{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T09:48:03Z","timestamp":1791280083831,"version":"4.1.0"},"reference-count":178,"publisher":"Portland Press Ltd.","issue":"3","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2009,6,1]]},"abstract":"<jats:p>The six Saccharomyces cerevisiae SLX genes were identified in a screen for factors required for the viability of cells lacking Sgs1, a member of the RecQ helicase family involved in processing stalled replisomes and in the maintenance of genome stability. The six SLX gene products form three distinct heterodimeric complexes, and all three have catalytic activity. Slx3\u2013Slx2 (also known as Mus81\u2013Mms4) and Slx1\u2013Slx4 are both heterodimeric endonucleases with a marked specificity for branched replication fork-like DNA species, whereas Slx5\u2013Slx8 is a SUMO (small ubiquitin-related modifier)-targeted E3 ubiquitin ligase. All three complexes play important, but distinct, roles in different aspects of the cellular response to DNA damage and perturbed DNA replication. Slx4 interacts physically not only with Slx1, but also with Rad1\u2013Rad10 [XPF (xeroderma pigmentosum complementation group F)\u2013ERCC1 (excision repair cross-complementing 1) in humans], another structure-specific endonuclease that participates in the repair of UV-induced DNA damage and in a subpathway of recombinational DNA DSB (double-strand break) repair. Curiously, Slx4 is essential for repair of DSBs by Rad1\u2013Rad10, but is not required for repair of UV damage. Slx4 also promotes cellular resistance to DNA-alkylating agents that block the progression of replisomes during DNA replication, by facilitating the error-free mode of lesion bypass. This does not require Slx1 or Rad1\u2013Rad10, and so Slx4 has several distinct roles in protecting genome stability. In the present article, I provide an overview of our current understanding of the cellular roles of the Slx proteins, paying particular attention to the advances that have been made in understanding the cellular roles of Slx4. In particular, protein\u2013protein interactions and underlying molecular mechanisms are discussed and I draw attention to the many questions that have yet to be answered.<\/jats:p>","DOI":"10.1042\/bst0370495","type":"journal-article","created":{"date-parts":[[2009,5,20]],"date-time":"2009-05-20T13:18:20Z","timestamp":1242825500000},"page":"495-510","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["Control of genome stability by Slx protein complexes"],"prefix":"10.1042","volume":"37","author":[{"given":"John","family":"Rouse","sequence":"first","affiliation":[{"name":"1MRC Protein Phosphorylation Unit, Sir James Black Centre, University of Dundee, Dundee DD1 5EH, Scotland, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2009,5,20]]},"reference":[{"key":"2021111718544567100_B1","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1007\/s00412-007-0142-4","article-title":"RecQ helicases: guardian angels of the DNA replication fork","volume":"117","author":"Bachrati","year":"2008","journal-title":"Chromosoma"},{"key":"2021111718544567100_B2","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/j.tibs.2008.09.003","article-title":"Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance","volume":"33","author":"Bohr","year":"2008","journal-title":"Trends Biochem. Sci."},{"key":"2021111718544567100_B3","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1126\/science.272.5259.258","article-title":"Positional cloning of the Werner's syndrome gene","volume":"272","author":"Yu","year":"1996","journal-title":"Science"},{"key":"2021111718544567100_B4","first-page":"193","article-title":"RECQL4: one gene behind three syndromes having an increased risk for cancers","volume":"273","author":"Siitonen","year":"2006","journal-title":"FEBS J."},{"key":"2021111718544567100_B5","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1136\/jmg.2005.031781","article-title":"Revisiting the craniosynostosis\u2013radial ray hypoplasia association: Baller\u2013Gerold syndrome caused by mutations in the RECQL4 gene","volume":"43","author":"Van\u00a0Maldergem","year":"2006","journal-title":"J. Med. 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J."},{"key":"2021111718544567100_B11","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1038\/cr.2008.1","article-title":"Homologous recombination in DNA repair and DNA damage tolerance","volume":"18","author":"Li","year":"2008","journal-title":"Cell Res."},{"key":"2021111718544567100_B12","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1128\/MMBR.63.2.349-404.1999","article-title":"Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae","volume":"63","author":"P\u00e2ques","year":"1999","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"2021111718544567100_B13","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1146\/annurev.biochem.77.061306.125255","article-title":"Mechanism of eukaryotic homologous recombination","volume":"77","author":"Filippo","year":"2008","journal-title":"Annu. Rev. 