The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1021/acs.jnatprod.9b00405 http://hdl.handle.net/11449/195342 |
Resumo: | The culture broth of Burkholderia rinojensis strain A396 is herbicidal to a number of weed species with greater observed efficacy against broadleaf than grass weeds. A portion of this activity is attributed to romidepsin, a 16-membered cyclic depsipeptide bridged by a 15-membered macrocyclic disulfide. Romidepsin, which is present in small amounts in the broth (18 to 25 mu g mL(-1)), was isolated and purified using standard chromatographic techniques. It was established that romidepsin is a natural proherbicide that targets the activity of plant histone deacetylases (HDAC). Assays to measure plant HDAC activity were optimized by testing a number of HDAC substrates. The activity of romidepsin was greater when its macrocyclic-forming disulfide bridge was reduced to liberate a highly reactive free butenyl thiol side chain. Reduction was achieved using 200 mM tris(2-carboxyethyl)phosphine hydrochloride. A similar bioactivation of the proherbicide via reduction of the disulfide bridge of romidepsin was observed in plant-cell-free extracts. Molecular dynamic simulation of the binding of romidepsin to Arabidopsis thaliana HDAC19 indicated the reduced form of the compound could reach deep inside the catalytic domain and interact with an associated zinc atom required for enzyme activity. |
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The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis BiopesticideThe culture broth of Burkholderia rinojensis strain A396 is herbicidal to a number of weed species with greater observed efficacy against broadleaf than grass weeds. A portion of this activity is attributed to romidepsin, a 16-membered cyclic depsipeptide bridged by a 15-membered macrocyclic disulfide. Romidepsin, which is present in small amounts in the broth (18 to 25 mu g mL(-1)), was isolated and purified using standard chromatographic techniques. It was established that romidepsin is a natural proherbicide that targets the activity of plant histone deacetylases (HDAC). Assays to measure plant HDAC activity were optimized by testing a number of HDAC substrates. The activity of romidepsin was greater when its macrocyclic-forming disulfide bridge was reduced to liberate a highly reactive free butenyl thiol side chain. Reduction was achieved using 200 mM tris(2-carboxyethyl)phosphine hydrochloride. A similar bioactivation of the proherbicide via reduction of the disulfide bridge of romidepsin was observed in plant-cell-free extracts. Molecular dynamic simulation of the binding of romidepsin to Arabidopsis thaliana HDAC19 indicated the reduced form of the compound could reach deep inside the catalytic domain and interact with an associated zinc atom required for enzyme activity.USDA-ARS Material Transfer and Research AgreementMarrone BioInnovationsUSDA National Institute of Food and Agriculture, Hatch ProjectFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Colorado State Univ, Agr Biol, Ft Collins, CO 80523 USAUniv Hawaii Manoa, Mol Biosci & Bioengn, Honolulu, HI 96822 USAUSDA ARS, Nat Prod Utilizat Res Unit, Thad Cochran Ctr, University, MS 38677 USASao Paulo State Univ, Fac Agron Sci, BR-01049010 Sao Paulo, SP, BrazilMarrone Bio Innovat, Davis, CA 95618 USASao Paulo State Univ, Fac Agron Sci, BR-01049010 Sao Paulo, SP, BrazilUSDA-ARS Material Transfer and Research Agreement: 58-6408-4-009USDA National Institute of Food and Agriculture, Hatch Project: 1016591USDA National Institute of Food and Agriculture, Hatch Project: COL00785Amer Chemical SocColorado State UnivUniv Hawaii ManoaUSDA ARSUniversidade Estadual Paulista (Unesp)Marrone Bio InnovatOwens, Daniel K.Bajsa-Hirschel, JoannaDuke, Stephen O.Carbonari, Caio A. [UNESP]Gomes, Giovanna L. G. C. [UNESP]Asolkar, RatnakarBoddy, LouisDayan, Franck E.2020-12-10T17:31:14Z2020-12-10T17:31:14Z2020-04-24info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article843-851http://dx.doi.org/10.1021/acs.jnatprod.9b00405Journal Of Natural Products. Washington: Amer Chemical Soc, v. 83, n. 4, p. 843-851, 2020.0163-3864http://hdl.handle.net/11449/19534210.1021/acs.jnatprod.9b00405WOS:000529168400005Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal Of Natural Productsinfo:eu-repo/semantics/openAccess2021-10-23T07:59:06Zoai:repositorio.unesp.br:11449/195342Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T15:09:59.667996Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
