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....
Main Authors: | , , , |
---|---|
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 |