APE1 is the major 3′-phosphoglycolate activity in human cell extracts
AUTOR(ES)
Parsons, Jason L.
FONTE
Oxford University Press
RESUMO
DNA strand breaks containing 3′-phosphoglycolate (3′-PG) ends are the major lesions induced by ionizing radiation. The repair of this lesion is not completely understood and several activities are thought to be involved in processing of 3′-PG ends. In this study we examined activities in human whole cell extracts (WCE) responsible for removal of 3′-PG. Using a radiolabelled oligonucleotide containing a single nucleotide gap with internal 5′-phosphate and 3′-PG ends, we demonstrate that the major 3′-PG activity in human WCE is Mg2+ dependent and that this activity co-purifies with AP endonuclease 1 (APE1) over phosphocellulose and gel filtration chromatography. Furthermore, immunodepletion of APE1 from active gel filtration fractions using APE1 specific antibodies reveals that the major activity against 3′-PG in human WCE is APE1.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=484167Documentos Relacionados
- Functional characterization of Ape1 variants identified in the human population
- Deficiency in 3′-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)
- Removal of 3'-phosphoglycolate from DNA strand-break damage in an oligonucleotide substrate by recombinant human apurinic/apyrimidinic endonuclease 1.
- DNA strand breaks produced by oxidative stress in mammalian cells exhibit 3'-phosphoglycolate termini.
- The major human AP endonuclease (Ape1) is involved in the nucleotide incision repair pathway