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Genet."},{"key":"2021111718544567100_B16","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0092-8674(83)90331-8","article-title":"The double-strand-break repair model for recombination","volume":"33","author":"Szostak","year":"1983","journal-title":"Cell"},{"key":"2021111718544567100_B17","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1038\/nrm951","article-title":"Recombinational repair and restart of damaged replication forks","volume":"3","author":"McGlynn","year":"2002","journal-title":"Nat. Rev. Mol. 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Biochem."},{"key":"2021111718544567100_B46","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1016\/j.dnarep.2007.02.019","article-title":"Exploring the roles of Mus81-Eme1\/Mms4 at perturbed replication forks","volume":"6","author":"Osman","year":"2007","journal-title":"DNA Repair"},{"key":"2021111718544567100_B47","doi-asserted-by":"crossref","first-page":"3487","DOI":"10.1128\/MCB.23.10.3487-3496.2003","article-title":"The mechanism of Mus81-Mms4 cleavage site selection distinguishes it from the homologous endonuclease Rad1-Rad10","volume":"23","author":"Bastin-Shanower","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B48","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1038\/nsmb1313","article-title":"The structure-specific endonuclease Mus81 contributes to replication restart by generating double-strand DNA breaks","volume":"14","author":"Hanada","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2021111718544567100_B49","doi-asserted-by":"crossref","first-page":"4921","DOI":"10.1038\/sj.emboj.7601344","article-title":"The structure-specific endonuclease Mus81-Eme1 promotes conversion of interstrand DNA crosslinks into double-strands breaks","volume":"25","author":"Hanada","year":"2006","journal-title":"EMBO J."},{"key":"2021111718544567100_B50","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1146\/annurev.pharmtox.051208.165340","article-title":"Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology","volume":"49","author":"Schwartz","year":"2009","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"2021111718544567100_B51","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1038\/nrm2293","article-title":"Concepts in sumoylation: a decade on","volume":"8","author":"Geiss-Friedlander","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021111718544567100_B52","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1586\/14789450.5.1.121","article-title":"Ubiquitin proteolytic system: focus on SUMO","volume":"5","author":"Wilson","year":"2008","journal-title":"Expert Rev. Proteomics"},{"key":"2021111718544567100_B53","doi-asserted-by":"crossref","first-page":"2800","DOI":"10.4161\/cc.6.22.4882","article-title":"The yeast Slx5-Slx8 DNA integrity complex displays ubiquitin ligase activity","volume":"6","author":"Li","year":"2007","journal-title":"Cell Cycle"},{"key":"2021111718544567100_B54","doi-asserted-by":"crossref","first-page":"34176","DOI":"10.1074\/jbc.M706025200","article-title":"The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation","volume":"282","author":"Xie","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B55","doi-asserted-by":"crossref","first-page":"34167","DOI":"10.1074\/jbc.M706505200","article-title":"Ubiquitin-dependent proteolytic control of SUMO conjugates","volume":"282","author":"Uzunova","year":"2007","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B56","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1016\/j.dnarep.2007.06.004","article-title":"Stimulation of in vitro sumoylation by Slx5-Slx8: Evidence for a functional interaction with the SUMO pathway","volume":"6","author":"Li","year":"2007","journal-title":"DNA Repair"},{"key":"2021111718544567100_B57","doi-asserted-by":"crossref","first-page":"19912","DOI":"10.1074\/jbc.M802690200","article-title":"Activation of the Slx5-Slx8 ubiquitin ligase by poly-small ubiquitin-like modifier conjugates","volume":"283","author":"Mullen","year":"2008","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B58","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1128\/MCB.01291-07","article-title":"Slx5 promotes transcriptional silencing and is required for robust growth in the absence of Sir2","volume":"28","author":"Darst","year":"2008","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B59","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1083\/jcb.147.5.981","article-title":"Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins","volume":"147","author":"Johnson","year":"1999","journal-title":"J. Cell Biol."