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dc.contributor.authorDurand, Mathieu
dc.contributor.authorKolpak, Adrianne L.
dc.contributor.authorFarrell, Timothy
dc.contributor.authorElliott, Nathan Andrew
dc.contributor.authorShao, Wenlin
dc.contributor.authorBrown, Myles A.
dc.contributor.authorVolkert, Michael R.
dc.date2022-08-11T08:08:57.000
dc.date.accessioned2022-08-23T16:13:38Z
dc.date.available2022-08-23T16:13:38Z
dc.date.issued2007-03-30
dc.date.submitted2008-09-04
dc.identifier.citationBMC Cell Biol. 2007 Mar 28;8:13. <a href="http://dx.doi.org/10.1186/1471-2121-8-13">Link to article on publisher's site</a>
dc.identifier.issn1471-2121 (Electronic)
dc.identifier.doi10.1186/1471-2121-8-13
dc.identifier.pmid17391516
dc.identifier.urihttp://hdl.handle.net/20.500.14038/33670
dc.description.abstractBACKGROUND: The NCOA7 gene product is an estrogen receptor associated protein that is highly similar to the human OXR1 gene product, which functions in oxidation resistance. OXR genes are conserved among all sequenced eukaryotes from yeast to humans. In this study we examine if NCOA7 has an oxidation resistance function similar to that demonstrated for OXR1. We also examine NCOA7 expression in response to oxidative stress and its subcellular localization in human cells, comparing these properties with those of OXR1. RESULTS: We find that NCOA7, like OXR1 can suppress the oxidative mutator phenotype when expressed in an E. coli strain that exhibits an oxidation specific mutator phenotype. Moreover, NCOA7's oxidation resistance function requires expression of only its carboxyl-terminal domain and is similar in this regard to OXR1. We find that, in human cells, NCOA7 is constitutively expressed and is not induced by oxidative stress and appears to localize to the nucleus following estradiol stimulation. These properties of NCOA7 are in striking contrast to those of OXR1, which is induced by oxidative stress, localizes to mitochondria, and appears to be excluded, or largely absent from nuclei. CONCLUSION: NCOA7 most likely arose from duplication. Like its homologue, OXR1, it is capable of reducing the DNA damaging effects of reactive oxygen species when expressed in bacteria, indicating the protein has an activity that can contribute to oxidation resistance. Unlike OXR1, it appears to localize to nuclei and interacts with the estrogen receptor. This raises the possibility that NCOA7 encodes the nuclear counterpart of the mitochondrial OXR1 protein and in mammalian cells it may reduce the oxidative by-products of estrogen metabolite-mediated DNA damage.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17391516&dopt=Abstract">Link to article in PubMed</a>
dc.subjectCell Nucleus; Conserved Sequence; DNA Damage; Escherichia coli; Eukaryotic Cells; Gene Expression Regulation; Humans; Hydrogen Peroxide; Intracellular Signaling Peptides and; Proteins; Multigene Family; *Oxidative Stress; Protein Structure, Tertiary; Proteins; Tumor Cells, Cultured
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleThe OXR domain defines a conserved family of eukaryotic oxidation resistance proteins
dc.typeJournal Article
dc.source.journaltitleBMC cell biology
dc.source.volume8
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1334&amp;context=gsbs_sp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/335
dc.identifier.contextkey619047
refterms.dateFOA2022-08-23T16:13:38Z
html.description.abstract<p>BACKGROUND: The NCOA7 gene product is an estrogen receptor associated protein that is highly similar to the human OXR1 gene product, which functions in oxidation resistance. OXR genes are conserved among all sequenced eukaryotes from yeast to humans. In this study we examine if NCOA7 has an oxidation resistance function similar to that demonstrated for OXR1. We also examine NCOA7 expression in response to oxidative stress and its subcellular localization in human cells, comparing these properties with those of OXR1.</p> <p>RESULTS: We find that NCOA7, like OXR1 can suppress the oxidative mutator phenotype when expressed in an E. coli strain that exhibits an oxidation specific mutator phenotype. Moreover, NCOA7's oxidation resistance function requires expression of only its carboxyl-terminal domain and is similar in this regard to OXR1. We find that, in human cells, NCOA7 is constitutively expressed and is not induced by oxidative stress and appears to localize to the nucleus following estradiol stimulation. These properties of NCOA7 are in striking contrast to those of OXR1, which is induced by oxidative stress, localizes to mitochondria, and appears to be excluded, or largely absent from nuclei.</p> <p>CONCLUSION: NCOA7 most likely arose from duplication. Like its homologue, OXR1, it is capable of reducing the DNA damaging effects of reactive oxygen species when expressed in bacteria, indicating the protein has an activity that can contribute to oxidation resistance. Unlike OXR1, it appears to localize to nuclei and interacts with the estrogen receptor. This raises the possibility that NCOA7 encodes the nuclear counterpart of the mitochondrial OXR1 protein and in mammalian cells it may reduce the oxidative by-products of estrogen metabolite-mediated DNA damage.</p>
dc.identifier.submissionpathgsbs_sp/335
dc.contributor.departmentDepartment of Molecular Genetics and Microbiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages13


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