Literature DB >> 17272721

The DEAD-box RNA helicase Dbp5 functions in translation termination.

Thomas Gross1, Anja Siepmann, Dorotheé Sturm, Merle Windgassen, John J Scarcelli, Matthias Seedorf, Charles N Cole, Heike Krebber.   

Abstract

In eukaryotes, termination of messenger RNA (mRNA) translation is mediated by the release factors eRF1 and eRF3. Using Saccharomyces cerevisiae as a model organism, we have identified a member of the DEAD-box protein (DBP) family, the DEAD-box RNA helicase and mRNA export factor Dbp5, as a player in translation termination. Dbp5 interacts genetically with both release factors and the polyadenlyate-binding protein Pab1. A physical interaction was specifically detected with eRF1. Moreover, we show that the helicase activity of Dbp5 is required for efficient stop-codon recognition, and intact Dbp5 is essential for recruitment of eRF3 into termination complexes. Therefore, Dbp5 controls the eRF3-eRF1 interaction and thus eRF3-mediated downstream events.

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Year:  2007        PMID: 17272721     DOI: 10.1126/science.1134641

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  80 in total

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8.  Monosome formation during translation initiation requires the serine/arginine-rich protein Npl3.

Authors:  Claudia Baierlein; Alexandra Hackmann; Thomas Gross; Lysann Henker; Frederik Hinz; Heike Krebber
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9.  Nup42 and IP6 coordinate Gle1 stimulation of Dbp5/DDX19B for mRNA export in yeast and human cells.

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Journal:  Traffic       Date:  2017-10-16       Impact factor: 6.215

10.  The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation.

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