MUS81_ARATH
ID MUS81_ARATH Reviewed; 659 AA.
AC Q5W9E7; A1Z073; O65562;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Crossover junction endonuclease MUS81 {ECO:0000303|PubMed:18182028};
DE EC=3.1.22.-;
DE AltName: Full=Protein MMS AND UV SENSITIVE 81 {ECO:0000303|PubMed:17327258, ECO:0000303|PubMed:18182028};
DE Short=AtMUS81 {ECO:0000303|PubMed:17327258, ECO:0000303|PubMed:18182028};
GN Name=MUS81 {ECO:0000303|PubMed:17327258, ECO:0000303|PubMed:18182028};
GN OrderedLocusNames=At4g30870 {ECO:0000312|Araport:AT4G30870};
GN ORFNames=F6I18.220 {ECO:0000312|EMBL:CAA18206.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17327258; DOI=10.1093/pcp/pcm029;
RA Mimida N., Kitamoto H., Osakabe K., Nakashima M., Ito Y., Heyer W.D.,
RA Toki S., Ichikawa H.;
RT "Two alternatively spliced transcripts generated from OsMUS81, a rice
RT homolog of yeast MUS81, are up-regulated by DNA-damaging treatments.";
RL Plant Cell Physiol. 48:648-654(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18182028; DOI=10.1111/j.1365-313x.2008.03403.x;
RA Higgins J.D., Buckling E.F., Franklin F.C., Jones G.H.;
RT "Expression and functional analysis of AtMUS81 in Arabidopsis meiosis
RT reveals a role in the second pathway of crossing-over.";
RL Plant J. 54:152-162(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP FUNCTION, AND H-H-H MOTIF.
RX PubMed=16945961; DOI=10.1093/nar/gkl576;
RA Hartung F., Suer S., Bergmann T., Puchta H.;
RT "The role of AtMUS81 in DNA repair and its genetic interaction with the
RT helicase AtRecQ4A.";
RL Nucleic Acids Res. 34:4438-4448(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17696612; DOI=10.1371/journal.pgen.0030132;
RA Berchowitz L.E., Francis K.E., Bey A.L., Copenhaver G.P.;
RT "The role of AtMUS81 in interference-insensitive crossovers in A.
RT thaliana.";
RL PLoS Genet. 3:E132-E132(2007).
RN [7]
RP REVIEW.
RX PubMed=17208327; DOI=10.1016/j.tig.2006.12.007;
RA Mezard C., Vignard J., Drouaud J., Mercier R.;
RT "The road to crossovers: plants have their say.";
RL Trends Genet. 23:91-99(2007).
RN [8]
RP FUNCTION, INTERACTION WITH EME1A AND EME1B, MUTAGENESIS OF 470-ASP-ASP-471,
RP AND COFACTOR.
RX PubMed=19339504; DOI=10.1104/pp.109.136846;
RA Geuting V., Kobbe D., Hartung F., Duerr J., Focke M., Puchta H.;
RT "Two distinct MUS81-EME1 complexes from Arabidopsis process Holliday
RT junctions.";
RL Plant Physiol. 150:1062-1071(2009).
RN [9]
RP FUNCTION.
RX PubMed=20971895; DOI=10.1105/tpc.110.078568;
RA Mannuss A., Dukowic-Schulze S., Suer S., Hartung F., Pacher M., Puchta H.;
RT "RAD5A, RECQ4A, and MUS81 have specific functions in homologous
RT recombination and define different pathways of DNA repair in Arabidopsis
RT thaliana.";
RL Plant Cell 22:3318-3330(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26704385; DOI=10.1105/tpc.15.00898;
RA Olivier M., Da Ines O., Amiard S., Serra H., Goubely C., White C.I.,
RA Gallego M.E.;
RT "The structure-specific endonucleases MUS81 and SEND1 are essential for
RT telomere stability in Arabidopsis.";
RL Plant Cell 28:74-86(2016).
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, nicked Holliday junctions and
CC also intact Holliday junctions with a reduced efficiency. May be
CC required in mitosis for the processing of stalled or collapsed
CC replication fork intermediates. Plays a role in DNA repair and in
CC genotoxic stress-induced homologous recombination (HR) in somatic
CC cells. Mediates a subset of meiotic recombination events that are
CC insensitive to crossover interference. Together with SEND1, essential
CC for the resolution of toxic replication structures to ensure genome
CC stability, and to maintain telomere integrity and replication
CC (PubMed:26704385). {ECO:0000269|PubMed:16945961,
CC ECO:0000269|PubMed:17696612, ECO:0000269|PubMed:18182028,
CC ECO:0000269|PubMed:19339504, ECO:0000269|PubMed:20971895,
CC ECO:0000269|PubMed:26704385}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19339504};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19339504};
CC -!- SUBUNIT: Forms a heterodimer with EME1A or EME1B.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18182028}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:18182028}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but preferentially expressed in young
CC flowers buds, notably in anthers. {ECO:0000269|PubMed:17696612,
CC ECO:0000269|PubMed:18182028}.
CC -!- INDUCTION: By DNA-damaging treatments such as MMS, cisplatin and gamma-
CC radiation. {ECO:0000269|PubMed:17696612}.
