic_DNA.
DR PIR; T41371; T41371.
DR RefSeq; XP_001713161.1; XM_001713109.1.
DR AlphaFoldDB; P87231; -.
DR SMR; P87231; -.
DR BioGRID; 275578; 57.
DR IntAct; P87231; 1.
DR MINT; P87231; -.
DR STRING; 4896.SPCC4G3.05c.1; -.
DR iPTMnet; P87231; -.
DR PaxDb; P87231; -.
DR EnsemblFungi; SPCC4G3.05c.1; SPCC4G3.05c.1:pep; SPCC4G3.05c.
DR PomBase; SPCC4G3.05c; mus81.
DR VEuPathDB; FungiDB:SPCC4G3.05c; -.
DR eggNOG; KOG2379; Eukaryota.
DR HOGENOM; CLU_014329_1_0_1; -.
DR InParanoid; P87231; -.
DR OMA; WIKEWLD; -.
DR PhylomeDB; P87231; -.
DR Reactome; R-SPO-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR PRO; PR:P87231; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0048257; F:3'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:PomBase.
DR GO; GO:0006302; P:double-strand break repair; IMP:PomBase.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0000709; P:meiotic joint molecule formation; TAS:PomBase.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; IMP:PomBase.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IMP:PomBase.
DR GO; GO:0006301; P:postreplication repair; TAS:PomBase.
DR GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IDA:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 1.10.150.670; -; 1.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR042530; EME1/EME2_C.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR033309; Mus81.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR13451; PTHR13451; 1.
DR Pfam; PF02732; ERCC4; 1.
DR SMART; SM00891; ERCC4; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Endonuclease; Hydrolase;
KW Magnesium; Meiosis; Metal-binding; Nuclease; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..608
FT /note="Crossover junction endonuclease mus81"
FT /id="PRO_0000198860"
FT DOMAIN 331..429
FT /note="ERCC4"
FT REGION 82..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..303
FT /note="Interaction with cds1"
FT COMPBIAS 82..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 275
FT /note="T->A: In allele mus81.T239A; abrogates
FT phosphorylation in response to hydroxyurea and abolishes
FT interaction with cds1."
FT /evidence="ECO:0000269|PubMed:15805465"
FT MUTAGEN 395..396
FT /note="DD->AA: In allele mus81-DD; abrogates endonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:11719193"
SQ SEQUENCE 608 AA; 69044 MW; 481EBE3846931732 CRC64;
MDCGNPLFLQ WIQEWMEEST RRFPKSYQTW RKAYDSMKSC PITFHRPSQA LALKGIGPTI
CAKLEKKWNA YCLENNIPIS THNEQNDSHV NANKSSSETS SEKPRSVKKP TTRKRKVYVP
SYRSGAYSIL CALYMLNKHE FATKPQIVTM AQPYCDSSFG SATDRNMRYT AWSAMKTLIT
KNLVYQTGHP SKYCLTDDGE EVCIRLAKVD DSFQRKHTVS NFSVSKSDDH DSSLCQPPNF
VTSINKAGSS SDHGGELHVT YCPVDHNEVS DGVETDIDVD QVDSLTGIHD HHIINNEQLI
DLTEQEKKQP NESNLSNLKI ETVLFSNCTV FLLIDTREIR SPLDRNLIID KLTNDFGVNC
QVRSLELGDA LWVARDMESG QEVVLDFVVE RKRYDDLVAS IKDGRFHEQK ARLKKSGIRS
VTYILEESSY DESFTESIRT AVSNTQVDQL FHVRHTRSLE HSVSLLAEMT KQINLFYEKR
KTLAVIPDLS IEAKTYESLR EQLLKIDPST PYHISYHAFS SVLSKSSTLT VGDIFIRMLM
TIKGISASKA IEIQKKYPTF MHLFEAYEKS SSSQERNLLL NKTCQGYGFQ TIGPALSAKV
ASVFFPES
