ArticleNature communications2018
UPF1-like helicase grip on nucleic acids dictates processivity.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- UPF1 shuttles between nucleus and cytoplasm independently of its RNA-binding and ATPase activities.RNA (New York, N.Y.) · 2025Article
- Synergistic Methods to Investigate Eukaryotic Translation and Its Quality Control.Journal of molecular biology · 2025Review
- An anti-virulence drug targeting the evolvability protein Mfd protects against infections with antimicrobial resistant ESKAPE pathogens.Nature communications · 2025Article
- The Stalk and 1B Domains Are Required for Porcine Deltacoronavirus Helicase NSP13 to Separate the Double-Stranded Nucleic Acids, and the Deletion of the ZBD Impairs This Activity.Animals : an open access journal from MDPI · 2025Article
- RNA anchoring of Upf1 facilitates recruitment of Dcp2 in the NMD decapping complex.Nucleic acids research · 2025Article
- Article
- Annotation and functional prediction of RNA helicases inIMA fungus · 2025Review
- Expanding the genetic spectrum of hereditary motor sensory neuropathies in Pakistan.BMC neurology · 2024Article
- IGHMBP2 deletion suppresses translation and activates the integrated stress response.Life science alliance · 2024Article
- Article
- UPF1 ATPase autoinhibition and activation modulate RNA binding kinetics and NMD efficiency.Nucleic acids research · 2024Article
- Disease Mechanisms and Therapeutic Approaches in SMARD1-Insights from Animal Models and Cell Models.Biomedicines · 2024Review
- The contribution and therapeutic implications of IGHMBP2 mutations on IGHMBP2 biochemical activity and ABT1 association.Biochimica et biophysica acta. Molecular basis of disease · 2024Article
- IGHMBP2 deletion suppresses translation and activates the integrated stress response.bioRxiv : the preprint server for biology · 2023Article
- UPF1 ATPase autoinhibition and activation modulate RNA binding kinetics and NMD efficiency.bioRxiv : the preprint server for biology · 2023Article
- Identifying Potent Nonsense-Mediated mRNA Decay Inhibitors with a Novel Screening System.Biomedicines · 2023Article
- Cellular functions of eukaryotic RNA helicases and their links to human diseases.Nature reviews. Molecular cell biology · 2023Review
- HELZ2: a new, interferon-regulated, human 3'-5' exoribonuclease of the RNB family is expressed from a non-canonical initiation codon.Nucleic acids research · 2023Article
- Article
- The nexus between RNA-binding proteins and their effectors.Nature reviews. Genetics · 2023Review
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicases are molecular engines which translocate along nucleic acids (NA) to unwind double-strands or remodel NA-protein complexes. While they have an essential role in genome structure and expression, the rules dictating their processivity remain elusive. Here, we developed single-molecule methods to investigate helicase binding lifetime on DNA. We found that UPF1, a highly processive helicase central to nonsense-mediated mRNA decay (NMD), tightly holds onto NA, allowing long lasting action. Conversely, the structurally similar IGHMBP2 helicase has a short residence time. UPF1 mutants with variable grip on DNA show that grip tightness dictates helicase residence time and processivity. In addition, we discovered via functional studies that a decrease in UPF1 grip impairs NMD efficiency in vivo. Finally, we propose a three-state model with bound, sliding and unbound molecular clips, that can accurately predict the modulation of helicase processivity.
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