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Crossover junction endonuclease MUS81 (EC 3.1.22.-) (MMS and UV-sensitive protein 81)

 MUS81_YEAST             Reviewed;         632 AA.
Q04149; D6VT20;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 147.
RecName: Full=Crossover junction endonuclease MUS81;
EC=3.1.22.-;
AltName: Full=MMS and UV-sensitive protein 81;
Name=MUS81; Synonyms=SLX3; OrderedLocusNames=YDR386W;
ORFNames=D9509.6;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, DNA REPAIR, AND INTERACTION WITH RAD54.
PubMed=10905349; DOI=10.1007/s004380000241;
Interthal H., Heyer W.-D.;
"MUS81 encodes a novel helix-hairpin-helix protein involved in the
response to UV- and methylation-induced DNA damage in Saccharomyces
cerevisiae.";
Mol. Gen. Genet. 263:812-827(2000).
[4]
FUNCTION, PROCESSING OF STALLED REPLICATION FORK, AND INTERACTION WITH
MMS4.
PubMed=11641278; DOI=10.1101/gad.932201;
Kaliraman V., Mullen J.R., Fricke W.M., Bastin-Shanower S.A.,
Brill S.J.;
"Functional overlap between Sgs1-Top3 and the Mms4-Mus81
endonuclease.";
Genes Dev. 15:2730-2740(2001).
[5]
FUNCTION, AND INTERACTION WITH MMS4.
PubMed=11139495;
Mullen J.R., Kaliraman V., Ibrahim S.S., Brill S.J.;
"Requirement for three novel protein complexes in the absence of the
Sgs1 DNA helicase in Saccharomyces cerevisiae.";
Genetics 157:103-118(2001).
[6]
FUNCTION.
PubMed=12475932; DOI=10.1073/pnas.252652399;
Fabre F., Chan A., Heyer W.-D., Gangloff S.;
"Alternate pathways involving Sgs1/Top3, Mus81/ Mms4, and Srs2 prevent
formation of toxic recombination intermediates from single-stranded
gaps created by DNA replication.";
Proc. Natl. Acad. Sci. U.S.A. 99:16887-16892(2002).
[7]
ERRATUM.
Fabre F., Chan A., Heyer W.-D., Gangloff S.;
Proc. Natl. Acad. Sci. U.S.A. 100:1462-1462(2002).
[8]
FUNCTION, INTERACTION WITH MMS4, AND SUBCELLULAR LOCATION.
PubMed=14642571; DOI=10.1016/j.dnarep.2003.08.013;
Fu Y., Xiao W.;
"Functional domains required for the Saccharomyces cerevisiae Mus81-
Mms4 endonuclease complex formation and nuclear localization.";
DNA Repair 2:1435-1447(2003).
[9]
FUNCTION, CROSSOVER WITHOUT DOUBLE HOLLIDAY JUNCTION, AND MUTAGENESIS
OF 414-ASP-ASP-415.
PubMed=12750322;
de los Santos T., Hunter N., Lee C., Larkin B., Loidl J.,
Hollingsworth N.M.;
"The Mus81/Mms4 endonuclease acts independently of double-Holliday
junction resolution to promote a distinct subset of crossovers during
meiosis in budding yeast.";
Genetics 164:81-94(2003).
[10]
FUNCTION.
PubMed=12473680; DOI=10.1074/jbc.M210006200;
Whitby M.C., Osman F., Dixon J.;
"Cleavage of model replication forks by fission yeast Mus81-Eme1 and
budding yeast Mus81-Mms4.";
J. Biol. Chem. 278:6928-6935(2003).
[11]
FUNCTION, AND CLEAVAGE SITE SELECTION.
PubMed=12724407; DOI=10.1128/MCB.23.10.3487-3496.2003;
Bastin-Shanower S.A., Fricke W.M., Mullen J.R., Brill S.J.;
"The mechanism of Mus81-Mms4 cleavage site selection distinguishes it
from the homologous endonuclease Rad1-Rad10.";
Mol. Cell. Biol. 23:3487-3496(2003).
[12]
FUNCTION, AND CROSSOVER WITHOUT DOUBLE HOLLIDAY JUNCTION.
PubMed=14527420; DOI=10.1016/S1097-2765(03)00343-5;
Osman F., Dixon J., Doe C.L., Whitby M.C.;
"Generating crossovers by resolution of nicked Holliday junctions: a
role for Mus81-Eme1 in meiosis.";
Mol. Cell 12:761-774(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
FUNCTION.
PubMed=16193328; DOI=10.1007/s00294-005-0014-5;
Ii M., Brill S.J.;
"Roles of SGS1, MUS81, and RAD51 in the repair of lagging-strand
replication defects in Saccharomyces cerevisiae.";
Curr. Genet. 48:213-225(2005).
