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Science 2 February 2007:
Vol. 315. no. 5812, pp. 646 - 649
DOI: 10.1126/science.1134641
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Reports

The DEAD-Box RNA Helicase Dbp5 Functions in Translation Termination

Thomas Gross,1 Anja Siepmann,1 Dorotheé Sturm,1 Merle Windgassen,1* John J. Scarcelli,2 Matthias Seedorf,3 Charles N. Cole,2 Heike Krebber1{dagger}

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.

1 Institut für Molekularbiologie und Tumorforschung der Philipps-Universität Marburg, Emil-Mannkopff-Strasse 2, 35037 Marburg, Germany.
2 Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
3 Zentrum für Molekulare Biologie der Universität in Heidelberg, Im Neuenheimer Feld 282, 69129 Heidelberg, Germany.

* Present address: Medical Biotechnology Center (MBC) of the University of Southern Denmark, Winsløwparken 25, 5000 Odense C, Denmark.

{dagger} To whom correspondence should be addressed. E-mail: krebber{at}imt.uni-marburg.de

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