Haloferax volcanii proteome response to deletion of a rhomboid protease gene

Autores
Costa, Mariana Inés; Cerletti, Micaela; Paggi, Roberto Alejandro; Trötschel, Christian; de Castro, Rosana Esther; Poetsch, Ansgar; Gimenez, Maria Ines
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Rhomboids are conserved intramembrane serine proteases involved in cell signaling processes. Their role in prokaryotes is scarcely known and remains to be investigated in Archaea. We previously constructed a rhomboid homologue deletion mutant (ΔrhoII) in Haloferax volcanii, which showed reduced motility, increased novobiocin sensitivity, and an N- glycosylation defect. To address the impact of rhoII deletion on H. volcanii physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. A total of 1847 proteins were identified (45.8% of H. volcanii predicted proteome), from which 103 differed in amount. Additionally, the mutant strain evidenced 99 proteins with altered electrophoretic migration, which suggested differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration, electrophoretic migration, or semitryptic cleavage in the mutant were considered as potential RhoII targets. These included a PrsW protease homologue (which was less stable in the mutant strain), a predicted halocyanin, and six integral membrane proteins potentially related to the mutant glycosylation (S-layer glycoprotein, Agl15) and cell adhesion/motility (flagellin1, HVO-1153, PilA1, and PibD) defects. This study investigated for the first time the impact of a rhomboid protease on the whole proteome of an organism.
Fil: Costa, Mariana Inés. Universidad Nacional de Mar del Plata; Argentina
Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; Argentina
Fil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; Argentina
Fil: Trötschel, Christian. Ruhr Universität Bochum; Alemania
Fil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Poetsch, Ansgar. Ruhr Universität Bochum; Alemania
Fil: Gimenez, Maria Ines. Universidad Nacional de Mar del Plata; Argentina
Materia
Archea
Halorerax volcanii
Protease substrate
Rhomboid protease
Shotgun proteomics
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:11336/88113

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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Haloferax volcanii proteome response to deletion of a rhomboid protease geneCosta, Mariana InésCerletti, MicaelaPaggi, Roberto AlejandroTrötschel, Christiande Castro, Rosana EstherPoetsch, AnsgarGimenez, Maria InesArcheaHalorerax volcaniiProtease substrateRhomboid proteaseShotgun proteomicshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Rhomboids are conserved intramembrane serine proteases involved in cell signaling processes. Their role in prokaryotes is scarcely known and remains to be investigated in Archaea. We previously constructed a rhomboid homologue deletion mutant (ΔrhoII) in Haloferax volcanii, which showed reduced motility, increased novobiocin sensitivity, and an N- glycosylation defect. To address the impact of rhoII deletion on H. volcanii physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. A total of 1847 proteins were identified (45.8% of H. volcanii predicted proteome), from which 103 differed in amount. Additionally, the mutant strain evidenced 99 proteins with altered electrophoretic migration, which suggested differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration, electrophoretic migration, or semitryptic cleavage in the mutant were considered as potential RhoII targets. These included a PrsW protease homologue (which was less stable in the mutant strain), a predicted halocyanin, and six integral membrane proteins potentially related to the mutant glycosylation (S-layer glycoprotein, Agl15) and cell adhesion/motility (flagellin1, HVO-1153, PilA1, and PibD) defects. This study investigated for the first time the impact of a rhomboid protease on the whole proteome of an organism.Fil: Costa, Mariana Inés. Universidad Nacional de Mar del Plata; ArgentinaFil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; ArgentinaFil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; ArgentinaFil: Trötschel, Christian. Ruhr Universität Bochum; AlemaniaFil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; ArgentinaFil: Poetsch, Ansgar. Ruhr Universität Bochum; AlemaniaFil: Gimenez, Maria Ines. Universidad Nacional de Mar del Plata; ArgentinaAmerican Chemical Society2018-01-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/88113Costa, Mariana Inés; Cerletti, Micaela; Paggi, Roberto Alejandro; Trötschel, Christian; de Castro, Rosana Esther; et al.; Haloferax volcanii proteome response to deletion of a rhomboid protease gene; American Chemical Society; Journal of Proteome Research; 17; 3; 5-1-2018; 961-9771535-3893CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://pubs.acs.org/doi/10.1021/acs.jproteome.7b00530info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.jproteome.7b00530info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:24:29Zoai:ri.conicet.gov.ar:11336/88113instacron: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:34982025-10-15 14:24:29.554CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Haloferax volcanii proteome response to deletion of a rhomboid protease gene
title Haloferax volcanii proteome response to deletion of a rhomboid protease gene
spellingShingle Haloferax volcanii proteome response to deletion of a rhomboid protease gene
Costa, Mariana Inés
Archea
Halorerax volcanii
Protease substrate
Rhomboid protease
