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Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction
BACKGROUND: Topo-poisons can produce an enzyme-DNA complex linked by a 3'- or 5'-phosphotyrosyl covalent bond. 3'-phosphotyrosyl bonds can be repaired by tyrosyl DNA phosphodiesterase-1 (TDP1), an enzyme known for years, but a complementary human enzyme 5'-tyrosyl DNA phosphodies...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315744/ https://www.ncbi.nlm.nih.gov/pubmed/22405347 http://dx.doi.org/10.1186/1756-0500-5-134 |
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author | Adhikari, Sanjay Karmahapatra, Soumendra K Karve, Tejaswita M Bandyopadhyay, Sanjona Woodrick, Jordan Manthena, Praveen V Glasgow, Eric Byers, Stephen Saha, Tapas Uren, Aykut |
author_facet | Adhikari, Sanjay Karmahapatra, Soumendra K Karve, Tejaswita M Bandyopadhyay, Sanjona Woodrick, Jordan Manthena, Praveen V Glasgow, Eric Byers, Stephen Saha, Tapas Uren, Aykut |
author_sort | Adhikari, Sanjay |
collection | PubMed |
description | BACKGROUND: Topo-poisons can produce an enzyme-DNA complex linked by a 3'- or 5'-phosphotyrosyl covalent bond. 3'-phosphotyrosyl bonds can be repaired by tyrosyl DNA phosphodiesterase-1 (TDP1), an enzyme known for years, but a complementary human enzyme 5'-tyrosyl DNA phosphodiesterase (hTDP2) that cleaves 5'-phosphotyrosyl bonds has been reported only recently. Although hTDP2 possesses both 3'- and 5'- tyrosyl DNA phosphodiesterase activity, the role of Mg(2+ )in its activity was not studied in sufficient details. RESULTS: In this study we showed that purified hTDP2 does not exhibit any 5'-phosphotyrosyl phosphodiesterase activity in the absence of Mg(2+)/Mn(2+), and that neither Zn(2+ )or nor Ca(2+ )can activate hTDP2. Mg(2+ )also controls 3'-phosphotyrosyl activity of TDP2. In MCF-7 cell extracts and de-yolked zebrafish embryo extracts, Mg(2+ )controlled 5'-phosphotyrosyl activity. This study also showed that there is an optimal Mg(2+ )concentration above which it is inhibitory for hTDP2 activity. CONCLUSION: These results altogether reveal the optimal Mg(2+ )requirement in hTDP2 mediated reaction. |
format | Online Article Text |
id | pubmed-3315744 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-33157442012-03-31 Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction Adhikari, Sanjay Karmahapatra, Soumendra K Karve, Tejaswita M Bandyopadhyay, Sanjona Woodrick, Jordan Manthena, Praveen V Glasgow, Eric Byers, Stephen Saha, Tapas Uren, Aykut BMC Res Notes Research Article BACKGROUND: Topo-poisons can produce an enzyme-DNA complex linked by a 3'- or 5'-phosphotyrosyl covalent bond. 3'-phosphotyrosyl bonds can be repaired by tyrosyl DNA phosphodiesterase-1 (TDP1), an enzyme known for years, but a complementary human enzyme 5'-tyrosyl DNA phosphodiesterase (hTDP2) that cleaves 5'-phosphotyrosyl bonds has been reported only recently. Although hTDP2 possesses both 3'- and 5'- tyrosyl DNA phosphodiesterase activity, the role of Mg(2+ )in its activity was not studied in sufficient details. RESULTS: In this study we showed that purified hTDP2 does not exhibit any 5'-phosphotyrosyl phosphodiesterase activity in the absence of Mg(2+)/Mn(2+), and that neither Zn(2+ )or nor Ca(2+ )can activate hTDP2. Mg(2+ )also controls 3'-phosphotyrosyl activity of TDP2. In MCF-7 cell extracts and de-yolked zebrafish embryo extracts, Mg(2+ )controlled 5'-phosphotyrosyl activity. This study also showed that there is an optimal Mg(2+ )concentration above which it is inhibitory for hTDP2 activity. CONCLUSION: These results altogether reveal the optimal Mg(2+ )requirement in hTDP2 mediated reaction. BioMed Central 2012-03-09 /pmc/articles/PMC3315744/ /pubmed/22405347 http://dx.doi.org/10.1186/1756-0500-5-134 Text en Copyright ©2011 Adhikari et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Adhikari, Sanjay Karmahapatra, Soumendra K Karve, Tejaswita M Bandyopadhyay, Sanjona Woodrick, Jordan Manthena, Praveen V Glasgow, Eric Byers, Stephen Saha, Tapas Uren, Aykut Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction |
title | Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction |
title_full | Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction |
title_fullStr | Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction |
title_full_unstemmed | Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction |
title_short | Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction |
title_sort | characterization of magnesium requirement of human 5'-tyrosyl dna phosphodiesterase mediated reaction |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3315744/ https://www.ncbi.nlm.nih.gov/pubmed/22405347 http://dx.doi.org/10.1186/1756-0500-5-134 |
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