A conserved deubiquitinating enzyme controls cell growth by regulating RNA polymerase I stability.
Cell Rep
; 2(2): 372-85, 2012 Aug 30.
Article
em En
| MEDLINE
| ID: mdl-22902402
ABSTRACT
Eukaryotic ribosome biogenesis requires hundreds of trans-acting factors and dozens of RNAs. Although most factors required for ribosome biogenesis have been identified, little is known about their regulation. Here, we reveal that the yeast deubiquitinating enzyme Ubp10 is localized to the nucleolus and that ubp10Δ cells have reduced pre-rRNAs, mature rRNAs, and translating ribosomes. Through proteomic analyses, we found that Ubp10 interacts with proteins that function in rRNA production and ribosome biogenesis. In particular, we discovered that the largest subunit of RNA polymerase I (RNAPI) is stabilized via Ubp10-mediated deubiquitination and that this is required in order to achieve optimal levels of ribosomes and cell growth. USP36, the human ortholog of Ubp10, complements the ubp10Δ allele for RNAPI stability, pre-rRNA processing, and cell growth in yeast, suggesting that deubiquitination of RNAPI may be conserved in eukaryotes. Our work implicates Ubp10/USP36 as a key regulator of rRNA production through control of RNAPI stability.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Saccharomyces cerevisiae
/
RNA Polimerase I
/
RNA Fúngico
/
RNA Ribossômico
/
Proteínas Nucleares
/
Nucléolo Celular
/
Proteínas de Saccharomyces cerevisiae
/
Ubiquitina Tiolesterase
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Cell Rep
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Estados Unidos