Pnkp is a bifunctional enzyme: 2,3' cyclic phosphate and 5-OH ends are substrates for healing and sealing by Pnkp and Hen1, The 5' end is phosphorylated by the Pnkp kinase and the 2',3' cyclic phosphate is removed by the Pnkp phosphatase
Pnkp is a bifunctional enzyme: 2,3' cyclic phosphate and 5-OH ends are substrates for healing and sealing by Pnkp and Hen1, The 5' end is phosphorylated by the Pnkp kinase and the 2',3' cyclic phosphate is removed by the Pnkp phosphatase
PALF nuclease activity acts on single-stranded DNA or overhangs of duplex substrates. PALF does not open DNA hairpins. Reduction of PALF in vivo reduces the joining of incompatible DNA ends, PALF can function in concert with other nonhomologous DNA end joining proteins. PALF is able to resect 3 overhanging nucleotides and permit XRCC4-DNA ligase IV to complete the joining process in a manner that is as efficient as Artemis. Role for polynucleotide kinase and aprataxin-like forkhead-associated, PALF, in nonhomologous DNA end joining
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP forkhead-associated domain to phosphorylated motifs on XRCC1 and XRCC4, overview. Phosphorylation-independent interaction between PNKP and XRCC1 in human cells, since a non-phosphorylated XRCC1S518A/T519A/T523A triple mutant is also bound
PNKP function is modulated by interaction with the DNA repair scaffold proteins XRCC1 and XRCC4, which is mediated by binding of the PNKP forkhead-associated domain to phosphorylated motifs on XRCC1 and XRCC4, overview
in vivo role is possibly in maintaining DNA or RNA in the 5'-phosphorylated 3'-hydroxylated state which is the substrate for many reactions such as ligation and packaging
the enzyme catalyzes both, the phosphorylation of 5-hydroxyl termini and the hydrolysis of 3-phosphomonoesters and 2,3-cyclic phosphodiesters of polynucleotides
the enzyme catalyzes both, the phosphorylation of 5-hydroxyl termini and the hydrolysis of 3-phosphomonoesters and 2,3-cyclic phosphodiesters of polynucleotides