},{"key":"2021111718544567100_B60","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1038\/18457","article-title":"A new protease required for cell-cycle progression in yeast","volume":"398","author":"Li","year":"1999","journal-title":"Nature"},{"key":"2021111718544567100_B61","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.1016\/S1097-2765(02)00543-9","article-title":"The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II","volume":"9","author":"Bachant","year":"2002","journal-title":"Mol. Cell"},{"key":"2021111718544567100_B62","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1083\/jcb.200305080","article-title":"Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion","volume":"163","author":"Stead","year":"2003","journal-title":"J. Cell Biol."},{"key":"2021111718544567100_B63","doi-asserted-by":"crossref","first-page":"6153","DOI":"10.1128\/MCB.00787-07","article-title":"The slx5\u2013slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination","volume":"27","author":"Burgess","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B64","doi-asserted-by":"crossref","first-page":"1284","DOI":"10.1038\/ncb1488","article-title":"Control of Rad52 recombination activity by double-strand break-induced SUMO modification","volume":"8","author":"Sacher","year":"2006","journal-title":"Nat. Cell Biol."},{"key":"2021111718544567100_B65","doi-asserted-by":"crossref","first-page":"16887","DOI":"10.1073\/pnas.252652399","article-title":"Alternate pathways involving Sgs1\/Top3, Mus81\/Mms4, and Srs2 prevent formation of toxic recombination intermediates from single-stranded gaps created by DNA replication","volume":"99","author":"Fabre","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111718544567100_B66","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1016\/j.cell.2005.12.036","article-title":"A DNA integrity network in the yeast Saccharomyces cerevisiae","volume":"124","author":"Pan","year":"2006","journal-title":"Cell"},{"key":"2021111718544567100_B67","doi-asserted-by":"crossref","first-page":"4089","DOI":"10.1038\/sj.emboj.7601838","article-title":"SUMO-targeted ubiquitin ligases in genome stability","volume":"26","author":"Prudden","year":"2007","journal-title":"EMBO J."},{"key":"2021111718544567100_B68","doi-asserted-by":"crossref","first-page":"4102","DOI":"10.1038\/sj.emboj.7601839","article-title":"Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins","volume":"26","author":"Sun","year":"2007","journal-title":"EMBO J."},{"key":"2021111718544567100_B69","doi-asserted-by":"crossref","first-page":"3537","DOI":"10.1128\/MCB.22.10.3537-3548.2002","article-title":"The Schizosaccharomyces pombe rad60 gene is essential for repairing double-strand DNA breaks spontaneously occurring during replication and induced by DNA-damaging agents","volume":"22","author":"Morishita","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B70","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1128\/MCB.26.1.343-353.2006","article-title":"Rhp51-dependent recombination intermediates that do not generate checkpoint signal are accumulated in Schizosaccharomyces pombe rad60 and smc5\/6 mutants after release from replication arrest","volume":"26","author":"Miyabe","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B71","doi-asserted-by":"crossref","first-page":"27973","DOI":"10.1074\/jbc.M601943200","article-title":"SUMO-binding motifs mediate the Rad60-dependent response to replicative stress and self-association","volume":"281","author":"Raffa","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B72","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1038\/ncb1716","article-title":"RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation","volume":"10","author":"Tatham","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"2021111718544567100_B73","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1182\/blood.V88.3.1052.1052","article-title":"In vitro studies on cellular and molecular mechanisms of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia: As2O3 induces NB4 cell apoptosis with downregulation of bcl-2 expression and modulation of PML-RAR\u03b1\/PML proteins","volume":"88","author":"Chen","year":"1996","journal-title":"Blood"},{"key":"2021111718544567100_B74","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1084\/jem.193.12.1361","article-title":"Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML\/retinoic acid receptor \u03b1 degradation","volume":"193","author":"Lallemand-Breitenbach","year":"2001","journal-title":"J. Exp. Med."