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