APE1 is the major 3'-phosphoglycolate activity in human cell extracts.

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...

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প্রধান লেখক: Parsons, J, Dianova, I, Dianov, G
বিন্যাস: Journal article
ভাষা:English
প্রকাশিত: 2004
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author Parsons, J
Dianova, I
Dianov, G
author_facet Parsons, J
Dianova, I
Dianov, G
author_sort Parsons, J
collection OXFORD
description 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.
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spelling oxford-uuid:0fc44e28-0b42-41c4-829a-abfdee2e33cc2022-03-26T09:52:50ZAPE1 is the major 3'-phosphoglycolate activity in human cell extracts.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:0fc44e28-0b42-41c4-829a-abfdee2e33ccEnglishSymplectic Elements at Oxford2004Parsons, JDianova, IDianov, GDNA 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.
spellingShingle Parsons, J
Dianova, I
Dianov, G
APE1 is the major 3'-phosphoglycolate activity in human cell extracts.
title APE1 is the major 3'-phosphoglycolate activity in human cell extracts.
title_full APE1 is the major 3'-phosphoglycolate activity in human cell extracts.
title_fullStr APE1 is the major 3'-phosphoglycolate activity in human cell extracts.
title_full_unstemmed APE1 is the major 3'-phosphoglycolate activity in human cell extracts.
title_short APE1 is the major 3'-phosphoglycolate activity in human cell extracts.
title_sort ape1 is the major 3 phosphoglycolate activity in human cell extracts
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