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...
প্রধান লেখক: | , , |
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বিন্যাস: | Journal article |
ভাষা: | English |
প্রকাশিত: |
2004
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_version_ | 1826259421471178752 |
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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. |
first_indexed | 2024-03-06T18:49:36Z |
format | Journal article |
id | oxford-uuid:0fc44e28-0b42-41c4-829a-abfdee2e33cc |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T18:49:36Z |
publishDate | 2004 |
record_format | dspace |
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 |
work_keys_str_mv | AT parsonsj ape1isthemajor3phosphoglycolateactivityinhumancellextracts AT dianovai ape1isthemajor3phosphoglycolateactivityinhumancellextracts AT dianovg ape1isthemajor3phosphoglycolateactivityinhumancellextracts |