A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana

Detalhes bibliográficos
Autor(a) principal: Matos, Juliana L.
Data de Publicação: 2008
Outros Autores: Fiori, Celso S., Silva-Filho, Marcio C., Moura, Daniel Scherer de [UNIFESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNIFESP
Texto Completo: http://dx.doi.org/10.1016/j.febslet.2008.08.025
http://repositorio.unifesp.br/handle/11600/30967
Resumo: Prohormone proteins in animals and yeast are typically processed at dibasic sites by convertases. Propeptide hormones are also found in plants but little is known about processing. We show for the first time that a dibasic site upstream of a plant peptide hormone, AtRALF1, is essential for processing. Overexpression of preproAtRALF1 causes semidwarfism whereas overexpression of preproAtRALF1(R69A), the propeptide with a mutation in the dibasic site, shows a normal phenotype. RALF1(R69A) plants accumulate only the mutated proprotein and not the processed peptide. in vitro processing using microsomal fractions suggests that processing is carried out by a kexin-like convertase. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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spelling A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thalianaConvertaseProtein processingProhormoneProhormone proteins in animals and yeast are typically processed at dibasic sites by convertases. Propeptide hormones are also found in plants but little is known about processing. We show for the first time that a dibasic site upstream of a plant peptide hormone, AtRALF1, is essential for processing. Overexpression of preproAtRALF1 causes semidwarfism whereas overexpression of preproAtRALF1(R69A), the propeptide with a mutation in the dibasic site, shows a normal phenotype. RALF1(R69A) plants accumulate only the mutated proprotein and not the processed peptide. in vitro processing using microsomal fractions suggests that processing is carried out by a kexin-like convertase. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.Universidade Federal de São Paulo, Escola Paulista Ciencias Biol, Dept Ciencias Biol, BR-09972270 Diadema, SP, BrazilUniv São Paulo, Escola Super Agr Luiz de Queiroz, Dept Genet, BR-13400970 Piracicaba, SP, BrazilUniversidade Federal de São Paulo, Escola Paulista Ciencias Biol, Dept Ciencias Biol, BR-09972270 Diadema, SP, BrazilWeb of ScienceFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)FAPESP: 02/08661-1Elsevier B.V.Universidade Federal de São Paulo (UNIFESP)Universidade de São Paulo (USP)Matos, Juliana L.Fiori, Celso S.Silva-Filho, Marcio C.Moura, Daniel Scherer de [UNIFESP]2016-01-24T13:51:46Z2016-01-24T13:51:46Z2008-10-15info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion3343-3347application/pdfhttp://dx.doi.org/10.1016/j.febslet.2008.08.025Febs Letters. Amsterdam: Elsevier B.V., v. 582, n. 23-24, p. 3343-3347, 2008.10.1016/j.febslet.2008.08.025WOS000260806700016.pdf0014-5793http://repositorio.unifesp.br/handle/11600/30967WOS:000260806700016engFebs Lettersinfo:eu-repo/semantics/openAccesshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-07-31T00:09:40Zoai:repositorio.unifesp.br/:11600/30967Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-07-31T00:09:40Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false
dc.title.none.fl_str_mv A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
title A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
spellingShingle A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
Matos, Juliana L.
Convertase
Protein processing
Prohormone
title_short A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
title_full A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
title_fullStr A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
title_full_unstemmed A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
title_sort A conserved dibasic site is essential for correct processing of the peptide hormone AtRALF1 in Arabidopsis thaliana
author Matos, Juliana L.
author_facet Matos, Juliana L.
Fiori, Celso S.
Silva-Filho, Marcio C.
Moura, Daniel Scherer de [UNIFESP]
author_role author
author2 Fiori, Celso S.
Silva-Filho, Marcio C.
Moura, Daniel Scherer de [UNIFESP]
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Matos, Juliana L.
Fiori, Celso S.
Silva-Filho, Marcio C.
Moura, Daniel Scherer de [UNIFESP]
dc.subject.por.fl_str_mv Convertase
Protein processing
Prohormone
topic Convertase
Protein processing
Prohormone
description Prohormone proteins in animals and yeast are typically processed at dibasic sites by convertases. Propeptide hormones are also found in plants but little is known about processing. We show for the first time that a dibasic site upstream of a plant peptide hormone, AtRALF1, is essential for processing. Overexpression of preproAtRALF1 causes semidwarfism whereas overexpression of preproAtRALF1(R69A), the propeptide with a mutation in the dibasic site, shows a normal phenotype. RALF1(R69A) plants accumulate only the mutated proprotein and not the processed peptide. in vitro processing using microsomal fractions suggests that processing is carried out by a kexin-like convertase. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
publishDate 2008
dc.date.none.fl_str_mv 2008-10-15
2016-01-24T13:51:46Z
2016-01-24T13:51:46Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1016/j.febslet.2008.08.025
Febs Letters. Amsterdam: Elsevier B.V., v. 582, n. 23-24, p. 3343-3347, 2008.
10.1016/j.febslet.2008.08.025
WOS000260806700016.pdf
0014-5793
http://repositorio.unifesp.br/handle/11600/30967
WOS:000260806700016
url http://dx.doi.org/10.1016/j.febslet.2008.08.025
http://repositorio.unifesp.br/handle/11600/30967
identifier_str_mv Febs Letters. Amsterdam: Elsevier B.V., v. 582, n. 23-24, p. 3343-3347, 2008.
10.1016/j.febslet.2008.08.025
WOS000260806700016.pdf
0014-5793
WOS:000260806700016
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Febs Letters
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
eu_rights_str_mv openAccess
rights_invalid_str_mv http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.format.none.fl_str_mv 3343-3347
application/pdf
dc.publisher.none.fl_str_mv Elsevier B.V.
publisher.none.fl_str_mv Elsevier B.V.
dc.source.none.fl_str_mv reponame:Repositório Institucional da UNIFESP
instname:Universidade Federal de São Paulo (UNIFESP)
instacron:UNIFESP
instname_str Universidade Federal de São Paulo (UNIFESP)
instacron_str UNIFESP
institution UNIFESP
reponame_str Repositório Institucional da UNIFESP
collection Repositório Institucional da UNIFESP
repository.name.fl_str_mv Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)
repository.mail.fl_str_mv biblioteca.csp@unifesp.br
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