DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana

Detalhes bibliográficos
Autor(a) principal: Zhang, Jun
Data de Publicação: 2016
Outros Autores: Lin, Jinshan Ella, Harris, Chinchu, Pereira, Fernanda Campos Mastrotti [UNESP], Wu, Fan, Blakeslee, Joshua J., Peer, Wendy Ann
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1073/pnas.1604769113
http://hdl.handle.net/11449/220703
Resumo: Tight homeostatic regulation of the phytohormone auxin [indole-3-acetic acid (IAA)] is essential to plant growth. Auxin biosynthetic pathways and the processes that inactivate auxin by conjugation to amino acids and sugars have been thoroughly characterized. However, the enzyme that catalyzes oxidation of IAA to its primary catabolite 2-oxindole-3-acetic acid (oxIAA) remains uncharacterized. Here, we show that DIOXYGENASE FOR AUXIN OXIDATION 1 (DAO1) catalyzes formation of oxIAA in vitro and in vivo and that this mechanism regulates auxin homeostasis and plant growth. Null dao1-1 mutants contain 95% less oxIAA compared with wild type, and complementation of dao1 restores wild-type oxIAA levels, indicating that DAO1 is the primary IAA oxidase in seedlings. Furthermore, dao1 loss of function plants have altered morphology, including larger cotyledons, increased lateral root density, delayed sepal opening, elongated pistils, and reduced fertility in the primary inflorescence stem. These phenotypes are tightly correlated with DAO1 spatiotemporal expression patterns as shown by DAO1pro:β-glucuronidase (GUS) activity and DAO1pro:YFP-DAO1 signals, and transformation with DAO1pro:YFP-DAO1 complemented the mutant phenotypes. The dominant dao1-2D mutant has increased oxIAA levels and decreased stature with shorter leaves and inflorescence stems, thus supporting DAO1 IAA oxidase function in vivo. A second isoform, DAO2, is very weakly expressed in seedling root apices. Together, these data confirm that IAA oxidation by DAO1 is the principal auxin catabolic process in Arabidopsis and that localized IAA oxidation plays a role in plant morphogenesis.
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spelling DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thalianaAuxin homeostasisAuxin oxidaseAuxin oxidationFlowersLateral rootsTight homeostatic regulation of the phytohormone auxin [indole-3-acetic acid (IAA)] is essential to plant growth. Auxin biosynthetic pathways and the processes that inactivate auxin by conjugation to amino acids and sugars have been thoroughly characterized. However, the enzyme that catalyzes oxidation of IAA to its primary catabolite 2-oxindole-3-acetic acid (oxIAA) remains uncharacterized. Here, we show that DIOXYGENASE FOR AUXIN OXIDATION 1 (DAO1) catalyzes formation of oxIAA in vitro and in vivo and that this mechanism regulates auxin homeostasis and plant growth. Null dao1-1 mutants contain 95% less oxIAA compared with wild type, and complementation of dao1 restores wild-type oxIAA levels, indicating that DAO1 is the primary IAA oxidase in seedlings. Furthermore, dao1 loss of function plants have altered morphology, including larger cotyledons, increased lateral root density, delayed sepal opening, elongated pistils, and reduced fertility in the primary inflorescence stem. These phenotypes are tightly correlated with DAO1 spatiotemporal expression patterns as shown by DAO1pro:β-glucuronidase (GUS) activity and DAO1pro:YFP-DAO1 signals, and transformation with DAO1pro:YFP-DAO1 complemented the mutant phenotypes. The dominant dao1-2D mutant has increased oxIAA levels and decreased stature with shorter leaves and inflorescence stems, thus supporting DAO1 IAA oxidase function in vivo. A second isoform, DAO2, is very weakly expressed in seedling root apices. Together, these data confirm that IAA oxidation by DAO1 is the principal auxin catabolic process in Arabidopsis and that localized IAA oxidation plays a role in plant morphogenesis.Department of Plant Science and Landscape Architecture University of MarylandDepartment of Horticulture and Crop Science Ohio Agricultural Research and Development Center Ohio State UniversityOhio Agricultural Research and Development Center Metabolite Analysis Cluster Ohio Agricultural Research and Development Center The Ohio State UniversityDepartment of Environmental Science and Technology University of MarylandPlant Protection and Animal Health Forestry Agronomy Universidade Estadual de São PauloPlant Protection and Animal Health Forestry Agronomy Universidade Estadual de São PauloUniversity of MarylandOhio State UniversityUniversidade Estadual Paulista (UNESP)Zhang, JunLin, Jinshan EllaHarris, ChinchuPereira, Fernanda Campos Mastrotti [UNESP]Wu, FanBlakeslee, Joshua J.Peer, Wendy Ann2022-04-28T19:04:54Z2022-04-28T19:04:54Z2016-09-27info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article11010-11015http://dx.doi.org/10.1073/pnas.1604769113Proceedings of the National Academy of Sciences of the United States of America, v. 113, n. 39, p. 11010-11015, 2016.1091-64900027-8424http://hdl.handle.net/11449/22070310.1073/pnas.16047691132-s2.0-84989874686Scopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengProceedings of the National Academy of Sciences of the United States of Americainfo:eu-repo/semantics/openAccess2022-04-28T19:04:54Zoai:repositorio.unesp.br:11449/220703Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-05-23T11:48:09.124379Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
title DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
spellingShingle DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
Zhang, Jun
Auxin homeostasis
Auxin oxidase
Auxin oxidation
Flowers
Lateral roots
title_short DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
title_full DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
title_fullStr DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
title_full_unstemmed DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
title_sort DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
author Zhang, Jun
author_facet Zhang, Jun
Lin, Jinshan Ella
Harris, Chinchu
Pereira, Fernanda Campos Mastrotti [UNESP]
Wu, Fan
Blakeslee, Joshua J.