title |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
spellingShingle |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide Owens, Daniel K. |
title_short |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
title_full |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
title_fullStr |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
title_full_unstemmed |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
title_sort |
The Contribution of Romidepsin to the Herbicidal Activity of Burkholderia rinojensis Biopesticide |
author |
Owens, Daniel K. |
author_facet |
Owens, Daniel K. Bajsa-Hirschel, Joanna Duke, Stephen O. Carbonari, Caio A. [UNESP] Gomes, Giovanna L. G. C. [UNESP] Asolkar, Ratnakar Boddy, Louis Dayan, Franck E. |
author_role |
author |
author2 |
Bajsa-Hirschel, Joanna Duke, Stephen O. Carbonari, Caio A. [UNESP] Gomes, Giovanna L. G. C. [UNESP] Asolkar, Ratnakar Boddy, Louis Dayan, Franck E. |
author2_role |
author author author author author author author |
dc.contributor.none.fl_str_mv |
Colorado State Univ Univ Hawaii Manoa USDA ARS Universidade Estadual Paulista (Unesp) Marrone Bio Innovat |
dc.contributor.author.fl_str_mv |
Owens, Daniel K. Bajsa-Hirschel, Joanna Duke, Stephen O. Carbonari, Caio A. [UNESP] Gomes, Giovanna L. G. C. [UNESP] Asolkar, Ratnakar Boddy, Louis Dayan, Franck E. |
description |
The culture broth of Burkholderia rinojensis strain A396 is herbicidal to a number of weed species with greater observed efficacy against broadleaf than grass weeds. A portion of this activity is attributed to romidepsin, a 16-membered cyclic depsipeptide bridged by a 15-membered macrocyclic disulfide. Romidepsin, which is present in small amounts in the broth (18 to 25 mu g mL(-1)), was isolated and purified using standard chromatographic techniques. It was established that romidepsin is a natural proherbicide that targets the activity of plant histone deacetylases (HDAC). Assays to measure plant HDAC activity were optimized by testing a number of HDAC substrates. The activity of romidepsin was greater when its macrocyclic-forming disulfide bridge was reduced to liberate a highly reactive free butenyl thiol side chain. Reduction was achieved using 200 mM tris(2-carboxyethyl)phosphine hydrochloride. A similar bioactivation of the proherbicide via reduction of the disulfide bridge of romidepsin was observed in plant-cell-free extracts. Molecular dynamic simulation of the binding of romidepsin to Arabidopsis thaliana HDAC19 indicated the reduced form of the compound could reach deep inside the catalytic domain and interact with an associated zinc atom required for enzyme activity. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-12-10T17:31:14Z 2020-12-10T17:31:14Z 2020-04-24 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1021/acs.jnatprod.9b00405 Journal Of Natural Products. Washington: Amer Chemical Soc, v. 83, n. 4, p. 843-851, 2020. 0163-3864 http://hdl.handle.net/11449/195342 10.1021/acs.jnatprod.9b00405 WOS:000529168400005 |
url |
http://dx.doi.org/10.1021/acs.jnatprod.9b00405 http://hdl.handle.net/11449/195342 |
identifier_str_mv |
Journal Of Natural Products. Washington: Amer Chemical Soc, v. 83, n. 4, p. 843-851, 2020. 0163-3864 10.1021/acs.jnatprod.9b00405 WOS:000529168400005 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal Of Natural Products |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
843-851 |
dc.publisher.none.fl_str_mv |
Amer Chemical Soc |
publisher.none.fl_str_mv |
Amer Chemical Soc |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
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1808128472332107776 |