},{"key":"2021111718544567100_B75","doi-asserted-by":"crossref","first-page":"4308","DOI":"10.1182\/blood.V92.11.4308","article-title":"Trivalent antimonials induce degradation of the PML-RAR\u03b1 oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells","volume":"92","author":"Muller","year":"1998","journal-title":"Blood"},{"key":"2021111718544567100_B76","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1093\/jnci\/90.2.124","article-title":"Arsenic trioxide as an inducer of apoptosis and loss of PML\/RAR\u03b1 protein in acute promyelocytic leukemia cells","volume":"90","author":"Shao","year":"1998","journal-title":"J. Natl. Cancer Inst."},{"key":"2021111718544567100_B77","doi-asserted-by":"crossref","first-page":"3978","DOI":"10.1073\/pnas.94.8.3978","article-title":"Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia","volume":"94","author":"Zhu","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111718544567100_B78","doi-asserted-by":"crossref","first-page":"5170","DOI":"10.1128\/MCB.19.7.5170","article-title":"PIC-1\/SUMO-1-modified PML-retinoic acid receptor \u03b1 mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia","volume":"19","author":"Sternsdorf","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B79","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1038\/ncb1717","article-title":"Arsenic degrades PML or PML\u2013RAR \u03b1 through a SUMO-triggered RNF4\/ubiquitin-mediated pathway","volume":"10","author":"Lallemand-Breitenbach","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"2021111718544567100_B80","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1101\/gr.181001","article-title":"Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system","volume":"11","author":"Aravind","year":"2001","journal-title":"Genome Res."},{"key":"2021111718544567100_B81","doi-asserted-by":"crossref","first-page":"2446","DOI":"10.1099\/mic.0.2008\/017616-0","article-title":"Analysis of base excision and nucleotide excision repair in Candida albicans","volume":"154","author":"Legrand","year":"2008","journal-title":"Microbiology"},{"key":"2021111718544567100_B82","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1186\/1471-2164-7-98","article-title":"Phylogenomic analysis of the GIY-YIG nuclease superfamily","volume":"7","author":"Dunin-Horkawicz","year":"2006","journal-title":"BMC Genomics"},{"key":"2021111718544567100_B83","doi-asserted-by":"crossref","first-page":"2115","DOI":"10.1093\/nar\/27.10.2115","article-title":"Configuration of the catalytic GIY-YIG domain of intron endonuclease I-Tevl: coincidence of computational and molecular findings","volume":"27","author":"Kowalski","year":"1999","journal-title":"Nucleic Acids Res."},{"key":"2021111718544567100_B84","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/S0968-0004(99)01537-6","article-title":"SAP: a putative DNA-binding motif involved in chromosomal organization","volume":"25","author":"Aravind","year":"2000","journal-title":"Trends Biochem. Sci."},{"key":"2021111718544567100_B85","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.4161\/cc.7.23.7166","article-title":"Cooperation of replication protein A with the ubiquitin ligase Rad18 in DNA damage bypass","volume":"7","author":"Huttner","year":"2008","journal-title":"Cell Cycle"},{"key":"2021111718544567100_B86","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1091\/mbc.e03-08-0586","article-title":"Slx1\u2013Slx4 are subunits of a structure-specific endonuclease that maintains ribosomal DNA in fission yeast","volume":"15","author":"Coulon","year":"2004","journal-title":"Mol. Biol. 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Bacteriol."},{"key":"2021111718544567100_B90","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/ncb0508-507","article-title":"Marked for death","volume":"10","author":"Petrie","year":"2008","journal-title":"Nat. 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Cell. Biol."},{"key":"2021111718544567100_B96","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1007\/BF00332757","article-title":"Replicon size of yeast ribosomal DNA","volume":"195","author":"Walmsley","year":"1984","journal-title":"Mol. Gen. Genet."},{"key":"2021111718544567100_B97","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1007\/s00294-002-0319-6","article-title":"Role of SGS1 and SLX4 in maintaining rDNA structure in Saccharomyces cerevisiae","volume":"41","author":"Kaliraman","year":"2002","journal-title":"Curr. Genet."},{"key":"2021111718544567100_B98","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1101\/gad.5.6.958","article-title":"A group of interacting yeast DNA replication genes","volume":"5","author":"Hennessy","year":"1991","journal-title":"Genes Dev."},{"key":"2021111718544567100_B99","doi-asserted-by":"crossref","first-page":"2956","DOI":"10.1101\/gad.12.18.2956","article-title":"Recovery from DNA replicational stress is the essential function of the S-phase checkpoint pathway","volume":"12","author":"Desany","year":"1998","journal-title":"Genes Dev."