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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...

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Autores principales: Adhikari, Sanjay, Karmahapatra, Soumendra K, Karve, Tejaswita M, Bandyopadhyay, Sanjona, Woodrick, Jordan, Manthena, Praveen V, Glasgow, Eric, Byers, Stephen, Saha, Tapas, Uren, Aykut
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
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.
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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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