ArticleMolecular microbiology2013
Mutants of phage bIL67 RuvC with enhanced Holliday junction binding selectivity and resolution symmetry.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- A Combined Transcriptomic and Proteomic Analysis of Monkeypox Virus A23 Protein on HEK293T Cells.International journal of molecular sciences · 2024Article
- Crystal structure and initial characterization of a novel archaeal-like Holliday junction-resolving enzyme from Thermus thermophilus phage Tth15-6.Acta crystallographica. Section D, Structural biology · 2022Article
- Article
- Genome Characterization of Nocturne116, NovelMicroorganisms · 2021Article
- Structural insights into the promiscuous DNA binding and broad substrate selectivity of fowlpox virus resolvase.Scientific reports · 2020Article
- Viral genome packaging terminase cleaves DNA using the canonical RuvC-like two-metal catalysis mechanism.Nucleic acids research · 2017Article
- The Tomato Nucleotide-binding Leucine-rich Repeat Immune Receptor I-2 Couples DNA-binding to Nucleotide-binding Domain Nucleotide Exchange.The Journal of biological chemistry · 2016Article
- Proteomic Analysis of a Novel Bacillus Jumbo Phage Revealing Glycoside Hydrolase As Structural Component.Frontiers in microbiology · 2016Article
- The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein.The Journal of biological chemistry · 2015Article
- Crystal structure of RuvC resolvase in complex with Holliday junction substrate.Nucleic acids research · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Viral and bacterial Holliday junction resolvases differ in specificity with the former typically being more promiscuous, acting on a variety of branched DNA substrates, while the latter exclusively targets Holliday junctions. We have determined the crystal structure of a RuvC resolvase from bacteriophage bIL67 to help identify features responsible for DNA branch discrimination. Comparisons between phage and bacterial RuvC structures revealed significant differences in the number and position of positively-charged residues in the outer sides of the junction binding cleft. Substitutions were generated in phage RuvC residues implicated in branch recognition and six were found to confer defects in Holliday junction and replication fork cleavage in vivo. Two mutants, R121A and R124A that flank the DNA binding site were purified and exhibited reduced in vitro binding to fork and linear duplex substrates relative to the wild-type, while retaining the ability to bind X junctions. Crucially, these two variants cleaved Holliday junctions with enhanced specificity and symmetry, a feature more akin to cellular RuvC resolvases. Thus, additional positive charges in the phage RuvC binding site apparently stabilize productive interactions with branched structures other than the canonical Holliday junction, a feature advantageous for viral DNA processing but deleterious for their cellular counterparts.
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