The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes

The ribotoxin -sarcin belongs to a family of ribonucleases that cleave the sarcin/ricin loop (SRL), a critical functional rRNA element within the large ribosomal subunit (60S), thereby abolishing translation. Whether -sarcin targets the SRL only in mature 60S subunits remains unresolved. Here, we sh...

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Authors: Olombrada, Miriam, Peña, Cohue, Rodríguez Galán, Olga, Klingauf Nerurkar, Purnima, Portugal Calisto, Daniela, Oborská Oplová, Michaela, Altvater, Martin, Gavilanes, José G., Martínez Del Pozo, Álvaro, Cruz, Jesús de la, García Ortega, Lucía, Govind Panse, Vikram
Format: article
Publication Date:2020
Country:España
Institution:Universidad Complutense de Madrid (UCM)
Repository:Docta Complutense
Language:English
OAI Identifier:oai:docta.ucm.es:20.500.14352/6574
Online Access:https://hdl.handle.net/20.500.14352/6574
Access Level:Open access
Keyword:577.1
Ribosomes
Peptide Elongation Factor G
Anticodons
Biología molecular (Química)
Bioquímica (Química)
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spelling The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomesOlombrada, MiriamPeña, CohueRodríguez Galán, OlgaKlingauf Nerurkar, PurnimaPortugal Calisto, DanielaOborská Oplová, MichaelaAltvater, MartinGavilanes, José G.Martínez Del Pozo, ÁlvaroCruz, Jesús de laGarcía Ortega, LucíaGovind Panse, Vikram577.1RibosomesPeptide Elongation Factor GAnticodonsBiología molecular (Química)Bioquímica (Química)The ribotoxin -sarcin belongs to a family of ribonucleases that cleave the sarcin/ricin loop (SRL), a critical functional rRNA element within the large ribosomal subunit (60S), thereby abolishing translation. Whether -sarcin targets the SRL only in mature 60S subunits remains unresolved. Here, we show that, in yeast, -sarcin can cleave SRLs within late 60S pre-ribosomes containing mature 25S rRNA but not nucleolar/nuclear 60S pre-ribosomes containing 27S pre-rRNA in vivo. Conditional expression of -sarcin is lethal, but does not impede early pre-rRNA processing, nuclear export and the cytoplasmic maturation of 60S pre-ribosomes. Thus, SRL-cleaved containing late 60S pre-ribosomes seem to escape cytoplasmic proofreading steps. Polysome analyses revealed that SRL-cleaved 60S ribosomal subunits form 80S initiation complexes, but fail to progress to the step of translation elongation. We suggest that the functional integrity of a -sarcin cleaved SRL might be assessed only during translation.Oxford university pressUniversidad Complutense de Madrid20202020-01-0120202020-01-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/6574reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2Atribución-NoComercial 3.0 Españahttps://creativecommons.org/licenses/by-nc/3.0/es/info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/65742026-06-02T12:44:21Z
dc.title.none.fl_str_mv The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
title The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
spellingShingle The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
Olombrada, Miriam
577.1
Ribosomes
Peptide Elongation Factor G
Anticodons
Biología molecular (Química)
Bioquímica (Química)
title_short The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
title_full The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
title_fullStr The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
title_full_unstemmed The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
title_sort The ribotoxin -sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes
dc.creator.none.fl_str_mv Olombrada, Miriam
Peña, Cohue
Rodríguez Galán, Olga
Klingauf Nerurkar, Purnima
Portugal Calisto, Daniela
Oborská Oplová, Michaela
Altvater, Martin
Gavilanes, José G.
Martínez Del Pozo, Álvaro
Cruz, Jesús de la
García Ortega, Lucía
Govind Panse, Vikram
author Olombrada, Miriam
author_facet Olombrada, Miriam
Peña, Cohue
Rodríguez Galán, Olga
Klingauf Nerurkar, Purnima
Portugal Calisto, Daniela
Oborská Oplová, Michaela
Altvater, Martin
Gavilanes, José G.
Martínez Del Pozo, Álvaro
Cruz, Jesús de la
García Ortega, Lucía
Govind Panse, Vikram
author_role author
author2 Peña, Cohue
Rodríguez Galán, Olga
Klingauf Nerurkar, Purnima
Portugal Calisto, Daniela
Oborská Oplová, Michaela
Altvater, Martin
Gavilanes, José G.
Martínez Del Pozo, Álvaro
Cruz, Jesús de la
García Ortega, Lucía
Govind Panse, Vikram
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1
Ribosomes
Peptide Elongation Factor G
Anticodons
Biología molecular (Química)
Bioquímica (Química)
topic 577.1
Ribosomes
Peptide Elongation Factor G
Anticodons
Biología molecular (Química)
Bioquímica (Química)
description The ribotoxin -sarcin belongs to a family of ribonucleases that cleave the sarcin/ricin loop (SRL), a critical functional rRNA element within the large ribosomal subunit (60S), thereby abolishing translation. Whether -sarcin targets the SRL only in mature 60S subunits remains unresolved. Here, we show that, in yeast, -sarcin can cleave SRLs within late 60S pre-ribosomes containing mature 25S rRNA but not nucleolar/nuclear 60S pre-ribosomes containing 27S pre-rRNA in vivo. Conditional expression of -sarcin is lethal, but does not impede early pre-rRNA processing, nuclear export and the cytoplasmic maturation of 60S pre-ribosomes. Thus, SRL-cleaved containing late 60S pre-ribosomes seem to escape cytoplasmic proofreading steps. Polysome analyses revealed that SRL-cleaved 60S ribosomal subunits form 80S initiation complexes, but fail to progress to the step of translation elongation. We suggest that the functional integrity of a -sarcin cleaved SRL might be assessed only during translation.
publishDate 2020
dc.date.none.fl_str_mv 2020
2020-01-01
2020
2020-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/6574
url https://hdl.handle.net/20.500.14352/6574
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
Atribución-NoComercial 3.0 España
https://creativecommons.org/licenses/by-nc/3.0/es/
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
Atribución-NoComercial 3.0 España
https://creativecommons.org/licenses/by-nc/3.0/es/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Oxford university press
publisher.none.fl_str_mv Oxford university press
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869417362520801280
score 15,300719

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