The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.

Ubiquitin is a highly conserved small eukaryotic protein. It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal moiety to ribosomal proteins. Understanding the ro...

ver descrição completa

Detalhes bibliográficos
Autores: Martín-Villanueva, Sara, Fernández-Pevida, Antonio, Kressler, Dieter, de la Cruz, Jesús
Tipo de documento: artigo
Data de publicação:2019
País:España
Recursos:Instituto de Salud Carlos III (ISCIII)
Repositório:Repisalud
Idioma:inglês
OAI Identifier:oai:repisalud.isciii.es:20.500.12105/25250
Acesso em linha:https://hdl.handle.net/20.500.12105/25250
Access Level:Acceso aberto
Palavra-chave:UBI1/2 genes
pre-rRNA processing
Ribosomal protein L40 (eL40)
Ribosome biogenesis
Translation
Ubiquitin
Yeast
Ribosomal Proteins
Saccharomyces cerevisiae
id ES_9d26076f22f4cd975b3fc703c5e37f06
oai_identifier_str oai:repisalud.isciii.es:20.500.12105/25250
network_acronym_str ES
network_name_str España
repository_id_str
spelling The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.Martín-Villanueva, SaraFernández-Pevida, AntonioKressler, Dieterde la Cruz, JesúsUBI1/2 genespre-rRNA processingRibosomal protein L40 (eL40)Ribosome biogenesisTranslationUbiquitinYeastRibosomal ProteinsSaccharomyces cerevisiaeUbiquitinUbiquitin is a highly conserved small eukaryotic protein. It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal moiety to ribosomal proteins. Understanding the role of the ubiquitin fused to ribosomal proteins becomes relevant, as these proteins are practically invariably eS31 and eL40 in the different eukaryotes. Herein, we used the amenable yeast Saccharomyces cerevisiae to study whether ubiquitin facilitates the expression of the fused eL40 (Ubi1 and Ubi2 precursors) and eS31 (Ubi3 precursor) ribosomal proteins. We have analyzed the phenotypic effects of a genomic ubi1∆ub-HA ubi2∆ mutant, which expresses a ubiquitin-free HA-tagged eL40A protein as the sole source of cellular eL40. This mutant shows a severe slow-growth phenotype, which could be fully suppressed by increased dosage of the ubi1∆ub-HA allele, or partially by the replacement of ubiquitin by the ubiquitin-like Smt3 protein. While expression levels of eL40A-HA from ubi1∆ub-HA are low, eL40A is produced practically at normal levels from the Smt3-S-eL40A-HA precursor. Finally, we observed enhanced aggregation of eS31-HA when derived from a Ubi3∆ub-HA precursor and reduced aggregation of eL40A-HA when expressed from a Smt3-S-eL40A-HA precursor. We conclude that ubiquitin might serve as a cis-acting molecular chaperone that assists in the folding and synthesis of the fused eL40 and eS31 ribosomal proteins.20242024-10-2320192019-08-0720192019-08-07research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articlehttps://hdl.handle.net/20.500.12105/25250reponame:Repisaludinstname:Instituto de Salud Carlos III (ISCIII)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Attribution 4.0 Internationalhttp://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:repisalud.isciii.es:20.500.12105/252502026-06-12T12:43:37Z
dc.title.none.fl_str_mv The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
title The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
spellingShingle The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
Martín-Villanueva, Sara
UBI1/2 genes
pre-rRNA processing
Ribosomal protein L40 (eL40)
Ribosome biogenesis
Translation
Ubiquitin
Yeast
Ribosomal Proteins
Saccharomyces cerevisiae
Ubiquitin
title_short The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
title_full The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
title_fullStr The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
title_full_unstemmed The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
title_sort The Ubiquitin Moiety of Ubi1 Is Required for Productive Expression of Ribosomal Protein eL40 in Saccharomyces cerevisiae.
dc.creator.none.fl_str_mv Martín-Villanueva, Sara
Fernández-Pevida, Antonio
Kressler, Dieter
de la Cruz, Jesús
author Martín-Villanueva, Sara
author_facet Martín-Villanueva, Sara
Fernández-Pevida, Antonio
Kressler, Dieter
de la Cruz, Jesús
author_role author
author2 Fernández-Pevida, Antonio
Kressler, Dieter
de la Cruz, Jesús
author2_role author
author
author
dc.contributor.none.fl_str_mv
dc.subject.none.fl_str_mv UBI1/2 genes
pre-rRNA processing
Ribosomal protein L40 (eL40)
Ribosome biogenesis
Translation
Ubiquitin
Yeast
Ribosomal Proteins
Saccharomyces cerevisiae
Ubiquitin
topic UBI1/2 genes
pre-rRNA processing
Ribosomal protein L40 (eL40)
Ribosome biogenesis
Translation
Ubiquitin
Yeast
Ribosomal Proteins
Saccharomyces cerevisiae
Ubiquitin
description Ubiquitin is a highly conserved small eukaryotic protein. It is generated by proteolytic cleavage of precursor proteins in which it is fused either to itself, constituting a polyubiquitin precursor of head-to-tail monomers, or as a single N-terminal moiety to ribosomal proteins. Understanding the role of the ubiquitin fused to ribosomal proteins becomes relevant, as these proteins are practically invariably eS31 and eL40 in the different eukaryotes. Herein, we used the amenable yeast Saccharomyces cerevisiae to study whether ubiquitin facilitates the expression of the fused eL40 (Ubi1 and Ubi2 precursors) and eS31 (Ubi3 precursor) ribosomal proteins. We have analyzed the phenotypic effects of a genomic ubi1∆ub-HA ubi2∆ mutant, which expresses a ubiquitin-free HA-tagged eL40A protein as the sole source of cellular eL40. This mutant shows a severe slow-growth phenotype, which could be fully suppressed by increased dosage of the ubi1∆ub-HA allele, or partially by the replacement of ubiquitin by the ubiquitin-like Smt3 protein. While expression levels of eL40A-HA from ubi1∆ub-HA are low, eL40A is produced practically at normal levels from the Smt3-S-eL40A-HA precursor. Finally, we observed enhanced aggregation of eS31-HA when derived from a Ubi3∆ub-HA precursor and reduced aggregation of eL40A-HA when expressed from a Smt3-S-eL40A-HA precursor. We conclude that ubiquitin might serve as a cis-acting molecular chaperone that assists in the folding and synthesis of the fused eL40 and eS31 ribosomal proteins.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-08-07
2019
2019-08-07
2024
2024-10-23
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.12105/25250
url https://hdl.handle.net/20.500.12105/25250
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.source.none.fl_str_mv reponame:Repisalud
instname:Instituto de Salud Carlos III (ISCIII)
instname_str Instituto de Salud Carlos III (ISCIII)
reponame_str Repisalud
collection Repisalud
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869414718133764096
score 15,81155

Registros relacionados