ArticleJournal of molecular biology2010
Sin resolvase catalytic activity and oligomerization state are tightly coupled.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Structural basis of directionality control in large serine integrases.bioRxiv : the preprint server for biology · 2025Article
- Structural basis for topological regulation of Tn3 resolvase.Nucleic acids research · 2023Article
- Snapshots of a molecular swivel in action.Nucleic acids research · 2018Article
- Single-Molecule Tethered Particle Motion: Stepwise Analyses of Site-Specific DNA Recombination.Micromachines · 2018Review
- Nicked-site substrates for a serine recombinase reveal enzyme-DNA communications and an essential tethering role of covalent enzyme-DNA linkages.Nucleic acids research · 2015Article
- Serine Resolvases.Microbiology spectrum · 2015Review
- Expanding the zinc-finger recombinase repertoire: directed evolution and mutational analysis of serine recombinase specificity determinants.Nucleic acids research · 2014Article
- A proposed mechanism for IS607-family serine transposases.Mobile DNA · 2013Article
- Arginine as a general acid catalyst in serine recombinase-mediated DNA cleavage.The Journal of biological chemistry · 2013Article
- Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase.Nucleic acids research · 2013Article
- Biophysical studies of an NAD(P)(+)-dependent aldehyde dehydrogenase from Bacillus licheniformis.European biophysics journal : EBJ · 2011Article
- Structural basis for catalytic activation of a serine recombinase.Structure (London, England : 1993) · 2011Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Serine recombinases promote specific DNA rearrangements by a cut-and-paste mechanism that involves cleavage of all four DNA strands at two sites recognized by the enzyme. Dissecting the order and timing of these cleavage events and the steps leading up to them is difficult because the cleavage reaction is readily reversible. Here, we describe assays using activated Sin mutants and a DNA substrate with a 3'-bridging phosphorothiolate modification that renders Sin-mediated DNA cleavage irreversible. We find that activating Sin mutations promote DNA cleavage rather than simply stabilize the cleavage product. Cleavage events at the scissile phosphates on complementary strands of the duplex are tightly coupled, and the overall DNA cleavage rate is strongly dependent on Sin concentration. When combined with analytical ultracentrifugation data, these results suggest that Sin catalytic activity and oligomerization state are tightly linked, and that activating mutations promote formation of a cleavage-competent oligomeric state that is normally formed only transiently within the full synaptic complex.
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Registered trials
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.