RNA channelling by the eukaryotic exosomeMalet, Hélène; Topf, Maya; Clare, Daniel K; Ebert, Judith; Bonneau, Fabien; Basquin, Jerome; Drazkowska, Karolina; Tomecki, Rafal; Dziembowski, Andrzej; Conti, Elena; Saibil, Helen R; Lorentzen, Esben
doi: 10.1038/embor.2010.164pmid: 21072061
The eukaryotic exosome is a key nuclease for the degradation, processing and quality control of a wide variety of RNAs. Here, we report electron microscopic reconstructions and pseudo‐atomic models of the ten‐subunit Saccharomyces cerevisiae exosome in the unbound and RNA‐bound states. In the RNA‐bound structures, extra density that is visible at the entry and exit sites of the exosome channel indicates that a substrate‐threading mechanism is used by the eukaryotic exosome. This channelling mechanism seems to be conserved in exosome‐like complexes from all domains of life, and might have been present in the most recent common ancestor.
Of switches and hourglasses: regulation of subcellular traffic in circadian clocks by phosphorylationTataroğlu, Özgür; Schafmeier, Tobias
doi: 10.1038/embor.2010.174pmid: 21052092
Investigation of the phosphorylation of circadian clock proteins has shown that this modification contributes to circadian timing in all model organisms. Phosphorylation alters the stability, transcriptional activity and subcellular localization of clock proteins during the course of a day, such that time‐of‐day‐specific phosphorylation encodes information for measuring time and is crucial for the establishment of an approximately 24‐h period. One main feature of molecular timekeeping is the daytime‐specific nuclear accumulation of clock proteins, which can be regulated by phosphorylation. Here, we discuss increasing knowledge of how subcellular shuttling is regulated in circadian clocks, on the basis of recent observations in Neurospora crassa showing that clock proteins undergo maturation through sequential phosphorylation. In this model organism, clock proteins are regulated by the phosphorylation‐dependent modulation of rapid shuttling cycles that alter their subcellular localization in a time‐of‐day‐specific manner.
Receptor for activated C kinase 1 stimulates nascent polypeptide‐dependent translation arrestKuroha, Kazushige; Akamatsu, Mayuko; Dimitrova, Lyudmila; Ito, Takehiko; Kato, Yuki; Shirahige, Katsuhiko; Inada, Toshifumi
doi: 10.1038/embor.2010.169pmid: 21072063
Nascent peptide‐dependent translation arrest is crucial for the quality control of eukaryotic gene expression. Here we show that the receptor for activated C kinase 1 (RACK1) participates in nascent peptide‐dependent translation arrest, and that its binding to the 40S subunit is crucial for this. Translation arrest by a nascent peptide results in Dom34/Hbs1‐independent endonucleolytic cleavage of mRNA, and this is stimulated by RACK1. We propose that RACK1 stimulates the translation arrest that is induced by basic amino‐acid sequences that leads to endonucleolytic cleavage of the mRNA, as well as to co‐translational protein degradation.