The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.

The yeast nucleolar protein Nop8p has previously been shown to interact with Nip7p and to be required for 60S ribosomal subunit formation. Although depletion of Nop8p in yeast cells leads to premature degradation of rRNAs, the biochemical mechanism responsible for this phenotype is still not known....

Full description

Bibliographic Details
Main Authors: Marcia C T Santos, Mauricio B Goldfeder, Nilson I T Zanchin, Carla C Oliveira
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2011-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3126838?pdf=render
id doaj-080e6e2af9a44607b84007d1a9b16555
record_format Article
spelling doaj-080e6e2af9a44607b84007d1a9b165552020-11-25T02:28:42ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-0166e2168610.1371/journal.pone.0021686The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.Marcia C T SantosMauricio B GoldfederNilson I T ZanchinCarla C OliveiraThe yeast nucleolar protein Nop8p has previously been shown to interact with Nip7p and to be required for 60S ribosomal subunit formation. Although depletion of Nop8p in yeast cells leads to premature degradation of rRNAs, the biochemical mechanism responsible for this phenotype is still not known. In this work, we show that the Nop8p amino-terminal region mediates interaction with the 5.8S rRNA, while its carboxyl-terminal portion interacts with Nip7p and can partially complement the growth defect of the conditional mutant strain Δnop8/GAL::NOP8. Interestingly, Nop8p mediates association of Nip7p to pre-ribosomal particles. Nop8p also interacts with the exosome subunit Rrp6p and inhibits the complex activity in vitro, suggesting that the decrease in 60S ribosomal subunit levels detected upon depletion of Nop8p may result from degradation of pre-rRNAs by the exosome. These results strongly indicate that Nop8p may control the exosome function during pre-rRNA processing.http://europepmc.org/articles/PMC3126838?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Marcia C T Santos
Mauricio B Goldfeder
Nilson I T Zanchin
Carla C Oliveira
spellingShingle Marcia C T Santos
Mauricio B Goldfeder
Nilson I T Zanchin
Carla C Oliveira
The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.
PLoS ONE
author_facet Marcia C T Santos
Mauricio B Goldfeder
Nilson I T Zanchin
Carla C Oliveira
author_sort Marcia C T Santos
title The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.
title_short The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.
title_full The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.
title_fullStr The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.
title_full_unstemmed The essential nucleolar yeast protein Nop8p controls the exosome function during 60S ribosomal subunit maturation.
title_sort essential nucleolar yeast protein nop8p controls the exosome function during 60s ribosomal subunit maturation.
publisher Public Library of Science (PLoS)
series PLoS ONE
issn 1932-6203
publishDate 2011-01-01
description The yeast nucleolar protein Nop8p has previously been shown to interact with Nip7p and to be required for 60S ribosomal subunit formation. Although depletion of Nop8p in yeast cells leads to premature degradation of rRNAs, the biochemical mechanism responsible for this phenotype is still not known. In this work, we show that the Nop8p amino-terminal region mediates interaction with the 5.8S rRNA, while its carboxyl-terminal portion interacts with Nip7p and can partially complement the growth defect of the conditional mutant strain Δnop8/GAL::NOP8. Interestingly, Nop8p mediates association of Nip7p to pre-ribosomal particles. Nop8p also interacts with the exosome subunit Rrp6p and inhibits the complex activity in vitro, suggesting that the decrease in 60S ribosomal subunit levels detected upon depletion of Nop8p may result from degradation of pre-rRNAs by the exosome. These results strongly indicate that Nop8p may control the exosome function during pre-rRNA processing.
url http://europepmc.org/articles/PMC3126838?pdf=render
work_keys_str_mv AT marciactsantos theessentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT mauriciobgoldfeder theessentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT nilsonitzanchin theessentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT carlacoliveira theessentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT marciactsantos essentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT mauriciobgoldfeder essentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT nilsonitzanchin essentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
AT carlacoliveira essentialnucleolaryeastproteinnop8pcontrolstheexosomefunctionduring60sribosomalsubunitmaturation
_version_ 1724837101193658368