DAO1 catalyzes temporal and tissue-specific oxidative inactivation of auxin in Arabidopsis thaliana
Autor(a) principal: | |
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Data de Publicação: | 2016 |
Outros Autores: | , , , , , |
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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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:29462024-08-05T14:18:54.620838Repositório 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 |
|
_version_ |
1808128345984991232 |