},{"key":"2021111718544567100_B100","doi-asserted-by":"crossref","first-page":"2081","DOI":"10.1091\/mbc.e05-11-1006","article-title":"Rad22Rad52-dependent repair of ribosomal DNA repeats cleaved by Slx1-Slx4 endonuclease","volume":"17","author":"Coulon","year":"2006","journal-title":"Mol. Biol. 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Natl. Acad. Sci. U.S.A."},{"key":"2021111718544567100_B104","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1042\/BJ20050768","article-title":"Slx4 becomes phosphorylated after DNA damage in a Mec1\/Tel1-dependent manner and is required for repair of DNA alkylation damage","volume":"391","author":"Flott","year":"2005","journal-title":"Biochem. J."},{"key":"2021111718544567100_B105","doi-asserted-by":"crossref","first-page":"6433","DOI":"10.1128\/MCB.00135-07","article-title":"Phosphorylation of Slx4 by mec1 and tel1 regulates the single-strand annealing mode of DNA repair in budding yeast","volume":"27","author":"Flott","year":"2007","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B106","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/0027-5107(90)90173-2","article-title":"Distribution of methyl and ethyl adducts following alkylation with monofunctional alkylating agents","volume":"231","author":"Beranek","year":"1990","journal-title":"Mutat. Res."},{"key":"2021111718544567100_B107","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1091\/mbc.e05-08-0785","article-title":"Slx4 regulates DNA damage checkpoint-dependent phosphorylation of the BRCT domain protein Rtt107\/Esc4","volume":"17","author":"Roberts","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"2021111718544567100_B108","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0921-8777(01)00089-1","article-title":"Translesion synthesis by the UmuC family of DNA polymerases","volume":"486","author":"Wang","year":"2001","journal-title":"Mutat. Res."},{"key":"2021111718544567100_B109","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1038\/nrm1781","article-title":"Suffering in silence: the tolerance of DNA damage","volume":"6","author":"Friedberg","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021111718544567100_B110","doi-asserted-by":"crossref","first-page":"1735","DOI":"10.1002\/cbic.200500139","article-title":"The RAD6 pathway: control of DNA damage bypass and mutagenesis by ubiquitin and SUMO","volume":"6","author":"Ulrich","year":"2005","journal-title":"Chembiochem"},{"key":"2021111718544567100_B111","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1016\/j.mrfmmm.2003.08.014","article-title":"Regulation of alternative replication bypass pathways at stalled replication forks and its effects on genome stability: a yeast model","volume":"532","author":"Barbour","year":"2003","journal-title":"Mutat. Res."},{"key":"2021111718544567100_B112","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1007\/BF00352525","article-title":"Characterization of postreplication repair in Saccharomyces cerevisiae and effects of rad6, rad18, rev3 and rad52 mutations","volume":"184","author":"Prakash","year":"1981","journal-title":"Mol. Gen. Genet."},{"key":"2021111718544567100_B113","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/329131a0","article-title":"The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme","volume":"329","author":"Jentsch","year":"1987","journal-title":"Nature"},{"key":"2021111718544567100_B114","doi-asserted-by":"crossref","first-page":"23360","DOI":"10.1074\/jbc.272.37.23360","article-title":"Yeast DNA repair proteins Rad6 and Rad18 form a heterodimer that has ubiquitin conjugating, DNA binding, and ATP hydrolytic activities","volume":"272","author":"Bailly","year":"1997","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B115","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1101\/gad.8.7.811","article-title":"Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites","volume":"8","author":"Bailly","year":"1994","journal-title":"Genes Dev."},{"key":"2021111718544567100_B116","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/nature00991","article-title":"RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO","volume":"419","author":"Hoege","year":"2002","journal-title":"Nature"},{"key":"2021111718544567100_B117","doi-asserted-by":"crossref","first-page":"4267","DOI":"10.1128\/MCB.24.10.4267-4274.2004","article-title":"Opposing effects of ubiquitin conjugation and SUMO modification of PCNA on replicational bypass of DNA lesions in Saccharomyces cerevisiae","volume":"24","author":"Haracska","year":"2004","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B118","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1146\/annurev.biochem.74.082803.133250","article-title":"Eukaryotic translesion synthesis DNA polymerases: specificity of structure and function","volume":"74","author":"Prakash","year":"2005","journal-title":"Annu. Rev. Biochem."