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Literature summary extracted from

  • Li, S.; Kanno, S.; Watanabe, R.; Ogiwara, H.; Kohno, T.; Watanabe, G.; Yasui, A.; Lieber, M.R.
    Polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3 exonuclease and can participate in DNA end joining in a biochemical system (2011), J. Biol. Chem., 286, 36368-36377.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.78 expression of N-terminally His-tagged polynucleotide kinase and aprataxin-like forkhead-associated in Escherichia coli strain BL21(DE3) Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.78 Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.78 ATP + 5'-dephospho-DNA Homo sapiens
-
ADP + 5'-phospho-DNA
-
?
2.7.1.78 additional information Homo sapiens 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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.78 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.78 recombinant N-terminally His-tagged polynucleotide kinase and aprataxin-like forkhead-associated from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.78 ATP + 5'-dephospho-DNA
-
Homo sapiens ADP + 5'-phospho-DNA
-
?
2.7.1.78 additional information 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 Homo sapiens ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.78 PALF
-
Homo sapiens
2.7.1.78 PNK
-
Homo sapiens
2.7.1.78 polynucleotide kinase and aprataxin-like forkhead-associated
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.78 37
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.78 7.5
-
assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.78 ATP
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.1.78 malfunction knockdown of polynucleotide kinase and aprataxin-like forkhead-associated using siRNA reduces rejoining of two incompatible I-SceI-generated DNA ends by 50% Homo sapiens
2.7.1.78 additional information the nuclease activity of polynucleotide kinase and aprataxin-like forkhead-associated is not affected by Ku or XRCC4-DNA ligase IV Homo sapiens
2.7.1.78 physiological function polynucleotide kinase and aprataxin-like forkhead-associated protein (PALF) acts as both a single-stranded DNA endonuclease and a single-stranded DNA 3 exonuclease and can participate in DNA end joining in a biochemical system, they use the forkhead-associated domain to bind to x-ray repair complementing defective repair in Chinese hamster cells 4, XRCC4, overview Homo sapiens