CC -!- DISRUPTION PHENOTYPE: Sensitive to the mutagens MMS and MMC. Increased
CC sensitivity to gamma radiation. Deficiency in homologous recombination
CC in somatic cells but only after induction by genotoxic stress.
CC Decreased pollen viability with morphologically aberrant (small and
CC misshaped) grain. Moderate reduction in meiotic crossovers. The double
CC mutant mus81 send1 exhibits severe developmental defects (e.g. strong
CC growth retardation and impaired leaf and shoot development), increased
CC endoreduplication, slower cell cycle progression, spontaneous cell
CC death and genome instability associated with a dramatic loss of
CC telomeric repeats (PubMed:26704385). {ECO:0000269|PubMed:17696612,
CC ECO:0000269|PubMed:18182028, ECO:0000269|PubMed:26704385}.
CC -!- MISCELLANEOUS: Two distinct classes of crossovers have been
CC demonstrated in Arabidopsis. Class I is MSH4 dependent and exhibits
CC crossover interference. Class II is MUS81 dependent and exhibits no
CC interference.
CC -!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABL98212.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA18206.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB177892; BAD66696.1; -; mRNA.
DR EMBL; EF154086; ABL98212.1; ALT_FRAME; mRNA.
DR EMBL; AL022198; CAA18206.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161577; CAB79805.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85822.1; -; Genomic_DNA.
DR PIR; D85361; D85361.
DR RefSeq; NP_194816.2; NM_119234.4.
DR AlphaFoldDB; Q5W9E7; -.
DR SMR; Q5W9E7; -.
DR BioGRID; 14498; 1.
DR STRING; 3702.AT4G30870.1; -.
DR PaxDb; Q5W9E7; -.
DR PRIDE; Q5W9E7; -.
DR ProteomicsDB; 251021; -.
DR EnsemblPlants; AT4G30870.1; AT4G30870.1; AT4G30870.
DR GeneID; 829211; -.
DR Gramene; AT4G30870.1; AT4G30870.1; AT4G30870.
DR KEGG; ath:AT4G30870; -.
DR Araport; AT4G30870; -.
DR TAIR; locus:2126729; AT4G30870.
DR eggNOG; KOG2379; Eukaryota.
DR HOGENOM; CLU_014329_2_0_1; -.
DR InParanoid; Q5W9E7; -.
DR OMA; RTADNCA; -.
DR OrthoDB; 738810at2759; -.
DR PhylomeDB; Q5W9E7; -.
DR PRO; PR:Q5W9E7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q5W9E7; baseline and differential.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:TAIR.
DR GO; GO:0048476; C:Holliday junction resolvase complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048257; F:3'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
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:TAIR.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IGI:TAIR.
DR GO; GO:0031573; P:mitotic intra-S DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006312; P:mitotic recombination; IMP:TAIR.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.150.670; -; 1.
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; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Endonuclease; Hydrolase; Magnesium; Meiosis;
KW Metal-binding; Mitosis; Nuclease; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..659
FT /note="Crossover junction endonuclease MUS81"
FT /id="PRO_0000418424"
FT DOMAIN 404..503
FT /note="ERCC4"
FT MOTIF 59..78
FT /note="Helix-hairpin-helix motif 1"
FT MOTIF 585..622
FT /note="Helix-hairpin-helix motif 2"
FT MUTAGEN 470..471
FT /note="DD->AA: Able to form heterodimer with EME1A or EME1B
FT but without any endonucleolytic activity."
FT /evidence="ECO:0000269|PubMed:19339504"
SQ SEQUENCE 659 AA; 74056 MW; D073C0B1137255C4 CRC64;
MDDERRVLCP ENRGLAAYVL QKKQEYAEKP KGLSENLERT FVKGYRSVCD AKDPINTLKD
LSQIKGFGKW MVKLMKGYFD TAVESSEQED LPDNRAGKKA NGKKRYIPQR NSVGYALLIT
LHRRTTNGKE FMRKQELIDA ADANGLSHAP VGPEKGKGKA GLGHSKREWY SGWSCMTTLI
QKGLVVKSSN PAKYMLTVEG REVANECILR SGLPDSVDIL SVDEMDPTPQ AKKTPNQNPT
CSFTMREELP YVDPRCRAQS AIPSDILEKF TPFGYSKEQV VAAFREVSDG SGDKDPSTLW
LSVMCHLRQA EVYNSCPDSR NSKKDSSGPF KSQIRQVDLE GSRAKKFRSC NDGSTLNPCS
SGSSHAVKAC SSSLASDGTK GITNIPRLPP LQFGETFEEA YDVILILDDR EKFATKGSRS
RNIVENICSE FNIKIEVRRL PVGDCIWIAR HKYLETEYVL DFIAERKNVD DMRSSIRDNR
YRDQKLRLQR SGFKKLIYIL EGDPNHSDAA ESIKTACFTT EILEGFDVLR THGLGETLRK
YGYLTKSIYQ YYKLRVNDND QSKGAASCPS FDSFVKRCQD LDKMTISDVF AIQLMQVPQV
TEEIAIAVLD MYPTLLSLAS AYSHLEADVS AQEEMLRNRS NNVICASASK NIFKLVWGE
