ArticlePloS one2015
Endonuclease specificity and sequence dependence of type IIS restriction enzymes.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- One-pot DTECT enables rapid and efficient capture of genetic signatures for precision genome editing and clinical diagnostics.Cell reports methods · 2024Article
- miR-AB, a miRNA-based shRNA viral toolkit for multicolor-barcoded multiplex RNAi at a single-cell level.EMBO reports · 2022Article
- Detection of Marker-Free Precision Genome Editing and Genetic Variation through the Capture of Genomic Signatures.Cell reports · 2020Article
- BtsCI and BseGI display sequence preference in the nucleotides flanking the recognition sequence.PloS one · 2018Article
- Highly efficient one-step scarless protein tagging by type IIS restriction endonuclease-mediated precision cloning.Biochemical and biophysical research communications · 2017Article
- A method to convert mRNA into a gRNA library for CRISPR/Cas9 editing of any organism.Science advances · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Restriction enzymes that recognize specific sequences but cleave unknown sequence outside the recognition site are extensively utilized tools in molecular biology. Despite this, systematic functional categorization of cleavage performance has largely been lacking. We established a simple and automatable model system to assay cleavage distance variation (termed slippage) and the sequence dependence thereof. We coupled this to massively parallel sequencing in order to provide sensitive and accurate measurement. With this system 14 enzymes were assayed (AcuI, BbvI, BpmI, BpuEI, BseRI, BsgI, Eco57I, Eco57MI, EcoP15I, FauI, FokI, GsuI, MmeI and SmuI). We report significant variation of slippage ranging from 1-54%, variations in sequence context dependence, as well as variation between isoschizomers. We believe this largely overlooked property of enzymes with shifted cleavage would benefit from further large scale classification and engineering efforts seeking to improve performance. The gained insights of in-vitro performance may also aid the in-vivo understanding of these enzymes.
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Registered trials
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