title: A versatile scaffold contributes to damage survival via sumoylation and nuclease interactions.
abstract: DNA repair scaffolds mediate specific DNA and protein interactions in order to assist repair enzymes in recognizing and removing damaged sequences. Many scaffold proteins are dedicated to repairing a particular type of lesion. Here, we show that the budding yeast Saw1 scaffold is more versatile. It helps cells cope with base lesions and protein-DNA adducts through its known function of recruiting the Rad1-Rad10 nuclease to DNA. In addition, it promotes UV survival via a mechanism mediated by its sumoylation. Saw1 sumoylation favors its interaction with another nuclease Slx1-Slx4, and this SUMO-mediated role is genetically separable from two main UV lesion repair processes. These effects of Saw1 and its sumoylation suggest that Saw1 is a multifunctional scaffold that can facilitate diverse types of DNA repair through its modification and nuclease interactions.
authors.affiliation: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Programs in Biochemistry, Cell, and Molecular Biology, Weill Cornell Graduate School of Medical Sciences, New York, NY 10065, USA.
authors.forename: Prabha
authors.initials: P
authors.lastname: Sarangi
authors.affiliation: Department of Biology, Masaryk University, Brno 62500, Czech Republic.
authors.forename: Veronika
authors.initials: V
authors.lastname: Altmannova
authors.affiliation: Department of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
authors.forename: Cory
authors.initials: C
authors.lastname: Holland
authors.affiliation: Department of Biology, Masaryk University, Brno 62500, Czech Republic.
authors.forename: Zdenka
authors.initials: Z
authors.lastname: Bartosova
authors.affiliation: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
authors.forename: Fanfan
authors.initials: F
authors.lastname: Hao
authors.affiliation: Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Vienna 1030, Austria.
authors.forename: Dorothea
authors.initials: D
authors.lastname: Anrather
authors.affiliation: Department of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Vienna 1030, Austria.
authors.forename: Gustav
authors.initials: G
authors.lastname: Ammerer
authors.affiliation: Department of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA; Division of Radiation Biology, Department of Radiation Oncology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
authors.forename: Sang Eun
authors.initials: SE
authors.lastname: Lee
authors.affiliation: Department of Biology, Masaryk University, Brno 62500, Czech Republic; National Centre for Biomolecular Research, Masaryk University, Brno 62500, Czech Republic; International Clinical Research Center, St. Anne's University Hospital in Brno, Brno 60200, Czech Republic. Electronic address: lkrejci@chemi.muni.cz.
authors.forename: Lumir
authors.initials: L
authors.lastname: Krejci
authors.affiliation: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Programs in Biochemistry, Cell, and Molecular Biology, Weill Cornell Graduate School of Medical Sciences, New York, NY 10065, USA. Electronic address: zhaox1@mskcc.org.
authors.forename: Xiaolan
authors.initials: X
authors.lastname: Zhao
mesh_terms: D004249:DNA Damage; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000378:metabolism*; D004720:Endonucleases / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics* / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics* / Q000378:metabolism*; D058207:Sumoylation; D016019:Survival Analysis
chemical_list: D004268:DNA-Binding Proteins; D029701:Saccharomyces cerevisiae Proteins; C579349:Saw1 protein, S cerevisiae; D004720:Endonucleases