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RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes
Tatiana Mikhailova1, Ekaterina Shuvalova1, Alexander Ivanov1,2
1Engelhardt Institute of Molecular Biology, The Russian Academy of Sciences, Moscow, Russia.
Nucleic Acids Research
|February 10, 2017
Summary
The human DEAD-box RNA helicase DDX19, previously known for mRNA export, is crucial for protein biosynthesis. It actively participates in translation termination by stabilizing ribosome complexes and enhancing peptide release during stop codon recognition.
Area of Science:
- Molecular Biology
- Protein Synthesis
- RNA Biology
Background:
- The DEAD-box RNA helicase DDX19 is known to function in mRNA export.
- Its yeast homolog, Dbp5, has been implicated in translation termination.
Purpose of the Study:
- To investigate the role of human DDX19 in translation termination.
- To elucidate the mechanism by which DDX19 influences protein biosynthesis.
Main Methods:
- Reconstituted mammalian in vitro translation system.
- Analysis of DDX19 association with translating ribosomes.
- Biochemical assays to study DDX19 interaction with pre-termination complexes (preTCs) and termination complexes (TCs).
- Utilized mutant eRF1 and non-hydrolyzable GTP analogs to probe termination steps.
Main Results:
- Human DDX19 is associated with translating ribosomes and plays a role in translation termination.
- DDX19 interacts with preTCs in a nucleotide-dependent manner.
- DDX19 enhances TC formation and peptide release, acting during stop codon recognition.
- DDX19 stabilizes ribosome complexes with elongation factors eEF1 and eEF2.
Conclusions:
- Human DDX19 is an active participant in protein biosynthesis, extending beyond its known role in mRNA export.
- DDX19's function in translation termination involves stabilizing ribosome complexes and promoting efficient peptide release.
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