The DEAD-box RNA helicase Dbp5 functions in translation termination.
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.
Mesh Terms:
Codon, Terminator, DEAD-box RNA Helicases, Mutation, Nucleocytoplasmic Transport Proteins, Peptide Chain Termination, Translational, Peptide Termination Factors, Poly(A)-Binding Proteins, Polyribosomes, RNA Helicases, RNA Stability, RNA, Fungal, RNA, Messenger, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Codon, Terminator, DEAD-box RNA Helicases, Mutation, Nucleocytoplasmic Transport Proteins, Peptide Chain Termination, Translational, Peptide Termination Factors, Poly(A)-Binding Proteins, Polyribosomes, RNA Helicases, RNA Stability, RNA, Fungal, RNA, Messenger, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Science
Date: Feb. 02, 2007
PubMed ID: 17272721
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