LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii

Autores
Cerletti, Micaela; Paggi, Roberto Alejandro; Troetschel, Christian; Ferrari, María Celeste; Guevara, Carina Ramallo; Albaum, Stefan; Poetsch, Ansgar; de Castro, Rosana Esther
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The membrane protease LonB is an essential protein in the archaeon Haloferax volcanii and globally impacts its physiology. However, natural substrates of the archaeal Lon protease have not been identified. The whole proteome turnover was examined in a H. volcanii LonB mutant under reduced and physiological protease levels. LC-MS/MS combined with stable isotope labeling was applied for the identification/quantitation of membrane and cytoplasm proteins. Differential synthesis and degradation rates were evidenced for 414 proteins in response to Lon expression. A total of 58 proteins involved in diverse cellular processes showed a degradation pattern (none/very little degradation in the absence of Lon and increased degradation in the presence of Lon) consistent with a LonB substrate, which was further substantiated for several of these candidates by pull-down assays. The most notable was phytoene synthase (PSY), the rate-limiting enzyme in carotenoid biosynthesis. The rapid degradation of PSY upon LonB induction in addition to the remarkable stabilization of this protein and hyperpigmentation phenotype in the Lon mutant strongly suggest that PSY is a LonB substrate. This work identifies for the first time candidate targets of the archaeal Lon protease and establishes proteolysis by Lon as a novel post-translational regulatory mechanism of carotenogenesis.
Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; Argentina
Fil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; Argentina
Fil: Troetschel, Christian. Ruhr Universität Bochum; Alemania
Fil: Ferrari, María Celeste. Universidad Nacional de Mar del Plata; Argentina
Fil: Guevara, Carina Ramallo. Ruhr Universität Bochum; Alemania
Fil: Albaum, Stefan. Universitat Bielefeld; Alemania
Fil: Poetsch, Ansgar. Plant Biochemistry, Ruhr University Bochum; Alemania
Fil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina
Materia
Archaea
Haloferax volcanii
Membrane protease
Lonb substrates
Phytoene synthase
Proteome turnover
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/87562
Acceder
id CONICETDig_24acd93ea176561f20c03979a87440de
oai_identifier_str oai:ri.conicet.gov.ar:11336/87562
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcaniiCerletti, MicaelaPaggi, Roberto AlejandroTroetschel, ChristianFerrari, María CelesteGuevara, Carina RamalloAlbaum, StefanPoetsch, Ansgarde Castro, Rosana EstherArchaeaHaloferax volcaniiMembrane proteaseLonb substratesPhytoene synthaseProteome turnoverhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The membrane protease LonB is an essential protein in the archaeon Haloferax volcanii and globally impacts its physiology. However, natural substrates of the archaeal Lon protease have not been identified. The whole proteome turnover was examined in a H. volcanii LonB mutant under reduced and physiological protease levels. LC-MS/MS combined with stable isotope labeling was applied for the identification/quantitation of membrane and cytoplasm proteins. Differential synthesis and degradation rates were evidenced for 414 proteins in response to Lon expression. A total of 58 proteins involved in diverse cellular processes showed a degradation pattern (none/very little degradation in the absence of Lon and increased degradation in the presence of Lon) consistent with a LonB substrate, which was further substantiated for several of these candidates by pull-down assays. The most notable was phytoene synthase (PSY), the rate-limiting enzyme in carotenoid biosynthesis. The rapid degradation of PSY upon LonB induction in addition to the remarkable stabilization of this protein and hyperpigmentation phenotype in the Lon mutant strongly suggest that PSY is a LonB substrate. This work identifies for the first time candidate targets of the archaeal Lon protease and establishes proteolysis by Lon as a novel post-translational regulatory mechanism of carotenogenesis.Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; ArgentinaFil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; ArgentinaFil: Troetschel, Christian. Ruhr Universität Bochum; AlemaniaFil: Ferrari, María Celeste. Universidad Nacional de Mar del Plata; ArgentinaFil: Guevara, Carina Ramallo. Ruhr Universität Bochum; AlemaniaFil: Albaum, Stefan. Universitat Bielefeld; AlemaniaFil: Poetsch, Ansgar. Plant Biochemistry, Ruhr University Bochum; AlemaniaFil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; ArgentinaAmerican Chemical Society2018-03-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/87562Cerletti, Micaela; Paggi, Roberto Alejandro; Troetschel, Christian; Ferrari, María Celeste; Guevara, Carina Ramallo; et al.; LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii; American Chemical Society; Journal of Proteome Research; 17; 3; 7-3-2018; 1158-11711535-3893CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:36:57Zoai:ri.conicet.gov.ar:11336/87562instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:36:57.453CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
title LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
spellingShingle LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
Cerletti, Micaela
