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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/88113
Ver los metadatos del registro completo
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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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1846082667226857472 |
score |
13.22299 |