A versatile scaffold contributes to damage survival via sumoylation and nuclease interactions

scientific article

A versatile scaffold contributes to damage survival via sumoylation and nuclease interactions is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1016/J.CELREP.2014.08.054
P932PMC publication ID4280569
P698PubMed publication ID25263559
P5875ResearchGate publication ID266263240

P50authorLumír KrejčíQ37373262
Xiaolan ZhaoQ42412104
Zdenka BartosovaQ63965665
P2093author name stringSang Eun Lee
Veronika Altmannova
Dorothea Anrather
Gustav Ammerer
Fanfan Hao
Cory Holland
Prabha Sarangi
P2860cites workThe SUMO system: an overviewQ37357956
Alternative excision repair pathwaysQ38104337
A Rad52 homolog is required for RAD51-independent mitotic recombination in Saccharomyces cerevisiaeQ38354045
SAW1 is required for SDSA double-strand break repair in S. cerevisiaeQ39002470
Characterization of a UV endonuclease gene from the fission yeast Schizosaccharomyces pombe and its bacterial homologQ39715901
Characterization of the alternative excision repair pathway of UV-damaged DNA in Schizosaccharomyces pombe.Q39719647
A new ATP-independent DNA endonuclease from Schizosaccharomyces pombe that recognizes cyclobutane pyrimidine dimers and 6-4 photoproductsQ40411071
Two alternative pathways of double-strand break repair that are kinetically separable and independently modulatedQ40678286
A eukaryotic gene encoding an endonuclease that specifically repairs DNA damaged by ultraviolet lightQ40806821
Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpointQ42142499
MLH1, PMS1, and MSH2 interactions during the initiation of DNA mismatch repair in yeastQ42427955
Coordination of structure-specific nucleases by human SLX4/BTBD12 is required for DNA repairQ24313572
Mammalian BTBD12/SLX4 assembles a Holliday junction resolvase and is required for DNA repairQ24314301
Human SLX4 is a Holliday junction resolvase subunit that binds multiple DNA repair/recombination endonucleasesQ24314357
XRCC1 coordinates the initial and late stages of DNA abasic site repair through protein-protein interactionsQ24535921
A bacterial two-hybrid selection system for studying protein-DNA and protein-protein interactionsQ24681782
DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiationQ24813820
Nucleotide excision repair in eukaryotesQ26850656
XRCC4 Protein Interactions with XRCC4-like Factor (XLF) Create an Extended Grooved Scaffold for DNA Ligation and Double Strand Break RepairQ27670908
A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organizationQ27930326
A novel factor required for the SUMO1/Smt3 conjugation of yeast septinsQ27930801
Slx1-Slx4 is a second structure-specific endonuclease functionally redundant with Sgs1-Top3.Q27932379
Yeast Tdp1 and Rad1-Rad10 function as redundant pathways for repairing Top1 replicative damageQ27933291
Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexesQ27933322
Microarray-based genetic screen defines SAW1, a gene required for Rad1/Rad10-dependent processing of recombination intermediatesQ27936561
Endogenous DNA abasic sites cause cell death in the absence of Apn1, Apn2 and Rad1/Rad10 in Saccharomyces cerevisiaeQ27937180
Role of Saw1 in Rad1/Rad10 complex assembly at recombination intermediates in budding yeastQ27938156
Protein group modification and synergy in the SUMO pathway as exemplified in DNA repairQ27939387
An E3-like factor that promotes SUMO conjugation to the yeast septinsQ28188846
Recombination proteins in yeastQ29617872
Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA associationQ33698685
Regulation of homologous recombination in eukaryotesQ33966065
Repair of UV damage in the fission yeast Schizosaccharomyces pombeQ33984307
Rad52 SUMOylation affects the efficiency of the DNA repairQ34058338
Complex formation with damage recognition protein Rad14 is essential for Saccharomyces cerevisiae Rad1-Rad10 nuclease to perform its function in nucleotide excision repair in vivoQ34302443
Abasic sites in DNA: repair and biological consequences in Saccharomyces cerevisiaeQ35617303
SUMOylation regulates telomere length homeostasis by targeting Cdc13.Q35794091
The Rad1-Rad10 nuclease promotes chromosome translocations between dispersed repeatsQ36236720
DNA damage checkpoint and recombinational repair differentially affect the replication stress tolerance of Smc6 mutantsQ37056627
P433issue1
P921main subjectprotein sumoylationQ3503705
P304page(s)143-152
P577publication date2014-09-25
P1433published inCell ReportsQ5058165
P1476titleA versatile scaffold contributes to damage survival via sumoylation and nuclease interactions
P478volume9

Reverse relations

cites work (P2860)
Q28551317A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation
Q36775152A new MCM modification cycle regulates DNA replication initiation
Q39192675Control of structure-specific endonucleases to maintain genome stability
Q55448530Coordination of Rad1-Rad10 interactions with Msh2-Msh3, Saw1 and RPA is essential for functional 3' non-homologous tail removal.
Q43069093Crystal structure and SUMO binding of Slx1-Slx4 complex
Q35740310DNA break-induced sumoylation is enabled by collaboration between a SUMO ligase and the ssDNA-binding complex RPA.
Q90424233Intricate SUMO-based control of the homologous recombination machinery
Q28086764SUMO-mediated regulation of DNA damage repair and responses
Q43067580Saw1 localizes to repair sites but is not required for recruitment of Rad10 to repair intermediates bearing short non-homologous 3' flaps during single-strand annealing in S. cerevisiae
Q64096515Sequence and Nuclease Requirements for Breakage and Healing of a Structure-Forming (AT)n Sequence within Fragile Site FRA16D
Q38831197Slx4 scaffolding in homologous recombination and checkpoint control: lessons from yeast.
Q35539883Sumoylation influences DNA break repair partly by increasing the solubility of a conserved end resection protein.

Search more.