Title : Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2 FHA domain.

Pub. Date : 2008 Dec

PMID : 18832348






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 We next show that 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. Threonine Lif1p Saccharomyces cerevisiae S288C
2 Two potential target threonines in Lif1 (T417 and T387) were inferred by identifying regions similar to a site in the human Lif1 homolog, XRCC4, known to be bound by the FHA domain of polynucleotide kinase. Threonine Lif1p Saccharomyces cerevisiae S288C
3 Two potential target threonines in Lif1 (T417 and T387) were inferred by identifying regions similar to a site in the human Lif1 homolog, XRCC4, known to be bound by the FHA domain of polynucleotide kinase. Threonine Lif1p Saccharomyces cerevisiae S288C
4 Mutating these threonines, especially T417, abolished the Xrs2-Lif1 interaction and impaired NHEJ epistatically with Xrs2 FHA mutation. Threonine Lif1p Saccharomyces cerevisiae S288C