Shotgun proteomics
title_short Haloferax volcanii proteome response to deletion of a rhomboid protease gene
title_full Haloferax volcanii proteome response to deletion of a rhomboid protease gene
title_fullStr Haloferax volcanii proteome response to deletion of a rhomboid protease gene
title_full_unstemmed Haloferax volcanii proteome response to deletion of a rhomboid protease gene
title_sort Haloferax volcanii proteome response to deletion of a rhomboid protease gene
dc.creator.none.fl_str_mv Costa, Mariana Inés
Cerletti, Micaela
Paggi, Roberto Alejandro
Trötschel, Christian
de Castro, Rosana Esther
Poetsch, Ansgar
Gimenez, Maria Ines
author Costa, Mariana Inés
author_facet Costa, Mariana Inés
Cerletti, Micaela
Paggi, Roberto Alejandro
Trötschel, Christian
de Castro, Rosana Esther
Poetsch, Ansgar
Gimenez, Maria Ines
author_role author
author2 Cerletti, Micaela
Paggi, Roberto Alejandro
Trötschel, Christian
de Castro, Rosana Esther
Poetsch, Ansgar
Gimenez, Maria Ines
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Archea
Halorerax volcanii
Protease substrate
Rhomboid protease
Shotgun proteomics
topic Archea
Halorerax volcanii
Protease substrate
Rhomboid protease
Shotgun proteomics
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Rhomboids are conserved intramembrane serine proteases involved in cell signaling processes. Their role in prokaryotes is scarcely known and remains to be investigated in Archaea. We previously constructed a rhomboid homologue deletion mutant (ΔrhoII) in Haloferax volcanii, which showed reduced motility, increased novobiocin sensitivity, and an N- glycosylation defect. To address the impact of rhoII deletion on H. volcanii physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. A total of 1847 proteins were identified (45.8% of H. volcanii predicted proteome), from which 103 differed in amount. Additionally, the mutant strain evidenced 99 proteins with altered electrophoretic migration, which suggested differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration, electrophoretic migration, or semitryptic cleavage in the mutant were considered as potential RhoII targets. These included a PrsW protease homologue (which was less stable in the mutant strain), a predicted halocyanin, and six integral membrane proteins potentially related to the mutant glycosylation (S-layer glycoprotein, Agl15) and cell adhesion/motility (flagellin1, HVO-1153, PilA1, and PibD) defects. This study investigated for the first time the impact of a rhomboid protease on the whole proteome of an organism.
Fil: Costa, Mariana Inés. Universidad Nacional de Mar del Plata; Argentina
Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; Argentina
Fil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; Argentina
Fil: Trötschel, Christian. Ruhr Universität Bochum; Alemania
Fil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
Fil: Poetsch, Ansgar. Ruhr Universität Bochum; Alemania
Fil: Gimenez, Maria Ines. Universidad Nacional de Mar del Plata; Argentina
description Rhomboids are conserved intramembrane serine proteases involved in cell signaling processes. Their role in prokaryotes is scarcely known and remains to be investigated in Archaea. We previously constructed a rhomboid homologue deletion mutant (ΔrhoII) in Haloferax volcanii, which showed reduced motility, increased novobiocin sensitivity, and an N- glycosylation defect. To address the impact of rhoII deletion on H. volcanii physiology, the proteomes of mutant and parental strains were compared by shotgun proteomics. A total of 1847 proteins were identified (45.8% of H. volcanii predicted proteome), from which 103 differed in amount. Additionally, the mutant strain evidenced 99 proteins with altered electrophoretic migration, which suggested differential post-translational processing/modification. Integral membrane proteins that evidenced variations in concentration, electrophoretic migration, or semitryptic cleavage in the mutant were considered as potential RhoII targets. These included a PrsW protease homologue (which was less stable in the mutant strain), a predicted halocyanin, and six integral membrane proteins potentially related to the mutant glycosylation (S-layer glycoprotein, Agl15) and cell adhesion/motility (flagellin1, HVO-1153, PilA1, and PibD) defects. This study investigated for the first time the impact of a rhomboid protease on the whole proteome of an organism.
publishDate 2018
dc.date.none.fl_str_mv 2018-01-05
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/11336/88113
Costa, Mariana Inés; Cerletti, Micaela; Paggi, Roberto Alejandro; Trötschel, Christian; de Castro, Rosana Esther; et al.; Haloferax volcanii proteome response to deletion of a rhomboid protease gene; American Chemical Society; Journal of Proteome Research; 17; 3; 5-1-2018; 961-977
1535-3893
CONICET Digital
CONICET
url http://hdl.handle.net/11336/88113
identifier_str_mv Costa, Mariana Inés; Cerletti, Micaela; Paggi, Roberto Alejandro; Trötschel, Christian; de Castro, Rosana Esther; et al.; Haloferax volcanii proteome response to deletion of a rhomboid protease gene; American Chemical Society; Journal of Proteome Research; 17; 3; 5-1-2018; 961-977
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/url/http://pubs.acs.org/doi/10.1021/acs.jproteome.7b00530
info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.jproteome.7b00530
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
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
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