[15]
FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND INTERACTION
WITH MMS4.
PubMed=15590332; DOI=10.1016/j.dnarep.2004.10.001;
Fricke W.M., Bastin-Shanower S.A., Brill S.J.;
"Substrate specificity of the Saccharomyces cerevisiae Mus81-Mms4
endonuclease.";
DNA Repair 4:243-251(2005).
[16]
REVIEW.
PubMed=14752007; DOI=10.1101/gad.1165904;
Hollingsworth N.M., Brill S.J.;
"The Mus81 solution to resolution: generating meiotic crossovers
without Holliday junctions.";
Genes Dev. 18:117-125(2004).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: Interacts with MMS4 to form a DNA structure-specific
endonuclease with substrate preference for branched DNA structures
with a 5'-end at the branch nick. Typical substrates include 3'-
flap structures, D-loops, replication forks with regressed leading
strands and nicked Holliday junctions. Cleavage probably occurs
approximately half a helical turn upstream of the free 5'-end in
these structures. May be required in mitosis for the processing of
stalled replication fork intermediates arising spontaneously or
subsequent to treatment with DNA damaging agents such as
methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be
required in meiosis for the repair of meiosis-specific double
strand breaks subsequent to single-end invasion (SEI). This
involves consecutive cleavage of D-loops and nicked Holliday
junctions leading to sister chromatid crossover. In contrast to
MSH4-MSH5 dependent crossover, double Holliday junctions do not
seem to be involved. Spore formation and viability are severely
impaired in deletion strains. {ECO:0000269|PubMed:10905349,
ECO:0000269|PubMed:11139495, ECO:0000269|PubMed:11641278,
ECO:0000269|PubMed:12473680, ECO:0000269|PubMed:12475932,
ECO:0000269|PubMed:12724407, ECO:0000269|PubMed:12750322,
ECO:0000269|PubMed:14527420, ECO:0000269|PubMed:14642571,
ECO:0000269|PubMed:15590332, ECO:0000269|PubMed:16193328}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15590332};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15590332};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=31.1 nM for a nicked Holliday junction
{ECO:0000269|PubMed:15590332};
KM=6.84 nM for a regressed leading strand replication fork
{ECO:0000269|PubMed:15590332};
KM=4.8 nM for for a 3'-flap structure
{ECO:0000269|PubMed:15590332};
KM=3.45 nM for a nicked duplex {ECO:0000269|PubMed:15590332};
KM=14.0 nM for a regressed lagging strand replication fork
{ECO:0000269|PubMed:15590332};
KM=245 nM for a Y structure {ECO:0000269|PubMed:15590332};
KM=173 nM for a double flap structure
{ECO:0000269|PubMed:15590332};
Vmax=55.6 nmol/min/ng enzyme with a nicked Holliday junction as
substrate {ECO:0000269|PubMed:15590332};
Vmax=31.3 nmol/min/ng enzyme with a regressed leading strand
replication fork as substrate {ECO:0000269|PubMed:15590332};
Vmax=24.4 nmol/min/ng enzyme with a 3'-flap structure as
substrate {ECO:0000269|PubMed:15590332};
Vmax=2.21 nmol/min/ng enzyme with a nicked duplex as substrate
{ECO:0000269|PubMed:15590332};
Vmax=0.832 nmol/min/ng enzyme with a regressed lagging strand
replication fork as subsystrate {ECO:0000269|PubMed:15590332};
Vmax=0.0468 nmol/min/ng enzyme with a Y structure as substrate
{ECO:0000269|PubMed:15590332};
Vmax=0.0879 nmol/min/ng enzyme with a double flap structure as
substrate {ECO:0000269|PubMed:15590332};
pH dependence:
Optimum pH is 8.0 for the cleavage of a 3'-flap structure.
{ECO:0000269|PubMed:15590332};
-!- SUBUNIT: Interacts with MMS4 and RAD54.
{ECO:0000269|PubMed:10905349, ECO:0000269|PubMed:11139495,
ECO:0000269|PubMed:11641278, ECO:0000269|PubMed:14642571,
ECO:0000269|PubMed:15590332}.
-!- INTERACTION:
P38257:MMS4; NbExp=5; IntAct=EBI-33508, EBI-21547;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14642571}.
-!- MISCELLANEOUS: Two distinct classes of meiotic crossovers have
been demonstrated in budding yeast. Class I crossovers exhibit
crossover interference and require MSH4 and MSH5 for their
resolution, while class II crossovers exhibit no crossover
interference and require MUS81 and MMS4. While class I crossovers
represent the majority of crossovers in S.cerevisiae, they are
virtually absent in S.pombe, which lacks orthologs of MSH4 and
MSH5.
