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RecA stimulates AlkB-mediated direct repair of DNA adducts
The Escherichia coli AlkB protein is a 2-oxoglutarate/Fe(II)-dependent demethylase that repairs alkylated single stranded and double stranded DNA. Immunoaffinity chromatography coupled with mass spectrometry identified RecA, a key factor in homologous recombination, as an AlkB-associated protein. Th...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062977/ https://www.ncbi.nlm.nih.gov/pubmed/27378775 http://dx.doi.org/10.1093/nar/gkw611 |
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author | Shivange, Gururaj Monisha, Mohan Nigam, Richa Kodipelli, Naveena Anindya, Roy |
author_facet | Shivange, Gururaj Monisha, Mohan Nigam, Richa Kodipelli, Naveena Anindya, Roy |
author_sort | Shivange, Gururaj |
collection | PubMed |
description | The Escherichia coli AlkB protein is a 2-oxoglutarate/Fe(II)-dependent demethylase that repairs alkylated single stranded and double stranded DNA. Immunoaffinity chromatography coupled with mass spectrometry identified RecA, a key factor in homologous recombination, as an AlkB-associated protein. The interaction between AlkB and RecA was validated by yeast two-hybrid assay; size-exclusion chromatography and standard pull down experiment and was shown to be direct and mediated by the N-terminal domain of RecA. RecA binding results AlkB–RecA heterodimer formation and RecA–AlkB repairs alkylated DNA with higher efficiency than AlkB alone. |
format | Online Article Text |
id | pubmed-5062977 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-50629772016-10-14 RecA stimulates AlkB-mediated direct repair of DNA adducts Shivange, Gururaj Monisha, Mohan Nigam, Richa Kodipelli, Naveena Anindya, Roy Nucleic Acids Res Genome Integrity, Repair and Replication The Escherichia coli AlkB protein is a 2-oxoglutarate/Fe(II)-dependent demethylase that repairs alkylated single stranded and double stranded DNA. Immunoaffinity chromatography coupled with mass spectrometry identified RecA, a key factor in homologous recombination, as an AlkB-associated protein. The interaction between AlkB and RecA was validated by yeast two-hybrid assay; size-exclusion chromatography and standard pull down experiment and was shown to be direct and mediated by the N-terminal domain of RecA. RecA binding results AlkB–RecA heterodimer formation and RecA–AlkB repairs alkylated DNA with higher efficiency than AlkB alone. Oxford University Press 2016-10-14 2016-07-04 /pmc/articles/PMC5062977/ /pubmed/27378775 http://dx.doi.org/10.1093/nar/gkw611 Text en © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Genome Integrity, Repair and Replication Shivange, Gururaj Monisha, Mohan Nigam, Richa Kodipelli, Naveena Anindya, Roy RecA stimulates AlkB-mediated direct repair of DNA adducts |
title | RecA stimulates AlkB-mediated direct repair of DNA adducts |
title_full | RecA stimulates AlkB-mediated direct repair of DNA adducts |
title_fullStr | RecA stimulates AlkB-mediated direct repair of DNA adducts |
title_full_unstemmed | RecA stimulates AlkB-mediated direct repair of DNA adducts |
title_short | RecA stimulates AlkB-mediated direct repair of DNA adducts |
title_sort | reca stimulates alkb-mediated direct repair of dna adducts |
topic | Genome Integrity, Repair and Replication |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5062977/ https://www.ncbi.nlm.nih.gov/pubmed/27378775 http://dx.doi.org/10.1093/nar/gkw611 |
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