},{"key":"2021111718544567100_B119","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.4161\/cc.3.8.1074","article-title":"Ubiquitination of PCNA and the polymerase switch in human cells","volume":"3","author":"Kannouche","year":"2004","journal-title":"Cell Cycle"},{"key":"2021111718544567100_B120","doi-asserted-by":"crossref","first-page":"1821","DOI":"10.1126\/science.1120615","article-title":"Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis","volume":"310","author":"Bienko","year":"2005","journal-title":"Science"},{"key":"2021111718544567100_B121","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1126\/science.283.5404.1001","article-title":"Efficient bypass of a thymine-thymine dimer by yeast DNA polymerase, Poleta","volume":"283","author":"Johnson","year":"1999","journal-title":"Science"},{"key":"2021111718544567100_B122","first-page":"3094","article-title":"Accuracy of thymine-thymine dimer bypass by Saccharomyces cerevisiae DNA polymerase \u03b7","volume":"97","author":"Washington","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111718544567100_B123","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1098\/rstb.2000.0001","article-title":"Mutagenesis in eukaryotes dependent on DNA polymerase \u03b6 and Rev1p","volume":"356","author":"Lawrence","year":"2001","journal-title":"Philos. Trans. R. Soc. London Ser. B"},{"key":"2021111718544567100_B124","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1128\/MCB.22.7.2419-2426.2002","article-title":"Requirement of RAD5 and MMS2 for postreplication repair of UV-damaged DNA in Saccharomyces cerevisiae","volume":"22","author":"Torres-Ramos","year":"2002","journal-title":"Mol. Cell. Biol."},{"key":"2021111718544567100_B125","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1016\/S0092-8674(00)80575-9","article-title":"Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair","volume":"96","author":"Hofmann","year":"1999","journal-title":"Cell"},{"key":"2021111718544567100_B126","doi-asserted-by":"crossref","first-page":"3388","DOI":"10.1093\/emboj\/19.13.3388","article-title":"Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair","volume":"19","author":"Ulrich","year":"2000","journal-title":"EMBO J."},{"key":"2021111718544567100_B127","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/0022-2836(76)90156-X","article-title":"A model for replication repair in mammalian cells","volume":"101","author":"Higgins","year":"1976","journal-title":"J. Mol. Biol."},{"key":"2021111718544567100_B128","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/bies.950160408","article-title":"The RAD6 DNA repair pathway in Saccharomyces cerevisiae: what does it do, and how does it do it?","volume":"16","author":"Lawrence","year":"1994","journal-title":"BioEssays"},{"key":"2021111718544567100_B129","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1186\/1471-2199-7-40","article-title":"Rtt107\/Esc4 binds silent chromatin and DNA repair proteins using different BRCT motifs","volume":"7","author":"Zappulla","year":"2006","journal-title":"BMC Mol. Biol."},{"key":"2021111718544567100_B130","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/S0014-5793(96)01312-9","article-title":"From BRCA1 to RAP1: a widespread BRCT module closely associated with DNA repair","volume":"400","author":"Callebaut","year":"1997","journal-title":"FEBS Lett."},{"key":"2021111718544567100_B131","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1096\/fasebj.11.1.9034168","article-title":"A superfamily of conserved domains in DNA damage-responsive cell cycle checkpoint proteins","volume":"11","author":"Bork","year":"1997","journal-title":"FASEB J."},{"key":"2021111718544567100_B132","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1093\/genetics\/159.4.1449","article-title":"Multiple regulators of Ty1 transposition in Saccharomyces cerevisiae have conserved roles in genome maintenance","volume":"159","author":"Scholes","year":"2001","journal-title":"Genetics"},{"key":"2021111718544567100_B133","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1038\/sj.emboj.7600129","article-title":"Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage","volume":"23","author":"Rouse","year":"2004","journal-title":"EMBO J."},{"key":"2021111718544567100_B134","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1091\/mbc.e05-08-0785","article-title":"Slx4 regulates DNA damage phosphorylation of the BRCT checkpoint-dependent domain protein Rtt107\/Esc4","volume":"17","author":"Roberts","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"2021111718544567100_B135","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1038\/sj.emboj.7600129","article-title":"Esc4p, a new target of Mec1p (ATR), promotes resumption of DNA synthesis after DNA damage","volume":"23","author":"Rouse","year":"2004","journal-title":"EMBO J."