XRS2 Antibody

1. Xrs2 dependent and independent functions of the Mre11-Rad50 complex orchestrating the cellular response to double-strand DNA breaks have been described. PMID: 27746018
2. The Saccharomyces cerevisiae Mre11-Rad50-Xrs2 complex promotes trinucleotide repeat expansions independently of homologous recombination. PMID: 27173583
3. Phosphorylation sites on Xrs2 that are required for MMS resistance were identified. PMID: 27017623
4. Mre11 recruits conjugated SUMO moieties to facilitate the assembly and function of the Mre11-Rad50-Xrs2 complex. PMID: 26743002
5. the Xrs2 FHA domain and Tel1 kinase work in a coordinated manner to maintain DSB repair fidelity. PMID: 26990569
6. the mechanisms of DNA end resection in Saccharomyces cerevisiae, which includes short-range resection by Mre11-Rad50-Xrs2 and Sae2, as well as processive long-range resection by Sgs1-Dna2 or Exo1 pathways. PMID: 26231213
7. Data suggest that the major function of Sae2 in response to DNA double-strand breaks (DSBs) is to actively remove Mre11-Rad50-Xrs2 from break ends and prevent Rad53 in response to DSBs. PMID: 25831494
8. To our surprise, genes encoding the Mre11-Rad50-Xrs2 (MRX) complex, which are also required for homologous recombination, are epistatic to TLS mutations PMID: 25343618
9. Sae2 promotes dsDNA-specific endonuclease activity by the Mre11 subunit within the Mre11-Rad50-Xrs2 (MRX) complex PMID: 25231868
10. Processing of DNA double-stranded breaks and intermediates of recombination and repair by Saccharomyces cerevisiae Mre11 and its stimulation by Rad50, Xrs2, and Sae2 proteins. PMID: 23443654
11. A pivotal role for the MRX (Mre11, Rad50, Xrs2) complex for fork integrity at replication forks. PMID: 23376930
12. interaction with Xrs2 may enable Pch2 to remodel chromosome structure adjacent to the site of a DSB and thereby promote accessibility of Hop1 to the Tel1 kinase PMID: 22072981
13. a direct role for the Mre11-Rad50-Xrs2 complex in the base excision repair process, which contributes to resistance against base-damaging agents and to the avoidance of mutations PMID: 20040573
14. total amount of Xrs2 protein is a critical determinant for the function of the Mre11/Rad50/Xrs2 complex especially with regard to telomere maintenance and meiotic DSB formation PMID: 15716496
15. confirmed that signal joint formation in yeast is dependent on the same Mre11p-Rad50p-Xrs2p (MRX) complex factors known to be required in mammalian cells PMID: 15757898
16. MRX (Mre11/Rad50/Xrs2) is not required for the intra-S-phase checkpoint in response to DNA alkylation damage, but is required in the presence of double-stranded DNA breaks PMID: 15970664
17. The Mre11/Rad50/Xrs2 (MRX) complex is essential for joining of incompatible ends by non-homologous end-joining during DNA repair. PMID: 16043424
18. Individual and combined deletions of the Yku80 C terminus and the Xrs2 forkhead-associated (FHA) domain were shown to block nonhomologous end joining. PMID: 16314503
19. expression of EcoRI activated the G1 and intra-S phase checkpoints in a MRX- and Mec1-dependent, but Tel1-independent manner. PMID: 16879433
20. Data show that the Saccharomyces cerevisiae MRX complex, or its subunits Mre11/Rad50/Xrs2, prefer G-quadruplex DNA much more than telomeric single-stranded or double-stranded DNA, implicating the possible existence of this DNA structure in vivo. PMID: 17698079
21. Recombinant Sae2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. PMID: 18042458
22. Forkhead-associated domain of yeast Xrs2, a homolog of human Nbs1, promotes nonhomologous end joining through interaction with a ligase IV partner protein, Lif1. PMID: 18458108
23. the Xrs2-Lif1 interaction depends on Xrs2 FHA residues (R32, S47, R48, and K75) analogous to those known in other proteins to contact phosphorylated threonines PMID: 18832348

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KEGG: sce:YDR369C

STRING: 4932.YDR369C