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dc.contributor.author
Cerletti, Micaela
dc.contributor.author
Paggi, Roberto Alejandro
dc.contributor.author
Troetschel, Christian
dc.contributor.author
Ferrari, María Celeste
dc.contributor.author
Guevara, Carina Ramallo
dc.contributor.author
Albaum, Stefan
dc.contributor.author
Poetsch, Ansgar
dc.contributor.author
de Castro, Rosana Esther
dc.date.available
2019-10-29T18:06:16Z
dc.date.issued
2018-03-07
dc.identifier.citation
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
dc.identifier.issn
1535-3893
dc.identifier.uri
http://hdl.handle.net/11336/87562
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Chemical Society
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Archaea
dc.subject
Haloferax volcanii
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Membrane protease
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Lonb substrates
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Phytoene synthase
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Proteome turnover
dc.subject.classification
Biología Celular, Microbiología
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
LonB protease Is a novel regulator of carotenogenesis controlling degradation of phytoene synthase in Haloferax volcanii
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-22T15:48:24Z
dc.journal.volume
17
dc.journal.number
3
dc.journal.pagination
1158-1171
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Cerletti, Micaela. Universidad Nacional de Mar del Plata; Argentina
dc.description.fil
Fil: Paggi, Roberto Alejandro. Universidad Nacional de Mar del Plata; Argentina
dc.description.fil
Fil: Troetschel, Christian. Ruhr Universität Bochum; Alemania
dc.description.fil
Fil: Ferrari, María Celeste. Universidad Nacional de Mar del Plata; Argentina
dc.description.fil
Fil: Guevara, Carina Ramallo. Ruhr Universität Bochum; Alemania
dc.description.fil
Fil: Albaum, Stefan. Universitat Bielefeld; Alemania
dc.description.fil
Fil: Poetsch, Ansgar. Plant Biochemistry, Ruhr University Bochum; Alemania
dc.description.fil
Fil: de Castro, Rosana Esther. Universidad Nacional de Mar del Plata; Argentina
dc.journal.title
Journal of Proteome Research
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://pubs.acs.org/doi/10.1021/acs.jproteome.7b00809


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