ArticleNucleic acids research2015
Synergistic effects of ATP and RNA binding to human DEAD-box protein DDX1.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- Regulation of RNA-binding proteins by small biomolecules.Nature reviews. Molecular cell biology · 2026Review
- Role of DEAD/DEAH-box helicases in immunity, infection and cancers.Cell communication and signaling : CCS · 2025Review
- Substrate Specificities of DDX1: A Human DEAD-Box Protein.ACS omega · 2025Article
- Passenger Gene Coamplifications Create Collateral Therapeutic Vulnerabilities in Cancer.Cancer discovery · 2024Article
- Substrate Specificities of DDX1: A Human DEAD-box protein.bioRxiv : the preprint server for biology · 2024Article
- Identification of RNA helicases with unwinding activity on angiogenin-processed tRNAs.Nucleic acids research · 2023Article
- DDX1 vesicles control calcium-dependent mitochondrial activity in mouse embryos.Nature communications · 2022Article
- Comprehensive Analysis of Key m6A Modification Related Genes and Immune Infiltrates in Human Aortic Dissection.Frontiers in cardiovascular medicine · 2022Article
- A novel thinking: DDR axis refines the classification of ccRCC with distinctive prognosis, multi omics landscape and management strategy.Frontiers in public health · 2022Article
- DNA-guided photoactivatable probe-based chemical proteomics reveals the reader protein of mRNA methylation.iScience · 2021Article
- Specific Interaction of DDX6 with an RNA Hairpin in the 3' UTR of the Dengue Virus Genome Mediates GJournal of virology · 2021Article
- Host DDX Helicases as Possible SARS-CoV-2 Proviral Factors: A Structural Overview of Their Hijacking Through Multiple Viral Proteins.Frontiers in chemistry · 2020Review
- Expression and subcellular localization of HSPC117 in min pig tissues and the PK15 cell line.Technology and health care : official journal of the European Society for Engineering and Medicine · 2019Article
- RNA Helicase DDX1 Converts RNA G-Quadruplex Structures into R-Loops to Promote IgH Class Switch Recombination.Molecular cell · 2018Article
- The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.Nucleic acids research · 2018Article
- The DEAD-box protein DDX43 (HAGE) is a dual RNA-DNA helicase and has a K-homology domain required for full nucleic acid unwinding activity.The Journal of biological chemistry · 2017Article
- Structure of the SPRY domain of the human RNA helicase DDX1, a putative interaction platform within a DEAD-box protein.Acta crystallographica. Section F, Structural biology communications · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA helicases of the DEAD-box protein family form the largest group of helicases. The human DEAD-box protein 1 (DDX1) plays an important role in tRNA and mRNA processing, is involved in tumor progression and is also hijacked by several virus families such as HIV-1 for replication and nuclear export. Although important in many cellular processes, the mechanism of DDX1's enzymatic function is unknown. We have performed equilibrium titrations and transient kinetics to determine affinities for nucleotides and RNA. We find an exceptional tight binding of DDX1 to adenosine diphosphate (ADP), one of the strongest affinities observed for DEAD-box helicases. ADP binds tighter by three orders of magnitude when compared to adenosine triphosphate (ATP), arresting the enzyme in a potential dead-end ADP conformation under physiological conditions. We thus suggest that a nucleotide exchange factor leads to DDX1 recycling. Furthermore, we find a strong cooperativity in binding of RNA and ATP to DDX1 that is also reflected in ATP hydrolysis. We present a model in which either ATP or RNA binding alone can partially shift the equilibrium from an 'open' to a 'closed'-state; this shift appears to be not further pronounced substantially even in the presence of both RNA and ATP as the low rate of ATP hydrolysis does not change.
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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.