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Title: 40S subunit dissociation and proteasome-dependent RNA degradation in nonfunctional 25S rRNA decay.
Authors: Fujii, Kotaro
Kitabatake, Makoto  kyouindb  KAKEN_id
Sakata, Tomoko
Ohno, Mutsuhito  kyouindb  KAKEN_id
Author's alias: 北畠, 真
Keywords: quality control
Issue Date: 30-May-2012
Publisher: Nature Publishing Group
Journal title: The EMBO journal
Volume: 31
Issue: 11
Start page: 2579
End page: 2589
Abstract: Eukaryotic cells have quality control systems that eliminate nonfunctional rRNAs with deleterious mutations (nonfunctional rRNA decay, NRD). We have previously reported that 25S NRD requires an E3 ubiquitin ligase complex, which is involved in ribosomal ubiquitination. However, the degradation process of nonfunctional ribosomes has remained unknown. Here, using genetic screening, we identified two ubiquitin-binding complexes, the Cdc48-Npl4-Ufd1 complex (Cdc48 complex) and the proteasome, as the factors involved in 25S NRD. We show that the nonfunctional 60S subunit is dissociated from the 40S subunit in a Cdc48 complex-dependent manner, before it is attacked by the proteasome. When we examined the nonfunctional 60S subunits that accumulated under proteasome-depleted conditions, the majority of mutant 25S rRNAs retained their full length at a single-nucleotide resolution. This indicates that the proteasome is an essential factor triggering rRNA degradation. We further showed that ribosomal ubiquitination can be stimulated solely by the suppression of the proteasome, suggesting that ubiquitin-proteasome-dependent RNA degradation occurs in broader situations, including in general rRNA turnover.
Rights: © 2012 European Molecular Biology Organization.
This is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
DOI(Published Version): 10.1038/emboj.2012.85
PubMed ID: 22505030
Appears in Collections:Journal Articles

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