ArticleNucleic acids research2024
The nuclease-associated short prokaryotic Argonaute system nonspecifically degrades DNA upon activation by target recognition.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Mechanism of the long-B prokaryotic Argonaute-mediated nuclease activation in bacterial immunity.Nucleic acids research · 2026Article
- Filament assembly induced by the recognition of target DNA activates the prokaryotic Argonaute SPARDA system.Nature communications · 2026Article
- Structure and activation mechanism of a Lamassu phage and plasmid defense system.Nature structural & molecular biology · 2025Article
- Activation of the SPARDA defense system by filament assembly using a beta-relay signaling mechanism widespread in prokaryotic Argonautes.Cell research · 2025Article
- Argonaute-HNH filaments triggered by invader DNA confer bacterial immunity.Nature communications · 2025Article
- Filament assembly powers NbaSPARDA in bacterial defense.Cell research · 2025Article
- Target DNA-induced filament formation and nuclease activation of SPARDA complex.Cell research · 2025Article
- Natronobacterium gregoryi Argonaute inhibits class 1 integron integrase-mediated excision and integration.Nucleic acids research · 2025Article
- Structural and mechanistic insights into the activation of a short prokaryotic argonaute system from archaeon Sulfolobus islandicus.Nucleic acids research · 2025Article
- Nucleic acid recognition during prokaryotic immunity.Molecular cell · 2025Review
- Identification of novel toxins associated with the extracellular contractile injection system using machine learning.Molecular systems biology · 2024Article
- Structures and functions of short argonautes.RNA biology · 2024Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Prokaryotic Argonautes (pAgos) play a vital role in host defense by utilizing short nucleic acid guides to recognize and target complementary nucleic acids. Despite being the majority of pAgos, short pAgos have only recently received attention. Short pAgos are often associated with proteins containing an APAZ domain and a nuclease domain including DUF4365, SMEK, or HNH domain. In contrast to long pAgos that specifically cleave the target DNA, our study demonstrates that the short pAgo from Thermocrispum municipal, along with its associated DUF4365-APAZ protein, forms a heterodimeric complex. Upon RNA-guided target DNA recognition, this complex is activated to nonspecifically cleave DNA. Additionally, we found that the TmuRE-Ago complex shows a preference for 5'-OH guide RNA, specifically requires a uridine nucleotide at the 5' end of the guide RNA, and is sensitive to single-nucleotide mismatches between the guide RNA and target DNA. Based on its catalytic properties, our study has established a novel nucleic acid detection method and demonstrated its feasibility. This study not only expands our understanding of the defense mechanism employed by short pAgo systems but also suggests their potential applications in nucleic acid detection.
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Registered trials
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