Archaea
Haloferax volcanii
Membrane protease
Lonb substrates
Phytoene synthase
Proteome turnover
title_short LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
title_full LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
title_fullStr LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
title_full_unstemmed LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
title_sort LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
dc.creator.none.fl_str_mv Cerletti, Micaela
Paggi, Roberto Alejandro
Troetschel, Christian
Ferrari, María Celeste
Guevara, Carina Ramallo
Albaum, Stefan
Poetsch, Ansgar
de Castro, Rosana Esther
author Cerletti, Micaela
author_facet Cerletti, Micaela
Paggi, Roberto Alejandro
Troetschel, Christian
Ferrari, María Celeste
Guevara, Carina Ramallo
Albaum, Stefan
Poetsch, Ansgar
de Castro, Rosana Esther
author_role author
author2 Paggi, Roberto Alejandro
Troetschel, Christian
Ferrari, María Celeste
Guevara, Carina Ramallo
Albaum, Stefan
Poetsch, Ansgar
de Castro, Rosana Esther
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Archaea
Haloferax volcanii
Membrane protease
Lonb substrates
Phytoene synthase
Proteome turnover
topic Archaea
Haloferax volcanii
Membrane protease
Lonb substrates
Phytoene synthase
Proteome turnover
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The membrane protease LonB is an essential protein in the archaeon Haloferax volcanii and globally impacts its physiology. However, natural substrates of the archaeal Lon protease have not been identified. The whole proteome turnover was examined in a H. volcanii LonB mutant under reduced and physiological protease levels. LC-MS/MS combined with stable isotope labeling was applied for the identification/quantitation of membrane and cytoplasm proteins. Differential synthesis and degradation rates were evidenced for 414 proteins in response to Lon expression. A total of 58 proteins involved in diverse cellular processes showed a degradation pattern (none/very little degradation in the absence of Lon and increased degradation in the presence of Lon) consistent with a LonB substrate, which was further substantiated for several of these candidates by pull-down assays. The most notable was phytoene synthase (PSY), the rate-limiting enzyme in carotenoid biosynthesis. The rapid degradation of PSY upon LonB induction in addition to the remarkable stabilization of this protein and hyperpigmentation phenotype in the Lon mutant strongly suggest that PSY is a LonB substrate. This work identifies for the first time candidate targets of the archaeal Lon protease and establishes proteolysis by Lon as a novel post-translational regulatory mechanism of carotenogenesis.
Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; Argentina
Fil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; Argentina
Fil: Troetschel, Christian. Ruhr Universität Bochum; Alemania
Fil: Ferrari, María Celeste. Universidad Nacional de Mar del Plata; Argentina
Fil: Guevara, Carina Ramallo. Ruhr Universität Bochum; Alemania
Fil: Albaum, Stefan. Universitat Bielefeld; Alemania
Fil: Poetsch, Ansgar. Plant Biochemistry, Ruhr University Bochum; Alemania
Fil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina
description The membrane protease LonB is an essential protein in the archaeon Haloferax volcanii and globally impacts its physiology. However, natural substrates of the archaeal Lon protease have not been identified. The whole proteome turnover was examined in a H. volcanii LonB mutant under reduced and physiological protease levels. LC-MS/MS combined with stable isotope labeling was applied for the identification/quantitation of membrane and cytoplasm proteins. Differential synthesis and degradation rates were evidenced for 414 proteins in response to Lon expression. A total of 58 proteins involved in diverse cellular processes showed a degradation pattern (none/very little degradation in the absence of Lon and increased degradation in the presence of Lon) consistent with a LonB substrate, which was further substantiated for several of these candidates by pull-down assays. The most notable was phytoene synthase (PSY), the rate-limiting enzyme in carotenoid biosynthesis. The rapid degradation of PSY upon LonB induction in addition to the remarkable stabilization of this protein and hyperpigmentation phenotype in the Lon mutant strongly suggest that PSY is a LonB substrate. This work identifies for the first time candidate targets of the archaeal Lon protease and establishes proteolysis by Lon as a novel post-translational regulatory mechanism of carotenogenesis.
publishDate 2018
dc.date.none.fl_str_mv 2018-03-07
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/87562
Cerletti, Micaela; Paggi, Roberto Alejandro; Troetschel, Christian; Ferrari, María Celeste; Guevara, Carina Ramallo; et al.; LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii; American Chemical Society; Journal of Proteome Research; 17; 3; 7-3-2018; 1158-1171
1535-3893
CONICET Digital
CONICET
url http://hdl.handle.net/11336/87562
identifier_str_mv Cerletti, Micaela; Paggi, Roberto Alejandro; Troetschel, Christian; Ferrari, María Celeste; Guevara, Carina Ramallo; et al.; LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii; American Chemical Society; Journal of Proteome Research; 17; 3; 7-3-2018; 1158-1171
1535-3893
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844613161925214208
score 13.070432

Publicaciones similares