-!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the XPF family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U32274; AAB64828.1; -; Genomic_DNA.
EMBL; BK006938; DAA12230.1; -; Genomic_DNA.
PIR; S69670; S69670.
RefSeq; NP_010674.3; NM_001180694.3.
ProteinModelPortal; Q04149; -.
SMR; Q04149; -.
BioGrid; 32447; 172.
DIP; DIP-1009N; -.
IntAct; Q04149; 41.
MINT; MINT-406845; -.
STRING; 4932.YDR386W; -.
iPTMnet; Q04149; -.
MaxQB; Q04149; -.
PRIDE; Q04149; -.
EnsemblFungi; YDR386W; YDR386W; YDR386W.
GeneID; 851994; -.
KEGG; sce:YDR386W; -.
EuPathDB; FungiDB:YDR386W; -.
SGD; S000002794; MUS81.
GeneTree; ENSGT00390000005498; -.
HOGENOM; HOG000248281; -.
InParanoid; Q04149; -.
KO; K08991; -.
OMA; KCGRLQR; -.
OrthoDB; EOG092C1AVP; -.
BioCyc; YEAST:G3O-29934-MONOMER; -.
PRO; PR:Q04149; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0048476; C:Holliday junction resolvase complex; IDA:SGD.
GO; GO:0005634; C:nucleus; IMP:SGD.
GO; GO:0048257; F:3'-flap endonuclease activity; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
GO; GO:0006281; P:DNA repair; IGI:SGD.
GO; GO:0006265; P:DNA topological change; IGI:SGD.
GO; GO:0000727; P:double-strand break repair via break-induced replication; IMP:SGD.
GO; GO:0031573; P:intra-S DNA damage checkpoint; IBA:GO_Central.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IBA:GO_Central.
GO; GO:0051097; P:negative regulation of helicase activity; IDA:SGD.
GO; GO:0007131; P:reciprocal meiotic recombination; IGI:SGD.
GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
GO; GO:0000712; P:resolution of meiotic recombination intermediates; IGI:SGD.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR006166; ERCC4_domain.
InterPro; IPR011335; Restrct_endonuc-II-like.
Pfam; PF02732; ERCC4; 1.
SMART; SM00891; ERCC4; 1.
SUPFAM; SSF47802; SSF47802; 1.
SUPFAM; SSF52980; SSF52980; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; DNA recombination; DNA repair;
Endonuclease; Hydrolase; Magnesium; Manganese; Meiosis; Metal-binding;
Nuclease; Nucleus; Reference proteome.
CHAIN 1 632 Crossover junction endonuclease MUS81.
/FTId=PRO_0000198861.
DOMAIN 351 448 ERCC4.
REGION 527 632 Interaction with MMS4.
ACT_SITE 415 415 {ECO:0000305}.
MUTAGEN 414 415 DD->AA: In allele MUS81-DD; abrogates
endonuclease activity.
{ECO:0000269|PubMed:12750322}.
SEQUENCE 632 AA; 72309 MW; F73FA3856C5F87F1 CRC64;
MELSSNLKDL YIEWLQELVD GLTPKQEQLK IAYEKAKRNL QNAEGSFYYP TDLKKVKGIG
NTIIKRLDTK LRNYCKIHHI SPVEAPSLTQ TSSTRPPKRT TTALRSIVNS CENDKNEAPE
EKGTKKRKTR KYIPKKRSGG YAILLSLLEL NAIPRGVSKE QIIEVAGKYS DHCMTPNFST
KEFYGAWSSI AALKKHSLVL EEGRPKRYSL TEEGVELTKS LKTADGISFP KENEEPNEYS
VTRNESSEFT ANLTDLRGEY GKEEEPCDIN NTSFMLDITF QDLSTPQRLQ NNVFKNDRLN
SQTNISSHKL EEVSDDQTVP DSALKAKSTI KRRRYNGVSY ELWCSGDFEV FPIIDHREIK
SQSDREFFSR AFERKGMKSE IRQLALGDII WVAKNKNTGL QCVLNTIVER KRLDDLALSI
RDNRFMEQKN RLEKSGCEHK YYLIEETMSG NIGNMNEALK TALWVILVYY KFSMIRTCNS
DETVEKIHAL HTVISHHYSQ KDLIVIFPSD LKSKDDYKKV LLQFRREFER KGGIECCHNL
ECFQELMGKG DLKTVGELTI HVLMLVKGIS LEKAVAIQEI FPTLNKILMA YKTCSSEEEA
KLLMFNVLGD APGAKKITKS LSEKIYDAFG KL


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