},{"key":"2021111718544567100_B136","doi-asserted-by":"crossref","first-page":"808","DOI":"10.1126\/science.1091317","article-title":"Global mapping of the yeast genetic interaction network","volume":"303","author":"Tong","year":"2004","journal-title":"Science"},{"key":"2021111718544567100_B137","doi-asserted-by":"crossref","first-page":"2364","DOI":"10.1126\/science.1065810","article-title":"Systematic genetic analysis with ordered arrays of yeast deletion mutants","volume":"294","author":"Tong","year":"2001","journal-title":"Science"},{"key":"2021111718544567100_B138","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1534\/genetics.105.044966","article-title":"Brcl-mediated DNA repair and damage tolerance","volume":"171","author":"Sheedy","year":"2005","journal-title":"Genetics"},{"key":"2021111718544567100_B139","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1101\/gad.1320505","article-title":"Dynamic molecular linkers of the genome: the first decade of SMC proteins","volume":"19","author":"Losada","year":"2005","journal-title":"Genes Dev."},{"key":"2021111718544567100_B140","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/nrm2309","article-title":"Smc5\/6: a link between DNA repair and unidirectional replication?","volume":"9","author":"Murray","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021111718544567100_B141","doi-asserted-by":"crossref","first-page":"4569","DOI":"10.1073\/pnas.061034498","article-title":"A comprehensive two-hybrid analysis to explore the yeast protein interactome","volume":"98","author":"Ito","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111718544567100_B142","doi-asserted-by":"crossref","first-page":"11236","DOI":"10.1073\/pnas.0504341102","article-title":"Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1","volume":"102","author":"Tsodikov","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111718544567100_B143","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1016\/j.str.2005.08.014","article-title":"The structure of the human ERCC1\/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair","volume":"13","author":"Tripsianes","year":"2005","journal-title":"Structure"},{"key":"2021111718544567100_B144","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1038\/362860a0","article-title":"Yeast DNA-repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease","volume":"362","author":"Tomkinson","year":"1993","journal-title":"Nature"},{"key":"2021111718544567100_B145","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1111\/j.1365-2958.1993.tb01662.x","article-title":"Yeast DNA recombination and repair proteins Rad1 and Rad10 constitute a complex in vivo mediated by localized hydrophobic domains","volume":"8","author":"Bardwell","year":"1993","journal-title":"Mol. Microbiol."},{"key":"2021111718544567100_B146","doi-asserted-by":"crossref","first-page":"2082","DOI":"10.1126\/science.8091230","article-title":"Specific cleavage of model recombination and repair intermediates by the yeast Rad1-Rad10 DNA endonuclease","volume":"265","author":"Bardwell","year":"1994","journal-title":"Science"},{"key":"2021111718544567100_B147","doi-asserted-by":"crossref","first-page":"24638","DOI":"10.1074\/jbc.270.42.24638","article-title":"Role of the Rad1 and Rad10 proteins in nucleotide excision-repair and recombination","volume":"270","author":"Davies","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B148","doi-asserted-by":"crossref","first-page":"20551","DOI":"10.1074\/jbc.271.34.20551","article-title":"Identification of functional domains within the RAD1\u00b7RAD10 repair and recombination endonuclease of Saccharomyces cerevisiae","volume":"271","author":"Rodriguez","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021111718544567100_B149","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1016\/j.biochi.2003.10.017","article-title":"The eukaryotic nucleotide excision repair pathway","volume":"85","author":"Costa","year":"2003","journal-title":"Biochimie"},{"key":"2021111718544567100_B150","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1101\/gad.13.7.768","article-title":"Molecular mechanism of nucleotide excision repair","volume":"13","author":"de\u00a0Laat","year":"1999","journal-title":"Genes Dev."},{"key":"2021111718544567100_B151","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0027-5107(00)00037-3","article-title":"Nucleotide excision repair in yeast","volume":"451","author":"Prakash","year":"2000","journal-title":"Mutat. 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