ArticleThe Journal of biological chemistry2011
Intermolecular interactions within the abundant DEAD-box protein Dhh1 regulate its activity in vivo.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 56 citations in OpenAlex.
- Deadenylation and decapping factors cooperatively stimulate biochemical activities of DEAD-box ATPase Dhh1.Nucleic acids research · 2026Article
- Deadenylation and Decapping Factors Cooperatively Stimulate Biochemical Activities of DEAD-Box ATPase Dhh1.bioRxiv : the preprint server for biology · 2026Article
- Degradation factor 1, Def1, regulates mRNA translation and decay through Ccr4-Not-dependent ubiquitylation of the ribosome.RNA (New York, N.Y.) · 2026Article
- Degradation factor 1, Def1, regulates mRNA translation and decay through Ccr4-Not-dependent ubiquitylation of the ribosome.bioRxiv : the preprint server for biology · 2025Article
- Substrate Specificities of DDX1: A Human DEAD-Box Protein.ACS omega · 2025Article
- The ATPase activity of yeast chromosome axis protein Hop1 affects the frequency of meiotic crossovers.Nucleic acids research · 2025Article
- Characterization of BioID tagging systems in budding yeast and exploring the interactome of the Ccr4-Not complex.G3 (Bethesda, Md.) · 2024Article
- DDX6 modulates P-body and stress granule assembly, composition, and docking.The Journal of cell biology · 2024Article
- Substrate Specificities of DDX1: A Human DEAD-box protein.bioRxiv : the preprint server for biology · 2024Article
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- Quantitative reconstitution of yeast RNA processing bodies.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity.Nature communications · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Specific Interaction of DDX6 with an RNA Hairpin in the 3' UTR of the Dengue Virus Genome Mediates GJournal of virology · 2021Article
- Roles of Dhh1 RNA helicase in yeast filamentous growth: Analysis of N-terminal phosphorylation residues and ATPase domains.Journal of microbiology (Seoul, Korea) · 2020Article
- Mechanisms and Regulation of RNA Condensation in RNP Granule Formation.Trends in biochemical sciences · 2020Review
- Mutations in genes encoding regulators of mRNA decapping and translation initiation: links to intellectual disability.Biochemical Society transactions · 2020Review
- Article
- Functional association of Loc1 and Puf6 with RNA helicase Dhh1 in translational regulation of Saccharomyces cerevisiae Ste12.PloS one · 2019Article
- Genome-Wide Mapping of Decay Factor-mRNA Interactions in Yeast Identifies Nutrient-Responsive Transcripts as Targets of the Deadenylase Ccr4.G3 (Bethesda, Md.) · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Dhh1 is a highly conserved DEAD-box protein that has been implicated in many processes involved in mRNA regulation. At least some functions of Dhh1 may be carried out in cytoplasmic foci called processing bodies (P-bodies). Dhh1 was identified initially as a putative RNA helicase based solely on the presence of conserved helicase motifs found in the superfamily 2 (Sf2) of DEXD/H-box proteins. Although initial mutagenesis studies revealed that the signature DEAD-box motif is required for Dhh1 function in vivo, enzymatic (ATPase or helicase) or ATP binding activities of Dhh1 or those of any its many higher eukaryotic orthologues have not been described. Here we provide the first characterization of the biochemical activities of Dhh1. Dhh1 has weaker RNA-dependent ATPase activity than other well characterized DEAD-box helicases. We provide evidence that intermolecular interactions between the N- and C-terminal RecA-like helicase domains restrict its ATPase activity; mutation of residues mediating these interactions enhanced ATP hydrolysis. Interestingly, the interdomain interaction mutant displayed enhanced mRNA turnover, RNA binding, and recruitment into cytoplasmic foci in vivo compared with wild type Dhh1. Also, we demonstrate that the ATPase activity of Dhh1 is not required for it to be recruited into cytoplasmic foci, but it regulates its association with RNA in vivo. We hypothesize that the activity of Dhh1 is restricted by interdomain interactions, which can be regulated by cellular factors to impart stringent control over this very abundant RNA helicase.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.