Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725

21 p.-14 fig.-2 tab.

Detalles Bibliográficos
Autores: Ibero, Juan, Galán, Beatriz, Rivero-Buceta, Virginia, García, José Luis
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/235015
Acceso en línea:http://hdl.handle.net/10261/235015
Access Level:acceso abierto
Palabra clave:Estrogens
Catabolism
Bacteria
Biodegradation
17b-estradiol
Cytochrome P450
E1-hydroxylase
Estrogen transport
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spelling Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725Ibero, JuanGalán, BeatrizRivero-Buceta, VirginiaGarcía, José LuisEstrogensCatabolismBacteriaBiodegradation17b-estradiolCytochrome P450E1-hydroxylaseEstrogen transport21 p.-14 fig.-2 tab.We have analyzed the catabolism of estrogens in Novosphingobium tardaugens NBRC 16725, which is able to use endocrine disruptors such as 17β-estradiol, estrone, and estriol as sole carbon and energy sources. A transcriptomic analysis enabled the identification of a cluster of catabolic genes (edc cluster) organized in two divergent operons that are involved in estrogen degradation. We have developed genetic tools for this estrogen-degrading bacterium, allowing us to delete by site-directed mutagenesis some of the genes of the edc cluster and complement them by using expression plasmids to better characterize their precise role in the estrogen catabolism. Based on these results, a catabolic pathway is proposed. The first enzyme of the pathway (17β-hydroxysteroid dehydrogenase) used to transform 17β-estradiol into estrone is encoded out of the cluster. A CYP450 encoded by the edcA gene performs the second metabolic step, i.e., the 4-hydroxylation of estrone in this strain. The edcB gene encodes a 4-hydroxyestrone-4,5-dioxygenase that opens ring A after 4-hydroxylation. The initial steps of the catabolism of estrogens and cholate proceed through different pathways. However, the degradation of estrogens converges with the degradation of testosterone in the final steps of the lower catabolic pathway used to degrade the common intermediate 3aα-H-4α(3′-propanoate)7a-β-methylhexahydro-1,5-indanedione (HIP). The TonB-dependent receptor protein EdcT appears to be involved in estrogen uptake, being the first time that this kind of proteins has been involved in steroid transport.This work was supported by the Ramon Areces Foundation (ELISA project).Peer reviewedFrontiers MediaFundación Ramón ArecesIbero, Juan [0000-0002-6934-8334]Galán, Beatriz [0000-0002-2596-6034]Rivero-Buceta, Virginia [0000-0002-5658-1997]García, José Luis [0000-0002-9238-2485]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202120212020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/235015reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.3389/fmicb.2020.588300Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2350152026-05-22T06:33:51Z
dc.title.none.fl_str_mv Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
title Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
spellingShingle Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
Ibero, Juan
Estrogens
Catabolism
Bacteria
Biodegradation
17b-estradiol
Cytochrome P450
E1-hydroxylase
Estrogen transport
title_short Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
title_full Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
title_fullStr Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
title_full_unstemmed Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
title_sort Unraveling the 17β-estradiol degradation pathway in Novosphingobium tardaugens NBRC 16725
dc.creator.none.fl_str_mv Ibero, Juan
Galán, Beatriz
Rivero-Buceta, Virginia
García, José Luis
author Ibero, Juan
author_facet Ibero, Juan
Galán, Beatriz
Rivero-Buceta, Virginia
García, José Luis
author_role author
author2 Galán, Beatriz
Rivero-Buceta, Virginia
García, José Luis
author2_role author
author
author
dc.contributor.none.fl_str_mv Fundación Ramón Areces
Ibero, Juan [0000-0002-6934-8334]
Galán, Beatriz [0000-0002-2596-6034]
Rivero-Buceta, Virginia [0000-0002-5658-1997]
García, José Luis [0000-0002-9238-2485]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Estrogens
Catabolism
Bacteria
Biodegradation
17b-estradiol
Cytochrome P450
E1-hydroxylase
Estrogen transport
topic Estrogens
Catabolism
Bacteria
Biodegradation
17b-estradiol
Cytochrome P450
E1-hydroxylase
Estrogen transport
description 21 p.-14 fig.-2 tab.
publishDate 2020
dc.date.none.fl_str_mv 2020
2021
2021
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/235015
url http://hdl.handle.net/10261/235015
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.3389/fmicb.2020.588300

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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