Peer, Wendy Ann
author_role author
author2 Lin, Jinshan Ella
Harris, Chinchu
Pereira, Fernanda Campos Mastrotti [UNESP]
Wu, Fan
Blakeslee, Joshua J.
Peer, Wendy Ann
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv University of Maryland
Ohio State University
Universidade Estadual Paulista (UNESP)
dc.contributor.author.fl_str_mv Zhang, Jun
Lin, Jinshan Ella
Harris, Chinchu
Pereira, Fernanda Campos Mastrotti [UNESP]
Wu, Fan
Blakeslee, Joshua J.
Peer, Wendy Ann
dc.subject.por.fl_str_mv Auxin homeostasis
Auxin oxidase
Auxin oxidation
Flowers
Lateral roots
topic Auxin homeostasis
Auxin oxidase
Auxin oxidation
Flowers
Lateral roots
description Tight homeostatic regulation of the phytohormone auxin [indole-3-acetic acid (IAA)] is essential to plant growth. Auxin biosynthetic pathways and the processes that inactivate auxin by conjugation to amino acids and sugars have been thoroughly characterized. However, the enzyme that catalyzes oxidation of IAA to its primary catabolite 2-oxindole-3-acetic acid (oxIAA) remains uncharacterized. Here, we show that DIOXYGENASE FOR AUXIN OXIDATION 1 (DAO1) catalyzes formation of oxIAA in vitro and in vivo and that this mechanism regulates auxin homeostasis and plant growth. Null dao1-1 mutants contain 95% less oxIAA compared with wild type, and complementation of dao1 restores wild-type oxIAA levels, indicating that DAO1 is the primary IAA oxidase in seedlings. Furthermore, dao1 loss of function plants have altered morphology, including larger cotyledons, increased lateral root density, delayed sepal opening, elongated pistils, and reduced fertility in the primary inflorescence stem. These phenotypes are tightly correlated with DAO1 spatiotemporal expression patterns as shown by DAO1pro:β-glucuronidase (GUS) activity and DAO1pro:YFP-DAO1 signals, and transformation with DAO1pro:YFP-DAO1 complemented the mutant phenotypes. The dominant dao1-2D mutant has increased oxIAA levels and decreased stature with shorter leaves and inflorescence stems, thus supporting DAO1 IAA oxidase function in vivo. A second isoform, DAO2, is very weakly expressed in seedling root apices. Together, these data confirm that IAA oxidation by DAO1 is the principal auxin catabolic process in Arabidopsis and that localized IAA oxidation plays a role in plant morphogenesis.
publishDate 2016
dc.date.none.fl_str_mv 2016-09-27
2022-04-28T19:04:54Z
2022-04-28T19:04:54Z
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/10.1073/pnas.1604769113
Proceedings of the National Academy of Sciences of the United States of America, v. 113, n. 39, p. 11010-11015, 2016.
1091-6490
0027-8424
http://hdl.handle.net/11449/220703
10.1073/pnas.1604769113
2-s2.0-84989874686
url http://dx.doi.org/10.1073/pnas.1604769113
http://hdl.handle.net/11449/220703
identifier_str_mv Proceedings of the National Academy of Sciences of the United States of America, v. 113, n. 39, p. 11010-11015, 2016.
1091-6490
0027-8424
10.1073/pnas.1604769113
2-s2.0-84989874686
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Proceedings of the National Academy of Sciences of the United States of America
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 11010-11015
dc.source.none.fl_str_mv Scopus
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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