ArticlemBio2023
Watson-Crick Base-Pairing Requirements for ssDNA Recognition and Processing in Replication-Initiating HUH Endonucleases.
Article in mBio, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Homogeneous Antibody-DNA Conjugates Using Unmodified Oligonucleotides and Photo-Cross-Linkable Protein G-HUH Endonuclease Fusion Proteins.Bioconjugate chemistry · 2026Article
- Molecular Characterization of Helicase and Nuclease Domains in PPV5 NS1 from Mexican Full-Length Sequence.Viruses · 2026Article
- Sequence-directed covalent protein-RNA linkages in a single step using engineered HUH-tags.Nucleic acids research · 2026Article
- Structures of nucleotide-bound Redondovirus Rep protein link conformation and function.PLoS pathogens · 2026Article
- Identification of novel CRESS-DNA viruses in the human vaginal microbiome.Frontiers in microbiology · 2026Article
- Reversible Sandwich-Based Particle Nanoswitch for Continuous Protein Monitoring at Picomolar Concentrations with Automated Calibration.Angewandte Chemie (International ed. in English) · 2025Article
- Identification and biochemical characterization of a novel porcine circovirus associated with porcine respiratory and diarrheal diseases.Microbiology spectrum · 2025Article
- Click editing enables programmable genome writing using DNA polymerases and HUH endonucleases.Nature biotechnology · 2025Article
- HUHgle: An Interactive Substrate Design Tool for Covalent Protein-ssDNA Labeling Using HUH-Tags.ACS synthetic biology · 2024Article
- Multiparametric domain insertional profiling of adeno-associated virus VP1.Molecular therapy. Methods & clinical development · 2023Article
- The crystal structure of the human smacovirus 1 Rep domain.Acta crystallographica. Section F, Structural biology communications · 2023Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Replication-initiating HUH endonucleases (Reps) are sequence-specific nucleases that cleave and rejoin single-stranded DNA (ssDNA) during rolling-circle replication. These functions are mediated by covalent linkage of the Rep to its substrate post cleavage. Here, we describe the structures of the endonuclease domain from the Muscovy duck circovirus Rep in complex with its cognate ssDNA 10-mer with and without manganese in the active site. Structural and functional analyses demonstrate that divalent cations play both catalytic and structural roles in Reps by polarizing and positioning their substrate. Further structural comparisons highlight the importance of an intramolecular substrate Watson-Crick (WC) base pairing between the -4 and +1 positions. Subsequent kinetic and functional analyses demonstrate a functional dependency on WC base pairing between these positions regardless of the pair's identity (i.e., A·T, T·A, G·C, or C·G), highlighting a structural specificity for substrate interaction. Finally, considering how well WC swaps were tolerated
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